ID THRB_HUMAN Reviewed; 622 AA. AC P00734; B2R7F7; B4E1A7; Q4QZ40; Q53H04; Q53H06; Q69EZ7; Q7Z7P3; Q9UCA1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 27-MAR-2024, entry version 280. DE RecName: Full=Prothrombin; DE EC=3.4.21.5; DE AltName: Full=Coagulation factor II; DE Contains: DE RecName: Full=Activation peptide fragment 1; DE Contains: DE RecName: Full=Activation peptide fragment 2; DE Contains: DE RecName: Full=Thrombin light chain; DE Contains: DE RecName: Full=Thrombin heavy chain; DE Flags: Precursor; GN Name=F2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2825773; DOI=10.1021/bi00393a033; RA Degen S.J.F., Davie E.W.; RT "Nucleotide sequence of the gene for human prothrombin."; RL Biochemistry 26:6165-6177(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT FA2D GLY-72. RC TISSUE=Blood; RX PubMed=14962227; DOI=10.1046/j.1365-2516.2003.00838.x; RA Wang W., Fu Q., Zhou R., Wu W., Ding Q., Hu Y., Wang X., Wang H., Wang Z.; RT "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 RT by Gly."; RL Haemophilia 10:94-97(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-165. RC TISSUE=Liver, and Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-165. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-622, AND GAMMA-CARBOXYGLUTAMATION AT RP GLU-49; GLU-50; GLU-57; GLU-59; GLU-62; GLU-63; GLU-68; GLU-69; GLU-72 AND RP GLU-75. RX PubMed=6305407; DOI=10.1021/bi00278a008; RA Degen S.J.F., McGillivray R.T.A., Davie E.W.; RT "Characterization of the complementary deoxyribonucleic acid and gene RT coding for human prothrombin."; RL Biochemistry 22:2087-2097(1983). RN [8] RP PROTEIN SEQUENCE OF 44-64. RC TISSUE=Urine; RX PubMed=8073540; DOI=10.1007/bf00431548; RA Suzuki K., Moriyama M., Nakajima C., Kawamura K., Miyazawa K., Tsugawa R., RA Kikuchi N., Nagata K.; RT "Isolation and partial characterization of crystal matrix protein as a RT potent inhibitor of calcium oxalate crystal aggregation: evidence of RT activation peptide of human prothrombin."; RL Urol. Res. 22:45-50(1994). RN [9] RP PROTEIN SEQUENCE OF 44-314. RX PubMed=266717; DOI=10.1073/pnas.74.5.1969; RA Walz D.A., Hewett-Emmett D., Seegers W.H.; RT "Amino acid sequence of human prothrombin fragments 1 and 2."; RL Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977). RN [10] RP PROTEIN SEQUENCE OF 315-622, GLYCOSYLATION AT ASN-416, AND VARIANT GLN-532. RX PubMed=873923; DOI=10.1016/s0021-9258(17)40144-x; RA Butkowski R.J., Elion J., Downing M.R., Mann K.G.; RT "Primary structure of human prethrombin 2 and alpha-thrombin."; RL J. Biol. Chem. 252:4942-4957(1977). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 364-622. RA Gruber A., Hanson S.R., DiCera E.; RT "Antithrombotic thrombin variants."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5. RX PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583; RA Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.; RT "Mechanism of inhibition of activated protein C by protein C inhibitor."; RL J. Biochem. 95:187-195(1984). RN [13] RP PROTEOLYTIC PROCESSING, AND GAMMA-CARBOXYGLUTAMATION AT GLU-49 AND GLU-50. RX PubMed=3759958; DOI=10.1016/s0021-9258(18)69292-0; RA Rabiet M.J., Blashill A., Furie B., Furie B.C.; RT "Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation RT in human plasma."; RL J. Biol. Chem. 261:13210-13215(1986). RN [14] RP FUNCTION, AND CHARACTERIZATION. RX PubMed=2856554; RA Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.; RT "Synthetic peptides bind to high-affinity thrombin receptors and modulate RT thrombin mitogenesis."; RL Pept. Res. 1:65-73(1988). RN [15] RP INTERACTION WITH ALPHA-1-MICROGLOBULIN. RX PubMed=9183005; DOI=10.1111/j.1432-1033.1997.00676.x; RA Berggaard T., Thelin N., Falkenberg C., Enghild J.J., Akerstroem B.; RT "Prothrombin, albumin and immunoglobulin A form covalent complexes with RT alpha1-microglobulin in human plasma."; RL Eur. J. Biochem. 245:676-683(1997). RN [16] RP INVOLVEMENT IN RPRGL2 SUSCEPTIBILITY. RX PubMed=11506076; DOI=10.1111/j.8755-8920.2001.460202.x; RA Pihusch R., Buchholz T., Lohse P., Rubsamen H., Rogenhofer N., RA Hasbargen U., Hiller E., Thaler C.J.; RT "Thrombophilic gene mutations and recurrent spontaneous abortion: RT prothrombin mutation increases the risk in the first trimester."; RL Am. J. Reprod. Immunol. 46:124-131(2001). RN [17] RP INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR. RX PubMed=15534175; DOI=10.1001/archneur.61.11.1652; RA Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.; RT "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes RT involving approximately 18,000 cases and 58,000 controls."; RL Arch. Neurol. 61:1652-1661(2004). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [19] RP CHARACTERIZATION OF THE TP508 PEPTIDE. RX PubMed=15885491; DOI=10.1016/j.orthres.2004.12.005; RA Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.; RT "rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce RT chemotaxis of human osteoblasts and microvascular endothelial cells."; RL J. Orthop. Res. 23:680-685(2005). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [21] RP THERAPEUTIC USAGE OF THE TP508 PEPTIDE. RX PubMed=17244316; DOI=10.1111/j.1524-475x.2006.00181.x; RA Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A., RA Zwernemann A., Ryaby J.T., Carney D.H.; RT "Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a RT placebo-controlled phase I/II study."; RL Wound Repair Regen. 15:23-34(2007). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [23] RP GLYCOSYLATION AT ASN-416. RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [24] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, AND STRUCTURE OF RP CARBOHYDRATE. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., RA Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [25] RP GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [27] RP PROTHROMBIN ACTIVATION, AND MUTAGENESIS OF ARG-314; ARG-363 AND SER-568. RX PubMed=34265300; DOI=10.1016/j.jbc.2021.100955; RA Stojanovski B.M., Di Cera E.; RT "Role of sequence and position of the cleavage sites in prothrombin RT activation."; RL J. Biol. Chem. 297:100955-100955(2021). RN [28] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=2583108; DOI=10.1002/j.1460-2075.1989.tb08511.x; RA Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.; RT "The refined 1.9 A crystal structure of human alpha-thrombin: interaction RT with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro- RT Trp insertion segment."; RL EMBO J. 8:3467-3475(1989). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN. RX PubMed=2369893; DOI=10.1002/j.1460-2075.1990.tb07410.x; RA Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W., RA Hofsteenge J., Stone S.R.; RT "Crystal structure of the thrombin-hirudin complex: a novel mode of serine RT protease inhibition."; RL EMBO J. 9:2361-2365(1990). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN. RX PubMed=2374926; DOI=10.1126/science.2374926; RA Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., RA Fenton J.W. II; RT "The structure of a complex of recombinant hirudin and human alpha- RT thrombin."; RL Science 249:277-280(1990). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN RP AND SYNTHETIC INHIBITOR. RX PubMed=8251938; DOI=10.1002/pro.5560021009; RA Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.; RT "Changes in interactions in complexes of hirudin derivatives and human RT alpha-thrombin due to different crystal forms."; RL Protein Sci. 2:1630-1642(1993). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8071320; DOI=10.1016/s0021-9258(17)31746-5; RA Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D., RA Correa P.E., Fenton J.W. II, Tulinsky A.; RT "Crystallographic structure of human gamma-thrombin."; RL J. Biol. Chem. 269:22000-22006(1994). RN [33] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=9214615; DOI=10.1093/emboj/16.11.2977; RA van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R., RA Esmon C.T., Stubbs M.T.; RT "The thrombin E192Q-BPTI complex reveals gross structural rearrangements: RT implications for the interaction with antithrombin and thrombomodulin."; RL EMBO J. 16:2977-2984(1997). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601. RX PubMed=10051558; DOI=10.1073/pnas.96.5.1852; RA Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E.; RT "Unexpected crucial role of residue 225 in serine proteases."; RL Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC RP INHIBITOR. RX PubMed=11493008; DOI=10.1006/jmbi.2001.4872; RA Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F., RA Hudson H.R., Kakkar V.V., Deadman J.J.; RT "Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds RT via a metastable pentacoordinated phosphorus intermediate."; RL J. Mol. Biol. 311:549-555(2001). RN [36] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN RP AND SYNTHETIC INHIBITOR. RX PubMed=16763681; DOI=10.1039/b602585d; RA Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U., RA Wagner B., Kansy M., Banner D.W., Diederich F.; RT "Multipolar interactions in the D pocket of thrombin: large differences RT between tricyclic imide and lactam inhibitors."; RL Org. Biomol. Chem. 4:2364-2375(2006). RN [37] RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN. RX PubMed=17685615; DOI=10.1021/ja0735002; RA Liu C.C., Brustad E., Liu W., Schultz P.G.; RT "Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin."; RL J. Am. Chem. Soc. 129:10648-10649(2007). RN [38] RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC RP INHIBITOR. RX PubMed=18291642; DOI=10.1016/j.bmcl.2008.01.098; RA Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M., RA McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y., RA Lynch J.J., Lyle E.A.; RT "Structure-based design of novel groups for use in the P1 position of RT thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles."; RL Bioorg. Med. Chem. Lett. 18:2062-2066(2008). RN [39] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 RP AND HEPARIN. RX PubMed=18362344; DOI=10.1073/pnas.0711055105; RA Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.; RT "Molecular basis of thrombin recognition by protein C inhibitor revealed by RT the 1.6-A structure of the heparin-bridged complex."; RL Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008). RN [40] RP VARIANT FA2D LYS-200, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=6405779; DOI=10.1111/j.1365-2141.1983.tb02092.x; RA Board P.G., Shaw D.C.; RT "Determination of the amino acid substitution in human prothrombin type 3 RT (157 Glu leads to Lys) and the localization of a third thrombin cleavage RT site."; RL Br. J. Haematol. 54:245-254(1983). RN [41] RP VARIANT FA2D CYS-314, AND PROTEIN SEQUENCE OF 310-327. RX PubMed=3771562; DOI=10.1016/s0021-9258(18)66826-7; RA Rabiet M.-J., Furie B.C., Furie B.; RT "Molecular defect of prothrombin Barcelona. Substitution of cysteine for RT arginine at residue 273."; RL J. Biol. Chem. 261:15045-15048(1986). RN [42] RP VARIANT FA2D TRP-461, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=3567158; DOI=10.1021/bi00378a020; RA Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A., Iwanaga S.; RT "Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that RT impairs the fibrinogen clotting activity of derived thrombin Tokushima."; RL Biochemistry 26:1117-1122(1987). RN [43] RP VARIANT FA2D TRP-461. RX PubMed=3801671; RA Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S., Miyoshi K., RA Morita T., Iwanaga S.; RT "Prothrombin Tokushima: characterization of dysfunctional thrombin derived RT from a variant of human prothrombin."; RL Blood 69:565-569(1987). RN [44] RP VARIANT FA2D CYS-425, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=3242619; DOI=10.1021/bi00426a013; RA Henriksen R.A., Mann K.G.; RT "Identification of the primary structural defect in the dysthrombin RT thrombin Quick I: substitution of cysteine for arginine-382."; RL Biochemistry 27:9160-9165(1988). RN [45] RP VARIANT FA2D VAL-601, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2719946; DOI=10.1021/bi00431a017; RA Henriksen R.A., Mann K.G.; RT "Substitution of valine for glycine-558 in the congenital dysthrombin RT thrombin Quick II alters primary substrate specificity."; RL Biochemistry 28:2078-2082(1989). RN [46] RP VARIANT FA2D ALA-509, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1354985; DOI=10.1021/bi00148a005; RA Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C., Iwanaga S.; RT "Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces RT the fibrinogen clotting activity and the esterase activity."; RL Biochemistry 31:7457-7462(1992). RN [47] RP VARIANTS FA2D THR-380 AND HIS-431. RX PubMed=1421398; RA Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T., RA Yamaguchi K.; RT "Prothrombin Himi: a compound heterozygote for two dysfunctional RT prothrombin molecules (Met-337-->Thr and Arg-388-->His)."; RL Blood 80:2275-2280(1992). RN [48] RP VARIANT FA2D TRP-461. RX PubMed=1349838; RA Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S., Itakura M.; RT "Detection of a single base substitution of the gene for prothrombin RT Tokushima. The application of PCR-SSCP for the genetic and molecular RT analysis of dysprothrombinemia."; RL Int. J. Hematol. 55:93-100(1992). RN [49] RP VARIANT FA2D HIS-314. RX PubMed=7865694; DOI=10.1097/00001721-199410000-00025; RA James H.L., Kim D.J., Zheng D.-Q., Girolami A.; RT "Prothrombin Padua I: incomplete activation due to an amino acid RT substitution at a factor Xa cleavage site."; RL Blood Coagul. Fibrinolysis 5:841-844(1994). RN [50] RP VARIANT FA2D ALA-509. RX PubMed=7792730; RA Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I.; RT "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by RT substitution of Glu-466 by Ala."; RL Thromb. Haemost. 73:203-209(1995). RN [51] RP VARIANTS MET-165 AND THR-386. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [52] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [53] RP VARIANTS MET-165; LYS-200; THR-386 AND GLN-532, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=22028381; DOI=10.1093/jmcb/mjr024; RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., RA Zeng R., Wu J.R.; RT "Quantitative detection of single amino acid polymorphisms by targeted RT proteomics."; RL J. Mol. Cell Biol. 3:309-315(2011). CC -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts CC fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in CC complex with thrombomodulin, protein C. Functions in blood homeostasis, CC inflammation and wound healing. {ECO:0000269|PubMed:2856554}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form CC fibrin and release fibrinopeptides A and B.; EC=3.4.21.5; CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. CC {ECO:0000269|PubMed:6323392}. CC -!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy CC chain; disulfide-linked. Forms a heterodimer with SERPINA5. In plasma, CC interacts (via N-terminus) with alpha-1-microglobulin with molar ratio CC 1:2 and 1:1; this interaction does not prevent the activation of CC prothrombin to thrombin. {ECO:0000269|PubMed:11493008, CC ECO:0000269|PubMed:16763681, ECO:0000269|PubMed:17685615, CC ECO:0000269|PubMed:18291642, ECO:0000269|PubMed:18362344, CC ECO:0000269|PubMed:2369893, ECO:0000269|PubMed:2374926, CC ECO:0000269|PubMed:9183005}. CC -!- INTERACTION: CC P00734; P05067: APP; NbExp=3; IntAct=EBI-297094, EBI-77613; CC P00734; P07204: THBD; NbExp=4; IntAct=EBI-297094, EBI-941422; CC P00734; Q846V4; Xeno; NbExp=5; IntAct=EBI-297094, EBI-989571; CC PRO_0000028160; PRO_0000032489 [P01008]: SERPINC1; NbExp=2; IntAct=EBI-26959170, EBI-26959093; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, CC result from the carboxylation of glutamyl residues by a microsomal CC enzyme, the vitamin K-dependent carboxylase. The modified residues are CC necessary for the calcium-dependent interaction with a negatively CC charged phospholipid surface, which is essential for the conversion of CC prothrombin to thrombin. {ECO:0000269|PubMed:3759958, CC ECO:0000269|PubMed:6305407}. CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 CC (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: CC Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). CC {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, CC ECO:0000269|PubMed:873923}. CC -!- PTM: In the penultimate step of the coagulation cascade, prothrombin is CC converted to thrombin by the prothrombinase complex composed of factor CC Xa (F10), cofactor Va (F5), and phospholipids. This activation requires CC factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg- CC 363, along 2 possible pathways. In the first pathway, the first CC cleavage occurs at Arg-314, leading to the formation of the inactive CC intermediate prethrombin-2. This pathway preferentially occurs on CC platelets and in the absence of cofactor Va. In the second pathway, the CC first cleavage occurs at Arg-363, which separates protease domain into CC 2 chains that remain connected through a disulfide bond and generates CC the active intermediate meizothrombin. The presence of cofactor Va CC directs activation along the meizothrombin pathway and greatly CC accelerates the rate of cleavage at Arg-363, but has a smaller effect CC on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates CC as an intermediate when prothrombinase is assembled on the membrane of CC red blood cells. {ECO:0000305|PubMed:34265300}. CC -!- DISEASE: Factor II deficiency (FA2D) [MIM:613679]: A very rare blood CC coagulation disorder characterized by mucocutaneous bleeding symptoms. CC The severity of the bleeding manifestations correlates with blood CC factor II levels. {ECO:0000269|PubMed:1349838, CC ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398, CC ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946, CC ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158, CC ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671, CC ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730, CC ECO:0000269|PubMed:7865694}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute CC neurologic event leading to death of neural tissue of the brain and CC resulting in loss of motor, sensory and/or cognitive function. Ischemic CC strokes, resulting from vascular occlusion, is considered to be a CC highly complex disease consisting of a group of heterogeneous disorders CC with multiple genetic and environmental risk factors. CC {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- DISEASE: Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A CC multifactorial disorder of hemostasis characterized by abnormal CC platelet aggregation in response to various agents and recurrent CC thrombi formation. {ECO:0000269|PubMed:2825773}. Note=The disease is CC caused by variants affecting the gene represented in this entry. A CC common genetic variation in the 3-prime untranslated region of the CC prothrombin gene is associated with elevated plasma prothrombin levels CC and an increased risk of venous thrombosis. CC -!- DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A common CC complication of pregnancy, resulting in spontaneous abortion before the CC fetus has reached viability. The term includes all miscarriages from CC the time of conception until 24 weeks of gestation. Recurrent pregnancy CC loss is defined as 3 or more consecutive spontaneous abortions. CC {ECO:0000269|PubMed:11506076}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- PHARMACEUTICAL: The peptide TP508 also known as Chrysalin (Orthologic) CC could be used to accelerate repair of both soft and hard tissues. CC -!- MISCELLANEOUS: It is not known whether 1 or 2 smaller activation CC peptides, with additional cleavage after Arg-314, are released in CC natural blood clotting. CC -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment CC (fragment 1) of the prothrombin, prior to its activation by factor Xa. CC -!- MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does not CC occur in plasma. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry; CC URL="https://en.wikipedia.org/wiki/Thrombin"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/f2/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M17262; AAC63054.1; -; Genomic_DNA. DR EMBL; AJ972449; CAJ01369.1; -; mRNA. DR EMBL; AK303747; BAG64719.1; -; mRNA. DR EMBL; AK312965; BAG35804.1; -; mRNA. DR EMBL; AK222775; BAD96495.1; -; mRNA. DR EMBL; AK222777; BAD96497.1; -; mRNA. DR EMBL; AF478696; AAL77436.1; -; Genomic_DNA. DR EMBL; BC051332; AAH51332.1; -; mRNA. DR EMBL; V00595; CAA23842.1; -; mRNA. DR EMBL; AY344794; AAR08143.1; -; mRNA. DR CCDS; CCDS31476.1; -. DR PIR; A29351; TBHU. DR RefSeq; NP_000497.1; NM_000506.4. DR RefSeq; NP_001298186.1; NM_001311257.1. DR PDB; 1A2C; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 1A3B; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 1A3E; X-ray; 1.85 A; H=364-622, L=328-363. DR PDB; 1A46; X-ray; 2.12 A; H=364-622, L=328-363. DR PDB; 1A4W; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 1A5G; X-ray; 2.06 A; H=364-622, L=328-363. DR PDB; 1A61; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 1ABI; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1ABJ; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 1AD8; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1AE8; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1AFE; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1AHT; X-ray; 1.60 A; H=364-622, L=328-363. DR PDB; 1AI8; X-ray; 1.85 A; H=364-622, L=328-363. DR PDB; 1AIX; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 1AWF; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 1AWH; X-ray; 3.00 A; A/C=328-363, B/D=364-622. DR PDB; 1AY6; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 1B5G; X-ray; 2.07 A; H=364-622, L=328-363. DR PDB; 1B7X; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 1BA8; X-ray; 1.80 A; A=328-363, B=364-622. DR PDB; 1BB0; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 1BCU; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1BHX; X-ray; 2.30 A; A=331-349, B=364-510, F=518-622. DR PDB; 1BMM; X-ray; 2.60 A; H=364-622, L=328-363. DR PDB; 1BMN; X-ray; 2.80 A; H=364-622, L=328-363. DR PDB; 1BTH; X-ray; 2.30 A; H/K=364-622, J/L=328-363. DR PDB; 1C1U; X-ray; 1.75 A; H=364-616, L=328-363. DR PDB; 1C1V; X-ray; 1.98 A; H=364-616, L=328-363. DR PDB; 1C1W; X-ray; 1.90 A; H=364-616, L=328-363. DR PDB; 1C4U; X-ray; 2.10 A; 1=328-363, 2=364-622. DR PDB; 1C4V; X-ray; 2.10 A; 1=328-363, 2=364-622. DR PDB; 1C4Y; X-ray; 2.70 A; 1=328-363, 2=364-622. DR PDB; 1C5L; X-ray; 1.47 A; H=364-622, L=328-363. DR PDB; 1C5N; X-ray; 1.50 A; H=364-622, L=328-363. DR PDB; 1C5O; X-ray; 1.90 A; H=364-622, L=328-363. DR PDB; 1CA8; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 1D3D; X-ray; 2.04 A; A=333-360, B=364-620. DR PDB; 1D3P; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 1D3Q; X-ray; 2.90 A; A=328-363, B=364-622. DR PDB; 1D3T; X-ray; 3.00 A; A=328-363, B=364-622. DR PDB; 1D4P; X-ray; 2.07 A; A=328-363, B=364-622. DR PDB; 1D6W; X-ray; 2.00 A; A=334-620. DR PDB; 1D9I; X-ray; 2.30 A; A=334-621. DR PDB; 1DE7; X-ray; 2.00 A; H/K=364-619, J/L=328-360. DR PDB; 1DIT; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1DM4; X-ray; 2.50 A; A=328-362, B=363-622. DR PDB; 1DOJ; X-ray; 1.70 A; A=328-622. DR PDB; 1DWB; X-ray; 3.16 A; H=364-622, L=328-363. DR PDB; 1DWC; X-ray; 3.00 A; H=364-622, L=328-363. DR PDB; 1DWD; X-ray; 3.00 A; H=364-622, L=328-363. DR PDB; 1DWE; X-ray; 3.00 A; H=364-622, L=328-363. DR PDB; 1DX5; X-ray; 2.30 A; A/B/C/D=328-363, M/N/O/P=364-622. DR PDB; 1E0F; X-ray; 3.10 A; A/B/C=328-363, D/E/F=364-622. DR PDB; 1EB1; X-ray; 1.80 A; H=364-620, L=334-360. DR PDB; 1EOJ; X-ray; 2.10 A; A=332-620. DR PDB; 1EOL; X-ray; 2.10 A; A=332-620. DR PDB; 1FPC; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1FPH; X-ray; 2.50 A; H=364-622, L=328-363. DR PDB; 1G30; X-ray; 2.00 A; A=328-363, B=364-622. DR PDB; 1G32; X-ray; 1.90 A; A=328-363, B=364-622. DR PDB; 1G37; X-ray; 2.00 A; A=334-620. DR PDB; 1GHV; X-ray; 1.85 A; H=364-620, L=328-363. DR PDB; 1GHW; X-ray; 1.75 A; H=364-620, L=328-363. DR PDB; 1GHX; X-ray; 1.65 A; H=364-620, L=328-363. DR PDB; 1GHY; X-ray; 1.85 A; H=364-620, L=328-363. DR PDB; 1GJ4; X-ray; 1.81 A; H=364-621, L=328-363. DR PDB; 1GJ5; X-ray; 1.73 A; H=364-621, L=328-363. DR PDB; 1H8D; X-ray; 1.40 A; H=364-621, L=333-360. DR PDB; 1H8I; X-ray; 1.75 A; H=364-622, L=334-360. DR PDB; 1HAG; X-ray; 2.00 A; E=328-622. DR PDB; 1HAH; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1HAI; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 1HAO; X-ray; 2.80 A; H=364-622, L=328-363. DR PDB; 1HAP; X-ray; 2.80 A; H=364-622, L=328-360. DR PDB; 1HBT; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1HDT; X-ray; 2.60 A; H=364-622, L=331-363. DR PDB; 1HGT; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 1HLT; X-ray; 3.00 A; H/K=364-622, J/L=334-349. DR PDB; 1HUT; X-ray; 2.90 A; H=364-622, L=328-363. DR PDB; 1HXE; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 1HXF; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 1IHS; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1IHT; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 1JMO; X-ray; 2.20 A; H=363-622, L=315-362. DR PDB; 1JOU; X-ray; 1.80 A; A/C/E=315-363, B/D/F=364-622. DR PDB; 1JWT; X-ray; 2.50 A; A=328-622. DR PDB; 1K21; X-ray; 1.86 A; H=364-622, L=328-363. DR PDB; 1K22; X-ray; 1.93 A; H=364-622, L=328-363. DR PDB; 1KTS; X-ray; 2.40 A; A=328-363, B=364-622. DR PDB; 1KTT; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 1LHC; X-ray; 1.95 A; H=364-622, L=328-363. DR PDB; 1LHD; X-ray; 2.35 A; H=364-622, L=328-363. DR PDB; 1LHE; X-ray; 2.25 A; H=364-622, L=328-363. DR PDB; 1LHF; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 1LHG; X-ray; 2.25 A; H=364-622, L=328-363. DR PDB; 1MH0; X-ray; 2.80 A; A/B=334-620. DR PDB; 1MU6; X-ray; 1.99 A; A=328-363, B=364-622. DR PDB; 1MU8; X-ray; 2.00 A; A=328-363, B=364-622. DR PDB; 1MUE; X-ray; 2.00 A; A=328-363, B=364-622. DR PDB; 1NM6; X-ray; 1.80 A; A=335-621. DR PDB; 1NO9; X-ray; 1.90 A; H=364-622, L=328-363. DR PDB; 1NRN; X-ray; 3.10 A; H=364-622, L=328-363. DR PDB; 1NRO; X-ray; 3.10 A; H=364-622, L=328-363. DR PDB; 1NRP; X-ray; 3.00 A; H=364-622, L=328-363. DR PDB; 1NRQ; X-ray; 3.50 A; H=364-622, L=328-363. DR PDB; 1NRR; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 1NRS; X-ray; 2.40 A; H=364-622, L=328-349. DR PDB; 1NT1; X-ray; 2.00 A; A=335-621. DR PDB; 1NU7; X-ray; 2.20 A; A/E=332-359, B/F=364-622. DR PDB; 1NU9; X-ray; 2.20 A; A/D=332-622. DR PDB; 1NY2; X-ray; 2.30 A; 1=328-363, 2=364-622. DR PDB; 1NZQ; X-ray; 2.18 A; H=364-620, L=328-361. DR PDB; 1O0D; X-ray; 2.44 A; H=364-622, L=328-363. DR PDB; 1O2G; X-ray; 1.58 A; H=364-622, L=328-363. DR PDB; 1O5G; X-ray; 1.75 A; H=364-622, L=328-363. DR PDB; 1OOK; X-ray; 2.30 A; A=328-363, B=364-622. DR PDB; 1OYT; X-ray; 1.67 A; H=364-622, L=328-363. DR PDB; 1P8V; X-ray; 2.60 A; B=333-361, C=364-621. DR PDB; 1PPB; X-ray; 1.92 A; H=364-622, L=328-363. DR PDB; 1QBV; X-ray; 1.80 A; H=364-622, L=328-359. DR PDB; 1QHR; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 1QJ1; X-ray; 2.00 A; A=328-363, B=364-622. DR PDB; 1QJ6; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 1QJ7; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 1QUR; X-ray; 2.00 A; H=364-620, L=334-360. DR PDB; 1RD3; X-ray; 2.50 A; A/C=328-363, B/D=364-622. DR PDB; 1RIW; X-ray; 2.04 A; A=328-363, B=364-510, C=518-622. DR PDB; 1SB1; X-ray; 1.90 A; H=364-621, L=333-361. DR PDB; 1SFQ; X-ray; 1.91 A; A/D=328-363, B/E=364-622. DR PDB; 1SG8; X-ray; 2.30 A; A/D=328-363, B/E=364-622. DR PDB; 1SGI; X-ray; 2.30 A; A/D=328-363, B/E=364-622. DR PDB; 1SHH; X-ray; 1.55 A; A/D=328-363, B/E=364-622. DR PDB; 1SL3; X-ray; 1.81 A; A=335-621. DR PDB; 1SR5; X-ray; 3.10 A; B=328-363, C=364-622. DR PDB; 1T4U; X-ray; 2.00 A; H=364-622, L=334-359. DR PDB; 1T4V; X-ray; 2.00 A; H=364-622, L=334-359. DR PDB; 1TA2; X-ray; 2.30 A; A=335-621. DR PDB; 1TA6; X-ray; 1.90 A; A=335-621. DR PDB; 1TB6; X-ray; 2.50 A; H=364-622, L=315-363. DR PDB; 1TBZ; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1THP; X-ray; 2.10 A; A=328-362, B=364-620. DR PDB; 1THR; X-ray; 2.30 A; H=364-622, L=328-349. DR PDB; 1THS; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 1TMB; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 1TMT; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 1TMU; X-ray; 2.50 A; H=364-620, L=333-349. DR PDB; 1TOM; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 1TQ0; X-ray; 2.80 A; A/C=333-363, B/D=364-620. DR PDB; 1TQ7; X-ray; 2.40 A; A=320-363, B=364-620. DR PDB; 1TWX; X-ray; 2.40 A; A=334-349, B=364-622. DR PDB; 1UMA; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 1UVS; X-ray; 2.80 A; H=364-622, L=328-363. DR PDB; 1VR1; X-ray; 1.90 A; H=364-620, L=334-360. DR PDB; 1VZQ; X-ray; 1.54 A; H=364-620, L=334-360. DR PDB; 1W7G; X-ray; 1.65 A; H=364-622, L=328-363. DR PDB; 1WAY; X-ray; 2.02 A; A=328-363, B=364-622. DR PDB; 1WBG; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 1XM1; X-ray; 2.30 A; A=328-622. DR PDB; 1XMN; X-ray; 1.85 A; A/C/E/G=328-363, B/D/F/H=364-622. DR PDB; 1YPE; X-ray; 1.81 A; H=364-620, L=334-360. DR PDB; 1YPG; X-ray; 1.80 A; H=364-620, L=334-360. DR PDB; 1YPJ; X-ray; 1.78 A; H=364-620, L=334-360. DR PDB; 1YPK; X-ray; 1.78 A; H=364-620, L=334-360. DR PDB; 1YPL; X-ray; 1.85 A; H=364-620, L=334-360. DR PDB; 1YPM; X-ray; 1.85 A; H=364-620, L=334-360. DR PDB; 1Z71; X-ray; 1.80 A; A=335-621. DR PDB; 1Z8I; X-ray; 2.00 A; A=324-361, B=364-622. DR PDB; 1Z8J; X-ray; 2.00 A; A=322-361, B=364-622. DR PDB; 1ZGI; X-ray; 2.20 A; A=335-621. DR PDB; 1ZGV; X-ray; 2.20 A; A=335-621. DR PDB; 1ZRB; X-ray; 1.90 A; A=335-621. DR PDB; 2A0Q; X-ray; 1.90 A; A/C=334-349, B/D=364-620. DR PDB; 2A2X; X-ray; 2.44 A; H=364-622, L=330-363. DR PDB; 2A45; X-ray; 3.65 A; A/D=328-363, B/E=364-622. DR PDB; 2AFQ; X-ray; 1.93 A; A/C=332-360, B/D=364-622. DR PDB; 2ANK; X-ray; 2.46 A; H=364-622, L=330-363. DR PDB; 2ANM; X-ray; 2.40 A; H=364-620, L=328-363. DR PDB; 2B5T; X-ray; 2.10 A; A/C=315-363, B/D=364-622. DR PDB; 2BDY; X-ray; 1.61 A; A=334-622. DR PDB; 2BVR; X-ray; 1.25 A; H=364-622, L=328-363. DR PDB; 2BVS; X-ray; 1.40 A; H=364-622, L=328-363. DR PDB; 2BVX; X-ray; 3.20 A; H=364-622, L=328-363. DR PDB; 2BXT; X-ray; 1.83 A; H=364-622, L=328-363. DR PDB; 2BXU; X-ray; 2.80 A; H=364-622, L=328-363. DR PDB; 2C8W; X-ray; 1.96 A; A=328-363, B=364-622. DR PDB; 2C8X; X-ray; 2.17 A; A=328-363, B=364-622. DR PDB; 2C8Y; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 2C8Z; X-ray; 2.14 A; A=328-363, B=364-622. DR PDB; 2C90; X-ray; 2.25 A; A=328-363, B=364-622. DR PDB; 2C93; X-ray; 2.20 A; A=328-363, B=364-622. DR PDB; 2CF8; X-ray; 1.30 A; H=364-620, L=334-361. DR PDB; 2CF9; X-ray; 1.79 A; H=364-620, L=334-361. DR PDB; 2CN0; X-ray; 1.30 A; H=364-620, L=334-361. DR PDB; 2FEQ; X-ray; 2.44 A; H=364-622, L=328-363. DR PDB; 2FES; X-ray; 2.42 A; H=364-622, L=328-363. DR PDB; 2GDE; X-ray; 2.00 A; H=364-622, L=328-363. DR PDB; 2GP9; X-ray; 1.87 A; A=328-362, B=364-620. DR PDB; 2H9T; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 2HGT; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 2HNT; X-ray; 2.50 A; C=364-433, E=437-517, F=518-622, L=328-363. DR PDB; 2HPP; X-ray; 3.30 A; H=364-622, L=328-363. DR PDB; 2HPQ; X-ray; 3.30 A; H=364-622, L=328-363, P=213-291. DR PDB; 2HWL; X-ray; 2.40 A; A/C=328-363, B/D=364-622. DR PDB; 2JH0; X-ray; 1.70 A; C=328-361, D=364-622. DR PDB; 2JH5; X-ray; 2.50 A; C=328-363, D=364-622. DR PDB; 2JH6; X-ray; 2.21 A; C=328-361, D=364-622. DR PDB; 2OD3; X-ray; 1.75 A; A=328-363, B=364-622. DR PDB; 2PGB; X-ray; 1.54 A; A=328-363, B=364-622. DR PDB; 2PGQ; X-ray; 1.80 A; A=319-363, B=364-622. DR PDB; 2PKS; X-ray; 2.50 A; A=334-360, B=364-510, C=518-619. DR PDB; 2PW8; X-ray; 1.84 A; H=364-621, L=334-360. DR PDB; 2R2M; X-ray; 2.10 A; A=334-359, B=364-622. DR PDB; 2THF; X-ray; 2.10 A; A=328-363, B=364-622. DR PDB; 2UUF; X-ray; 1.26 A; A=328-363, B=364-622. DR PDB; 2UUJ; X-ray; 1.32 A; A=328-363, B=364-622. DR PDB; 2UUK; X-ray; 1.39 A; A=328-363, B=364-622. DR PDB; 2V3H; X-ray; 1.79 A; H=364-620, L=334-361. DR PDB; 2V3O; X-ray; 1.79 A; H=364-620, L=334-361. DR PDB; 2ZC9; X-ray; 1.58 A; H=364-622, L=328-363. DR PDB; 2ZDA; X-ray; 1.73 A; H=364-622, L=328-363. DR PDB; 2ZDV; X-ray; 1.72 A; H=364-622, L=328-363. DR PDB; 2ZF0; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 2ZFF; X-ray; 1.47 A; H=364-622, L=328-363. DR PDB; 2ZFP; X-ray; 2.25 A; H=364-622, L=328-363. DR PDB; 2ZFQ; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 2ZFR; X-ray; 1.85 A; H=364-622, L=328-363. DR PDB; 2ZG0; X-ray; 1.75 A; H=364-622, L=328-363. DR PDB; 2ZGB; X-ray; 1.60 A; H=364-622, L=328-363. DR PDB; 2ZGX; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 2ZHE; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 2ZHF; X-ray; 1.98 A; H=364-622, L=328-363. DR PDB; 2ZHQ; X-ray; 1.96 A; H=364-622, L=328-363. DR PDB; 2ZHW; X-ray; 2.02 A; H=364-622, L=328-363. DR PDB; 2ZI2; X-ray; 1.65 A; H=364-622, L=328-363. DR PDB; 2ZIQ; X-ray; 1.65 A; H=364-622, L=328-363. DR PDB; 2ZNK; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 2ZO3; X-ray; 1.70 A; H=364-622, L=328-363. DR PDB; 3B23; X-ray; 2.40 A; A=328-363, B=364-622. DR PDB; 3B9F; X-ray; 1.60 A; H=364-622, L=315-363. DR PDB; 3BEF; X-ray; 2.20 A; A/D=320-363, B/E=364-622. DR PDB; 3BEI; X-ray; 1.55 A; A=320-363, B=364-622. DR PDB; 3BF6; X-ray; 2.50 A; H=364-622, L=328-363. DR PDB; 3BIU; X-ray; 2.30 A; H=364-620, L=333-361. DR PDB; 3BIV; X-ray; 1.80 A; H=364-620, L=333-361. DR PDB; 3BV9; X-ray; 1.80 A; A=333-363, B=364-622. DR PDB; 3C1K; X-ray; 1.84 A; A=335-621. DR PDB; 3C27; X-ray; 2.18 A; A=334-359, B=364-622. DR PDB; 3D49; X-ray; 1.50 A; H=364-622, L=328-363. DR PDB; 3DA9; X-ray; 1.80 A; A=328-363, B=364-622. DR PDB; 3DD2; X-ray; 1.90 A; H=364-621, L=332-361. DR PDB; 3DHK; X-ray; 1.73 A; H=364-622, L=328-363. DR PDB; 3DT0; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 3DUX; X-ray; 1.60 A; H=364-622, L=328-363. DR PDB; 3E6P; X-ray; 2.10 A; H=364-622, L=206-363. DR PDB; 3EE0; X-ray; 2.75 A; A=328-363, B=364-622. DR PDB; 3EGK; X-ray; 2.20 A; H=364-622, L=328-363. DR PDB; 3EQ0; X-ray; 1.53 A; H=364-622, L=328-363. DR PDB; 3F68; X-ray; 1.75 A; H=364-622, L=328-363. DR PDB; 3GIC; X-ray; 1.55 A; A=328-363, B=364-622. DR PDB; 3GIS; X-ray; 2.40 A; A/C/E=315-363, B/D/F=364-622. DR PDB; 3HAT; X-ray; 2.50 A; H=364-622, L=328-363. DR PDB; 3HKJ; X-ray; 2.60 A; A/D=333-363, B/E=364-622. DR PDB; 3HTC; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 3JZ1; X-ray; 1.60 A; A=328-363, B=364-622. DR PDB; 3JZ2; X-ray; 2.40 A; A=328-363, B=364-622. DR PDB; 3K65; X-ray; 1.85 A; A=199-314, B=315-622. DR PDB; 3LDX; X-ray; 2.25 A; H=364-622, L=328-363. DR PDB; 3LU9; X-ray; 1.80 A; A/D=318-363, B/E=364-622. DR PDB; 3NXP; X-ray; 2.20 A; A=199-622. DR PDB; 3P17; X-ray; 1.43 A; H=364-622, L=328-363. DR PDB; 3P6Z; X-ray; 1.70 A; A/G=328-363, B/H=364-622. DR PDB; 3P70; X-ray; 2.55 A; A/C/E/G=328-363, B/D/F/H=364-622. DR PDB; 3PMH; X-ray; 3.20 A; A=328-363, B=364-622. DR PDB; 3PO1; X-ray; 1.65 A; A=334-360, B=364-510, C=518-619. DR PDB; 3QDZ; X-ray; 2.80 A; A/C=333-363, B/D=364-622. DR PDB; 3QGN; X-ray; 2.10 A; A=333-363, B=364-622. DR PDB; 3QLP; X-ray; 2.14 A; H=364-622, L=328-363. DR PDB; 3QTO; X-ray; 1.52 A; H=364-622, L=328-363. DR PDB; 3QTV; X-ray; 1.63 A; H=364-622, L=328-363. DR PDB; 3QWC; X-ray; 1.75 A; H=364-622, L=328-363. DR PDB; 3QX5; X-ray; 1.35 A; H=364-622, L=328-363. DR PDB; 3R3G; X-ray; 1.75 A; A=333-363, B=364-622. DR PDB; 3RLW; X-ray; 1.69 A; H=364-622, L=328-363. DR PDB; 3RLY; X-ray; 1.51 A; H=364-622, L=328-363. DR PDB; 3RM0; X-ray; 1.34 A; H=364-622, L=328-363. DR PDB; 3RM2; X-ray; 1.23 A; H=364-622, L=328-363. DR PDB; 3RML; X-ray; 1.53 A; H=364-622, L=328-363. DR PDB; 3RMM; X-ray; 1.58 A; H=364-622, L=328-363. DR PDB; 3RMN; X-ray; 1.78 A; H=364-622, L=328-363. DR PDB; 3RMO; X-ray; 1.40 A; H=364-622, L=328-363. DR PDB; 3S7H; X-ray; 1.90 A; A=329-363, B=364-622. DR PDB; 3S7K; X-ray; 1.90 A; A/C=329-363, B/D=364-622. DR PDB; 3SHA; X-ray; 1.52 A; H=364-622, L=328-363. DR PDB; 3SHC; X-ray; 1.90 A; H=364-622, L=328-363. DR PDB; 3SI3; X-ray; 1.55 A; H=364-622, L=328-363. DR PDB; 3SI4; X-ray; 1.27 A; H=364-622, L=328-363. DR PDB; 3SQE; X-ray; 1.90 A; E=333-622. DR PDB; 3SQH; X-ray; 2.20 A; E=333-622. DR PDB; 3SV2; X-ray; 1.30 A; H=364-622, L=328-363. DR PDB; 3T5F; X-ray; 1.45 A; H=364-622, L=328-363. DR PDB; 3TU7; X-ray; 2.49 A; H=364-622, L=328-363. DR PDB; 3U69; X-ray; 1.55 A; H=364-622, L=334-363. DR PDB; 3U8O; X-ray; 1.28 A; H=364-622, L=334-363. DR PDB; 3U8R; X-ray; 1.47 A; H=364-622, L=334-363. DR PDB; 3U8T; X-ray; 1.86 A; H=364-620, L=334-360. DR PDB; 3U98; X-ray; 1.45 A; H=364-622, L=328-363. DR PDB; 3U9A; X-ray; 1.58 A; H=364-622, L=328-363. DR PDB; 3UTU; X-ray; 1.55 A; H=364-622, L=328-363. DR PDB; 3UWJ; X-ray; 1.50 A; H=364-622, L=328-363. DR PDB; 3VXE; X-ray; 1.25 A; H=364-622, L=328-363. DR PDB; 3VXF; Other; 1.60 A; H=364-622, L=328-363. DR PDB; 4AX9; X-ray; 1.90 A; H=364-620, L=334-361. DR PDB; 4AYV; X-ray; 2.80 A; A=332-361, B=364-620. DR PDB; 4AYY; X-ray; 2.60 A; A=332-361, B=364-620. DR PDB; 4AZ2; X-ray; 2.60 A; A=332-361, B=364-620. DR PDB; 4BAH; X-ray; 1.94 A; A=328-363, B=364-622. DR PDB; 4BAK; X-ray; 1.94 A; A=328-363, B=364-622. DR PDB; 4BAM; X-ray; 1.88 A; A=328-363, B=364-622. DR PDB; 4BAN; X-ray; 1.87 A; A=328-363, B=364-622. DR PDB; 4BAO; X-ray; 1.87 A; A=328-363, B=364-622. DR PDB; 4BAQ; X-ray; 1.89 A; A=328-363, B=364-622. DR PDB; 4BOH; X-ray; 2.60 A; A/H=364-622, B/L=328-363. DR PDB; 4CH2; X-ray; 1.60 A; A/C=328-363, B/D=364-622. DR PDB; 4CH8; X-ray; 1.75 A; A/C/E/G=328-363, B/D/F/H=364-622. DR PDB; 4DIH; X-ray; 1.80 A; H=364-622, L=328-363. DR PDB; 4DII; X-ray; 2.05 A; H=364-622, L=328-363. DR PDB; 4DT7; X-ray; 1.90 A; A/C=332-363, B/D=364-622. DR PDB; 4DY7; X-ray; 2.80 A; A/D=315-363, B/E=364-622. DR PDB; 4E05; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 4E06; X-ray; 3.20 A; H=364-622, L=328-363. DR PDB; 4E7R; X-ray; 2.25 A; G/H=364-622, L/M=328-363. DR PDB; 4H6S; X-ray; 2.19 A; A=333-363, B=364-622. DR PDB; 4H6T; X-ray; 2.40 A; A=317-622. DR PDB; 4HFP; X-ray; 2.40 A; A/C=333-363, B/D=364-622. DR PDB; 4HTC; X-ray; 2.30 A; H=364-622, L=328-363. DR PDB; 4HZH; X-ray; 3.30 A; A/B=90-622. DR PDB; 4I7Y; X-ray; 2.40 A; H=364-622, L=328-363. DR PDB; 4LOY; X-ray; 1.77 A; H=364-620, L=334-360. DR PDB; 4LXB; X-ray; 1.61 A; H=364-622, L=328-363. DR PDB; 4LZ1; X-ray; 1.65 A; H=364-622, L=328-363. DR PDB; 4LZ4; X-ray; 2.56 A; A/C=328-363, B/D=364-622. DR PDB; 4MLF; X-ray; 2.20 A; A=331-363, B=364-622. DR PDB; 4NZQ; X-ray; 2.81 A; A=44-622. DR PDB; 4O03; X-ray; 3.38 A; A=44-622. DR PDB; 4RKJ; X-ray; 1.70 A; A=330-363, B=364-622. DR PDB; 4RKO; X-ray; 1.84 A; A=322-363, B=364-622. DR PDB; 4RN6; X-ray; 3.00 A; A/B=333-622. DR PDB; 4THN; X-ray; 2.50 A; H=364-622, L=328-363. DR PDB; 4UD9; X-ray; 1.12 A; H=364-622, L=333-360. DR PDB; 4UDW; X-ray; 1.16 A; H=364-621, L=333-360. DR PDB; 4UE7; X-ray; 1.13 A; H=364-621, L=333-360. DR PDB; 4UEH; X-ray; 1.16 A; H=364-621, L=333-361. DR PDB; 4UFD; X-ray; 1.43 A; H=364-621, L=333-360. DR PDB; 4UFE; X-ray; 1.59 A; H=364-621, L=333-361. DR PDB; 4UFF; X-ray; 1.55 A; H=364-621, L=333-361. DR PDB; 4UFG; X-ray; 1.65 A; H=364-621, L=333-361. DR PDB; 4YES; X-ray; 1.50 A; A=328-363, B=364-622. DR PDB; 5A2M; X-ray; 1.40 A; H=364-621, L=333-361. DR PDB; 5AF9; X-ray; 1.18 A; H=364-621, L=333-361. DR PDB; 5AFY; X-ray; 1.12 A; H=364-621, L=333-361. DR PDB; 5AFZ; X-ray; 1.53 A; H=364-621, L=333-361. DR PDB; 5AHG; X-ray; 1.24 A; H=364-621, L=333-361. DR PDB; 5CMX; X-ray; 2.98 A; H=364-622, L=328-363. DR PDB; 5DO4; X-ray; 1.86 A; H=364-621, L=328-363. DR PDB; 5E8E; X-ray; 1.90 A; H=364-622, L=328-363. DR PDB; 5EDK; X-ray; 3.21 A; A=44-622. DR PDB; 5EDM; X-ray; 2.20 A; A=44-622. DR PDB; 5EW1; X-ray; 2.95 A; H=364-622, L=328-363. DR PDB; 5EW2; X-ray; 3.59 A; H=364-622, L=328-363. DR PDB; 5GDS; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 5GIM; X-ray; 2.09 A; A=328-363. DR PDB; 5JDU; X-ray; 1.70 A; A/C=331-363, B/D=364-622. DR PDB; 5JFD; X-ray; 1.46 A; H=364-622, L=328-363. DR PDB; 5JZY; X-ray; 1.27 A; H=364-622, L=328-363. DR PDB; 5L6N; X-ray; 1.63 A; H=364-622, L=328-363. DR PDB; 5MJT; X-ray; 1.40 A; H=364-622, L=328-363. DR PDB; 5MLS; X-ray; 1.62 A; H=364-622, L=328-363. DR PDB; 5MM6; X-ray; 1.29 A; H=364-622, L=328-363. DR PDB; 5NHU; X-ray; 1.45 A; A/C/H=364-622, B/D/L=328-363. DR PDB; 5TO3; X-ray; 2.34 A; A=318-363, B=364-621. DR PDB; 5Z5W; NMR; -; A=606-617. DR PDB; 5Z5X; NMR; -; A=605-622. DR PDB; 6BJR; X-ray; 6.00 A; A=44-622. DR PDB; 6C2W; X-ray; 4.12 A; A/B=44-622. DR PDB; 6EO6; X-ray; 1.69 A; H=364-622, L=328-363. DR PDB; 6EO7; X-ray; 2.24 A; H=364-622, L=328-363. DR PDB; 6EO8; X-ray; 1.94 A; H=364-622, L=328-363. DR PDB; 6EO9; X-ray; 1.84 A; H=364-622, L=328-363. DR PDB; 6V5T; X-ray; 2.10 A; E=333-622. DR PDB; 7KME; X-ray; 2.10 A; H=364-622, L=328-363. DR PDB; 7TPP; EM; 4.10 A; E=44-622. DR PDB; 8BWW; NMR; -; A=605-622. DR PDB; 8KME; X-ray; 2.10 A; 1=328-359, 2=364-620. DR PDBsum; 1A2C; -. DR PDBsum; 1A3B; -. DR PDBsum; 1A3E; -. DR PDBsum; 1A46; -. DR PDBsum; 1A4W; -. DR PDBsum; 1A5G; -. DR PDBsum; 1A61; -. DR PDBsum; 1ABI; -. DR PDBsum; 1ABJ; -. DR PDBsum; 1AD8; -. DR PDBsum; 1AE8; -. DR PDBsum; 1AFE; -. DR PDBsum; 1AHT; -. DR PDBsum; 1AI8; -. DR PDBsum; 1AIX; -. DR PDBsum; 1AWF; -. DR PDBsum; 1AWH; -. DR PDBsum; 1AY6; -. DR PDBsum; 1B5G; -. DR PDBsum; 1B7X; -. DR PDBsum; 1BA8; -. DR PDBsum; 1BB0; -. DR PDBsum; 1BCU; -. DR PDBsum; 1BHX; -. DR PDBsum; 1BMM; -. DR PDBsum; 1BMN; -. DR PDBsum; 1BTH; -. DR PDBsum; 1C1U; -. DR PDBsum; 1C1V; -. DR PDBsum; 1C1W; -. DR PDBsum; 1C4U; -. DR PDBsum; 1C4V; -. DR PDBsum; 1C4Y; -. DR PDBsum; 1C5L; -. DR PDBsum; 1C5N; -. DR PDBsum; 1C5O; -. DR PDBsum; 1CA8; -. DR PDBsum; 1D3D; -. DR PDBsum; 1D3P; -. DR PDBsum; 1D3Q; -. DR PDBsum; 1D3T; -. DR PDBsum; 1D4P; -. DR PDBsum; 1D6W; -. DR PDBsum; 1D9I; -. DR PDBsum; 1DE7; -. DR PDBsum; 1DIT; -. DR PDBsum; 1DM4; -. DR PDBsum; 1DOJ; -. DR PDBsum; 1DWB; -. DR PDBsum; 1DWC; -. DR PDBsum; 1DWD; -. DR PDBsum; 1DWE; -. DR PDBsum; 1DX5; -. DR PDBsum; 1E0F; -. DR PDBsum; 1EB1; -. DR PDBsum; 1EOJ; -. DR PDBsum; 1EOL; -. DR PDBsum; 1FPC; -. DR PDBsum; 1FPH; -. DR PDBsum; 1G30; -. DR PDBsum; 1G32; -. DR PDBsum; 1G37; -. DR PDBsum; 1GHV; -. DR PDBsum; 1GHW; -. DR PDBsum; 1GHX; -. DR PDBsum; 1GHY; -. DR PDBsum; 1GJ4; -. DR PDBsum; 1GJ5; -. DR PDBsum; 1H8D; -. DR PDBsum; 1H8I; -. DR PDBsum; 1HAG; -. DR PDBsum; 1HAH; -. DR PDBsum; 1HAI; -. DR PDBsum; 1HAO; -. DR PDBsum; 1HAP; -. DR PDBsum; 1HBT; -. DR PDBsum; 1HDT; -. DR PDBsum; 1HGT; -. DR PDBsum; 1HLT; -. DR PDBsum; 1HUT; -. DR PDBsum; 1HXE; -. DR PDBsum; 1HXF; -. DR PDBsum; 1IHS; -. DR PDBsum; 1IHT; -. DR PDBsum; 1JMO; -. DR PDBsum; 1JOU; -. DR PDBsum; 1JWT; -. DR PDBsum; 1K21; -. DR PDBsum; 1K22; -. DR PDBsum; 1KTS; -. DR PDBsum; 1KTT; -. DR PDBsum; 1LHC; -. DR PDBsum; 1LHD; -. DR PDBsum; 1LHE; -. DR PDBsum; 1LHF; -. DR PDBsum; 1LHG; -. DR PDBsum; 1MH0; -. DR PDBsum; 1MU6; -. DR PDBsum; 1MU8; -. DR PDBsum; 1MUE; -. DR PDBsum; 1NM6; -. DR PDBsum; 1NO9; -. DR PDBsum; 1NRN; -. DR PDBsum; 1NRO; -. DR PDBsum; 1NRP; -. DR PDBsum; 1NRQ; -. DR PDBsum; 1NRR; -. DR PDBsum; 1NRS; -. DR PDBsum; 1NT1; -. DR PDBsum; 1NU7; -. DR PDBsum; 1NU9; -. DR PDBsum; 1NY2; -. DR PDBsum; 1NZQ; -. DR PDBsum; 1O0D; -. DR PDBsum; 1O2G; -. DR PDBsum; 1O5G; -. DR PDBsum; 1OOK; -. DR PDBsum; 1OYT; -. DR PDBsum; 1P8V; -. DR PDBsum; 1PPB; -. DR PDBsum; 1QBV; -. DR PDBsum; 1QHR; -. DR PDBsum; 1QJ1; -. DR PDBsum; 1QJ6; -. DR PDBsum; 1QJ7; -. DR PDBsum; 1QUR; -. DR PDBsum; 1RD3; -. DR PDBsum; 1RIW; -. DR PDBsum; 1SB1; -. DR PDBsum; 1SFQ; -. DR PDBsum; 1SG8; -. DR PDBsum; 1SGI; -. DR PDBsum; 1SHH; -. DR PDBsum; 1SL3; -. DR PDBsum; 1SR5; -. DR PDBsum; 1T4U; -. DR PDBsum; 1T4V; -. DR PDBsum; 1TA2; -. DR PDBsum; 1TA6; -. DR PDBsum; 1TB6; -. DR PDBsum; 1TBZ; -. DR PDBsum; 1THP; -. DR PDBsum; 1THR; -. DR PDBsum; 1THS; -. DR PDBsum; 1TMB; -. DR PDBsum; 1TMT; -. DR PDBsum; 1TMU; -. DR PDBsum; 1TOM; -. DR PDBsum; 1TQ0; -. DR PDBsum; 1TQ7; -. DR PDBsum; 1TWX; -. DR PDBsum; 1UMA; -. DR PDBsum; 1UVS; -. DR PDBsum; 1VR1; -. DR PDBsum; 1VZQ; -. DR PDBsum; 1W7G; -. DR PDBsum; 1WAY; -. DR PDBsum; 1WBG; -. DR PDBsum; 1XM1; -. DR PDBsum; 1XMN; -. DR PDBsum; 1YPE; -. DR PDBsum; 1YPG; -. DR PDBsum; 1YPJ; -. DR PDBsum; 1YPK; -. DR PDBsum; 1YPL; -. DR PDBsum; 1YPM; -. DR PDBsum; 1Z71; -. DR PDBsum; 1Z8I; -. DR PDBsum; 1Z8J; -. DR PDBsum; 1ZGI; -. DR PDBsum; 1ZGV; -. DR PDBsum; 1ZRB; -. DR PDBsum; 2A0Q; -. DR PDBsum; 2A2X; -. DR PDBsum; 2A45; -. DR PDBsum; 2AFQ; -. DR PDBsum; 2ANK; -. DR PDBsum; 2ANM; -. DR PDBsum; 2B5T; -. DR PDBsum; 2BDY; -. DR PDBsum; 2BVR; -. DR PDBsum; 2BVS; -. DR PDBsum; 2BVX; -. DR PDBsum; 2BXT; -. DR PDBsum; 2BXU; -. DR PDBsum; 2C8W; -. DR PDBsum; 2C8X; -. DR PDBsum; 2C8Y; -. DR PDBsum; 2C8Z; -. DR PDBsum; 2C90; -. DR PDBsum; 2C93; -. DR PDBsum; 2CF8; -. DR PDBsum; 2CF9; -. DR PDBsum; 2CN0; -. DR PDBsum; 2FEQ; -. DR PDBsum; 2FES; -. DR PDBsum; 2GDE; -. DR PDBsum; 2GP9; -. DR PDBsum; 2H9T; -. DR PDBsum; 2HGT; -. DR PDBsum; 2HNT; -. DR PDBsum; 2HPP; -. DR PDBsum; 2HPQ; -. DR PDBsum; 2HWL; -. DR PDBsum; 2JH0; -. DR PDBsum; 2JH5; -. DR PDBsum; 2JH6; -. DR PDBsum; 2OD3; -. DR PDBsum; 2PGB; -. DR PDBsum; 2PGQ; -. DR PDBsum; 2PKS; -. DR PDBsum; 2PW8; -. DR PDBsum; 2R2M; -. DR PDBsum; 2THF; -. DR PDBsum; 2UUF; -. DR PDBsum; 2UUJ; -. DR PDBsum; 2UUK; -. DR PDBsum; 2V3H; -. DR PDBsum; 2V3O; -. DR PDBsum; 2ZC9; -. DR PDBsum; 2ZDA; -. DR PDBsum; 2ZDV; -. DR PDBsum; 2ZF0; -. DR PDBsum; 2ZFF; -. DR PDBsum; 2ZFP; -. DR PDBsum; 2ZFQ; -. DR PDBsum; 2ZFR; -. DR PDBsum; 2ZG0; -. DR PDBsum; 2ZGB; -. DR PDBsum; 2ZGX; -. DR PDBsum; 2ZHE; -. DR PDBsum; 2ZHF; -. DR PDBsum; 2ZHQ; -. DR PDBsum; 2ZHW; -. DR PDBsum; 2ZI2; -. DR PDBsum; 2ZIQ; -. DR PDBsum; 2ZNK; -. DR PDBsum; 2ZO3; -. DR PDBsum; 3B23; -. DR PDBsum; 3B9F; -. DR PDBsum; 3BEF; -. DR PDBsum; 3BEI; -. DR PDBsum; 3BF6; -. DR PDBsum; 3BIU; -. DR PDBsum; 3BIV; -. DR PDBsum; 3BV9; -. DR PDBsum; 3C1K; -. DR PDBsum; 3C27; -. DR PDBsum; 3D49; -. DR PDBsum; 3DA9; -. DR PDBsum; 3DD2; -. DR PDBsum; 3DHK; -. DR PDBsum; 3DT0; -. DR PDBsum; 3DUX; -. DR PDBsum; 3E6P; -. DR PDBsum; 3EE0; -. DR PDBsum; 3EGK; -. DR PDBsum; 3EQ0; -. DR PDBsum; 3F68; -. DR PDBsum; 3GIC; -. DR PDBsum; 3GIS; -. DR PDBsum; 3HAT; -. DR PDBsum; 3HKJ; -. DR PDBsum; 3HTC; -. DR PDBsum; 3JZ1; -. DR PDBsum; 3JZ2; -. DR PDBsum; 3K65; -. DR PDBsum; 3LDX; -. DR PDBsum; 3LU9; -. DR PDBsum; 3NXP; -. DR PDBsum; 3P17; -. DR PDBsum; 3P6Z; -. DR PDBsum; 3P70; -. DR PDBsum; 3PMH; -. DR PDBsum; 3PO1; -. DR PDBsum; 3QDZ; -. DR PDBsum; 3QGN; -. DR PDBsum; 3QLP; -. DR PDBsum; 3QTO; -. DR PDBsum; 3QTV; -. DR PDBsum; 3QWC; -. DR PDBsum; 3QX5; -. DR PDBsum; 3R3G; -. DR PDBsum; 3RLW; -. DR PDBsum; 3RLY; -. DR PDBsum; 3RM0; -. DR PDBsum; 3RM2; -. DR PDBsum; 3RML; -. DR PDBsum; 3RMM; -. DR PDBsum; 3RMN; -. DR PDBsum; 3RMO; -. DR PDBsum; 3S7H; -. DR PDBsum; 3S7K; -. DR PDBsum; 3SHA; -. DR PDBsum; 3SHC; -. DR PDBsum; 3SI3; -. DR PDBsum; 3SI4; -. DR PDBsum; 3SQE; -. DR PDBsum; 3SQH; -. DR PDBsum; 3SV2; -. DR PDBsum; 3T5F; -. DR PDBsum; 3TU7; -. DR PDBsum; 3U69; -. DR PDBsum; 3U8O; -. DR PDBsum; 3U8R; -. DR PDBsum; 3U8T; -. DR PDBsum; 3U98; -. DR PDBsum; 3U9A; -. DR PDBsum; 3UTU; -. DR PDBsum; 3UWJ; -. DR PDBsum; 3VXE; -. DR PDBsum; 3VXF; -. DR PDBsum; 4AX9; -. DR PDBsum; 4AYV; -. DR PDBsum; 4AYY; -. DR PDBsum; 4AZ2; -. DR PDBsum; 4BAH; -. DR PDBsum; 4BAK; -. DR PDBsum; 4BAM; -. DR PDBsum; 4BAN; -. DR PDBsum; 4BAO; -. DR PDBsum; 4BAQ; -. DR PDBsum; 4BOH; -. DR PDBsum; 4CH2; -. DR PDBsum; 4CH8; -. DR PDBsum; 4DIH; -. DR PDBsum; 4DII; -. DR PDBsum; 4DT7; -. DR PDBsum; 4DY7; -. DR PDBsum; 4E05; -. DR PDBsum; 4E06; -. DR PDBsum; 4E7R; -. DR PDBsum; 4H6S; -. DR PDBsum; 4H6T; -. DR PDBsum; 4HFP; -. DR PDBsum; 4HTC; -. DR PDBsum; 4HZH; -. DR PDBsum; 4I7Y; -. DR PDBsum; 4LOY; -. DR PDBsum; 4LXB; -. DR PDBsum; 4LZ1; -. DR PDBsum; 4LZ4; -. DR PDBsum; 4MLF; -. DR PDBsum; 4NZQ; -. DR PDBsum; 4O03; -. DR PDBsum; 4RKJ; -. DR PDBsum; 4RKO; -. DR PDBsum; 4RN6; -. DR PDBsum; 4THN; -. DR PDBsum; 4UD9; -. DR PDBsum; 4UDW; -. DR PDBsum; 4UE7; -. DR PDBsum; 4UEH; -. DR PDBsum; 4UFD; -. DR PDBsum; 4UFE; -. DR PDBsum; 4UFF; -. DR PDBsum; 4UFG; -. DR PDBsum; 4YES; -. DR PDBsum; 5A2M; -. DR PDBsum; 5AF9; -. DR PDBsum; 5AFY; -. DR PDBsum; 5AFZ; -. DR PDBsum; 5AHG; -. DR PDBsum; 5CMX; -. DR PDBsum; 5DO4; -. DR PDBsum; 5E8E; -. DR PDBsum; 5EDK; -. DR PDBsum; 5EDM; -. DR PDBsum; 5EW1; -. DR PDBsum; 5EW2; -. DR PDBsum; 5GDS; -. DR PDBsum; 5GIM; -. DR PDBsum; 5JDU; -. DR PDBsum; 5JFD; -. DR PDBsum; 5JZY; -. DR PDBsum; 5L6N; -. DR PDBsum; 5MJT; -. DR PDBsum; 5MLS; -. DR PDBsum; 5MM6; -. DR PDBsum; 5NHU; -. DR PDBsum; 5TO3; -. DR PDBsum; 5Z5W; -. DR PDBsum; 5Z5X; -. DR PDBsum; 6BJR; -. DR PDBsum; 6C2W; -. DR PDBsum; 6EO6; -. DR PDBsum; 6EO7; -. DR PDBsum; 6EO8; -. DR PDBsum; 6EO9; -. DR PDBsum; 6V5T; -. DR PDBsum; 7KME; -. DR PDBsum; 7TPP; -. DR PDBsum; 8BWW; -. DR PDBsum; 8KME; -. DR AlphaFoldDB; P00734; -. DR BMRB; P00734; -. DR EMDB; EMD-26060; -. DR SMR; P00734; -. DR BioGRID; 108447; 38. DR ComplexPortal; CPX-6222; alpha-thrombin complex. DR DIP; DIP-6115N; -. DR IntAct; P00734; 16. DR MINT; P00734; -. DR STRING; 9606.ENSP00000308541; -. DR BindingDB; P00734; -. DR ChEMBL; CHEMBL204; -. DR DrugBank; DB07211; (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE. DR DrugBank; DB07796; (3ASR,4RS,8ASR,8BRS)-4-(2-(4-FLUOROBENZYL)-1,3-DIOXODEACAHYDROPYRROLO[3,4-A] PYRROLIZIN-4-YL)BENZAMIDINE. DR DrugBank; DB07016; (3R)-8-(dioxidosulfanyl)-3-methyl-1,2,3,4-tetrahydroquinoline. DR DrugBank; DB07521; (3Z,6S)-6-Chloro-1-(2-{[(5-chloro-1-benzothiophen-3-yl)methyl]amino}ethyl)-3-({2-[(2R)-2-piperidinyl]ethyl}imino)-2-piperazinol. DR DrugBank; DB06850; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB07091; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB06845; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB07088; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB07131; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB07095; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide. DR DrugBank; DB07515; 1-(2-{[(6-amino-2-methylpyridin-3-yl)methyl]amino}ethyl)-6-chloro-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-1,4-dihydropyrazin-2-ol. DR DrugBank; DB07897; 1-(HYDROXYMETHYLENEAMINO)-8-HYDROXY-OCTANE. DR DrugBank; DB06878; 1-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)-L-prolinamide. DR DrugBank; DB06947; 1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)-L-prolinamide. DR DrugBank; DB08624; 1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine. DR DrugBank; DB06869; 1-[2-AMINO-2-CYCLOHEXYL-ACETYL]-PYRROLIDINE-3-CARBOXYLIC ACID 5-CHLORO-2-(2-ETHYLCARBAMOYL-ETHOXY)-BENZYLAMIDE. DR DrugBank; DB06929; 1-butanoyl-N-(4-carbamimidoylbenzyl)-L-prolinamide. DR DrugBank; DB07400; 1-ETHOXYCARBONYL-D-PHE-PRO-2(4-AMINOBUTYL)HYDRAZINE. DR DrugBank; DB04771; 1-GUANIDINO-4-(N-NITRO-BENZOYLAMINO-L-LEUCYL-L-PROLYLAMINO)BUTANE. DR DrugBank; DB04772; 1-GUANIDINO-4-(N-PHENYLMETHANESULFONYL-L-LEUCYL-L-PROLYLAMINO)BUTANE. DR DrugBank; DB02287; 2-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidine. DR DrugBank; DB07277; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE. DR DrugBank; DB07550; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(1-OXIDO-2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUOROPHENYL)METHYL]ACETAMIDE. DR DrugBank; DB07549; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-3-METHYL-6-PYRIDINYL)METHYL]ACETAMIDE. DR DrugBank; DB07548; 2-(6-Chloro-3-{[2,2-difluoro-2-(2-pyridinyl)ethyl]amino}-2-oxo-1(2H)-pyrazinyl)-N-[(2-fluoro-6-pyridinyl)methyl]acetamide. DR DrugBank; DB07105; 2-[2-(4-Chloro-Phenylsulfanyl)-Acetylamino]-3-(4-Guanidino-Phenyl)-Propionamide. DR DrugBank; DB04722; 2-[3-chloro-6-[2,2-difluoro-2-(1-oxidopyridin-1-ium-2-yl)ethyl]imino-1-hydroxypyridin-2-yl]-N-[(1R)-1-(3-chlorophenyl)ethyl]acetamide. DR DrugBank; DB07366; 2-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTER. DR DrugBank; DB08254; 2-Naphthalenesulfonic acid. DR DrugBank; DB01725; 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide. DR DrugBank; DB08062; 3-(4-CHLOROPHENYL)-5-(METHYLTHIO)-4H-1,2,4-TRIAZOLE. DR DrugBank; DB07639; 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER. DR DrugBank; DB07461; 3-AMINO-3-BENZYL-9-CARBOXAMIDE[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE. DR DrugBank; DB07120; 3-Carbamimidamido-1,1-diphenylurea. DR DrugBank; DB07190; 3-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamide. DR DrugBank; DB07741; 4-(1R,3AS,4R,8AS,8BR)-[1-DIFLUOROMETHYL-2-(4-FLUOROBENZYL)-3-OXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZAMIDINE. DR DrugBank; DB07353; 4-(2,5-DIAMINO-5-HYDROXY-PENTYL)-PHENOL. DR DrugBank; DB07508; 4-(5-BENZENESULFONYLAMINO-1-METHYL-1H-BENZOIMIDAZOL-2-YLMETHYL)-BENZAMIDINE. DR DrugBank; DB07809; 4-({[4-(3-METHYLBENZOYL)PYRIDIN-2-YL]AMINO}METHYL)BENZENECARBOXIMIDAMIDE. DR DrugBank; DB08546; 4-[(3AS,4R,7R,8AS,8BR)-2-(1,3-BENZODIOXOL-5-YLMETHYL)-7-HYDROXY-1,3-DIOXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZENECARBOXIMIDAMIDE. DR DrugBank; DB08061; 4-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINE. DR DrugBank; DB07718; 4-Hydroxyphenylpyruvic acid. DR DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine. DR DrugBank; DB02723; 4-Oxo-2-Phenylmethanesulfonyl-Octahydro-Pyrrolo[1,2-a]Pyrazine-6-Carboxylic Acid [1-(N-Hydroxycarbamimidoyl)-Piperidin-4-Ylmethyl]-Amide. DR DrugBank; DB07440; 4-TERT-BUTYLBENZENESULFONIC ACID. DR DrugBank; DB07376; 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID). DR DrugBank; DB06861; 6-(2-HYDROXY-CYCLOPENTYL)-7-OXO-HEPTANAMIDINE. DR DrugBank; DB06866; 6-CARBAMIMIDOYL-2-[2-HYDROXY-5-(3-METHOXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID. DR DrugBank; DB06865; 6-CARBAMIMIDOYL-2-[2-HYDROXY-6-(4-HYDROXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID. DR DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine. DR DrugBank; DB06841; [(2R)-1-[(2S)-2-[[(2S,3S)-1-Chloro-6-(diaminomethylideneamino)-2-hydroxyhexan-3-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]azanium. DR DrugBank; DB07934; [[CYCLOHEXANESULFONYL-GLYCYL]-3[PYRIDIN-4-YL-AMINOMETHYL]ALANYL]PIPERIDINE. DR DrugBank; DB08422; [PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINE. DR DrugBank; DB07659; AC-(D)PHE-PRO-BOROHOMOLYS-OH. DR DrugBank; DB07660; AC-(D)PHE-PRO-BOROHOMOORNITHINE-OH. DR DrugBank; DB07658; AC-(D)Phe-pro-borolys-OH. DR DrugBank; DB13151; Anti-inhibitor coagulant complex. DR DrugBank; DB00025; Antihemophilic factor, human recombinant. DR DrugBank; DB11166; Antithrombin Alfa. DR DrugBank; DB00278; Argatroban. DR DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine. DR DrugBank; DB07083; beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide. DR DrugBank; DB00006; Bivalirudin. DR DrugBank; DB00100; Coagulation Factor IX (Recombinant). DR DrugBank; DB13152; Coagulation Factor IX Human. DR DrugBank; DB09228; Conestat alfa. DR DrugBank; DB09130; Copper. DR DrugBank; DB03159; CRA_8696. DR DrugBank; DB06911; D-leucyl-N-(3-chlorobenzyl)-L-prolinamide. DR DrugBank; DB06996; D-leucyl-N-(4-carbamimidoylbenzyl)-L-prolinamide. DR DrugBank; DB06919; D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide. DR DrugBank; DB07027; D-phenylalanyl-N-(3-fluorobenzyl)-L-prolinamide. DR DrugBank; DB07133; D-phenylalanyl-N-(3-methylbenzyl)-L-prolinamide. DR DrugBank; DB07143; D-phenylalanyl-N-benzyl-L-prolinamide. DR DrugBank; DB07005; D-phenylalanyl-N-{4-[amino(iminio)methyl]benzyl}-L-prolinamide. DR DrugBank; DB06695; Dabigatran etexilate. DR DrugBank; DB00055; Drotrecogin alfa. DR DrugBank; DB01225; Enoxaparin. DR DrugBank; DB05714; Flovagatran. DR DrugBank; DB12831; Gabexate. DR DrugBank; DB03847; gamma-carboxy-L-glutamic acid. DR DrugBank; DB07278; GW-813893. DR DrugBank; DB01767; Hemi-Babim. DR DrugBank; DB06404; Human C1-esterase inhibitor. DR DrugBank; DB09332; Kappadione. DR DrugBank; DB00001; Lepirudin. DR DrugBank; DB13998; Lonoctocog alfa. DR DrugBank; DB04136; Lysophosphotidylserine. DR DrugBank; DB00170; Menadione. DR DrugBank; DB06838; methyl L-phenylalaninate. DR DrugBank; DB13999; Moroctocog alfa. DR DrugBank; DB06868; N-(3-chlorobenzyl)-1-(4-methylpentanoyl)-L-prolinamide. DR DrugBank; DB06942; N-(4-carbamimidoylbenzyl)-1-(3-phenylpropanoyl)-L-prolinamide. DR DrugBank; DB06936; N-(4-carbamimidoylbenzyl)-1-(4-methylpentanoyl)-L-prolinamide. DR DrugBank; DB07165; N-(5-CHLORO-BENZO[B]THIOPHEN-3-YLMETHYL)-2-[6-CHLORO-OXO-3-(2-PYRIDIN-2-YL-ETHYLAMINO)-2H-PYRAZIN-1-YL]-ACETAMIDE. DR DrugBank; DB07527; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]-4-METHOXY-2,3,6-TRIMETHYLBENZENESULFONAMIDE. DR DrugBank; DB07522; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]NAPHTHALENE-2-SULFONAMIDE. DR DrugBank; DB07665; N-[2-(carbamimidamidooxy)ethyl]-2-{6-cyano-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-2-fluorophenyl}acetamide. DR DrugBank; DB07946; N-[2-({[amino(imino)methyl]amino}oxy)ethyl]-2-{6-chloro-3-[(2,2-difluoro-2-phenylethyl)amino]-2-fluorophenyl}acetamide. DR DrugBank; DB06859; N-ALLYL-5-AMIDINOAMINOOXY-PROPYLOXY-3-CHLORO-N-CYCLOPENTYLBENZAMIDE. DR DrugBank; DB06853; N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide. DR DrugBank; DB06858; N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide. DR DrugBank; DB07279; N-ETHYL-N-ISOPROPYL-3-METHYL-5-{[(2S)-2-(PYRIDIN-4-YLAMINO)PROPYL]OXY}BENZAMIDE. DR DrugBank; DB08187; N-Methylphenylalanyl-N-[(trans-4-aminocyclohexyl)methyl]-L-prolinamide. DR DrugBank; DB04591; N-{2,2-DIFLUORO-2-[(2R)-PIPERIDIN-2-YL]ETHYL}-2-[2-(1H-1,2,4-TRIAZOL-1-YL)BENZYL][1,3]OXAZOLO[4,5-C]PYRIDIN-4-AMINE. DR DrugBank; DB07944; N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE. DR DrugBank; DB07128; N7-BUTYL-N2-(5-CHLORO-2-METHYLPHENYL)-5-METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDINE-2,7-DIAMINE. DR DrugBank; DB12598; Nafamostat. DR DrugBank; DB01123; Proflavine. DR DrugBank; DB04786; Suramin. DR DrugBank; DB05777; Thrombomodulin Alfa. DR DrugBank; DB04697; TRANS-4-(GUANIDINOMETHYL)-CYCLOHEXANE-L-YL-D-3-CYCLOHEXYLALANYL-L-AZETIDINE-2-YL-D-TYROSINYL-L-HOMOARGININAMIDE. DR DrugBank; DB09109; Turoctocog alfa. DR DrugBank; DB14738; Turoctocog alfa pegol. DR DrugBank; DB04898; Ximelagatran. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB08152; {(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate. DR DrugCentral; P00734; -. DR GuidetoPHARMACOLOGY; 2362; -. DR MEROPS; S01.217; -. DR MoonDB; P00734; Curated. DR GlyConnect; 518; 39 N-Linked glycans (4 sites). DR GlyCosmos; P00734; 10 sites, 50 glycans. DR GlyGen; P00734; 11 sites, 53 N-linked glycans (5 sites), 2 O-linked glycans (7 sites). DR iPTMnet; P00734; -. DR PhosphoSitePlus; P00734; -. DR BioMuta; F2; -. DR DMDM; 135807; -. DR EPD; P00734; -. DR jPOST; P00734; -. DR MassIVE; P00734; -. DR MaxQB; P00734; -. DR PaxDb; 9606-ENSP00000308541; -. DR PeptideAtlas; P00734; -. DR ProteomicsDB; 51269; -. DR TopDownProteomics; P00734; -. DR ABCD; P00734; 3 sequenced antibodies. DR Antibodypedia; 857; 1316 antibodies from 42 providers. DR DNASU; 2147; -. DR Ensembl; ENST00000311907.10; ENSP00000308541.5; ENSG00000180210.15. DR GeneID; 2147; -. DR KEGG; hsa:2147; -. DR MANE-Select; ENST00000311907.10; ENSP00000308541.5; NM_000506.5; NP_000497.1. DR UCSC; uc001ndf.5; human. DR AGR; HGNC:3535; -. DR CTD; 2147; -. DR DisGeNET; 2147; -. DR GeneCards; F2; -. DR GeneReviews; F2; -. DR HGNC; HGNC:3535; F2. DR HPA; ENSG00000180210; Tissue enriched (liver). DR MalaCards; F2; -. DR MIM; 176930; gene. DR MIM; 188050; phenotype. DR MIM; 601367; phenotype. DR MIM; 613679; phenotype. DR MIM; 614390; phenotype. DR neXtProt; NX_P00734; -. DR OpenTargets; ENSG00000180210; -. DR Orphanet; 329217; Cerebral sinovenous thrombosis. DR Orphanet; 325; Congenital factor II deficiency. DR Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia. DR PharmGKB; PA157; -. DR VEuPathDB; HostDB:ENSG00000180210; -. DR eggNOG; ENOG502QTSX; Eukaryota. DR GeneTree; ENSGT00940000154234; -. DR HOGENOM; CLU_006842_19_4_1; -. DR InParanoid; P00734; -. DR OMA; VMIFRKS; -. DR OrthoDB; 211181at2759; -. DR PhylomeDB; P00734; -. DR TreeFam; TF327329; -. DR BioCyc; MetaCyc:HS11470-MONOMER; -. DR BRENDA; 3.4.21.5; 2681. DR PathwayCommons; P00734; -. DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors. DR Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus. DR Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs). DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation). DR Reactome; R-HSA-9657688; Defective factor XII causes hereditary angioedema. DR Reactome; R-HSA-9672391; Defective F8 cleavage by thrombin. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SABIO-RK; P00734; -. DR SignaLink; P00734; -. DR SIGNOR; P00734; -. DR BioGRID-ORCS; 2147; 14 hits in 1152 CRISPR screens. DR EvolutionaryTrace; P00734; -. DR GeneWiki; Thrombin; -. DR GenomeRNAi; 2147; -. DR Pharos; P00734; Tclin. DR PRO; PR:P00734; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P00734; Protein. DR Bgee; ENSG00000180210; Expressed in right lobe of liver and 101 other cell types or tissues. DR ExpressionAtlas; P00734; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008083; F:growth factor activity; TAS:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0070053; F:thrombospondin receptor activity; IDA:BHF-UCL. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB. DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:BHF-UCL. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB. DR GO; GO:0051918; P:negative regulation of fibrinolysis; TAS:BHF-UCL. DR GO; GO:0010544; P:negative regulation of platelet activation; TAS:BHF-UCL. DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL. DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0030168; P:platelet activation; IDA:BHF-UCL. DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0090218; P:positive regulation of lipid kinase activity; IDA:BHF-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; NAS:BHF-UCL. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL. DR GO; GO:0006508; P:proteolysis; TAS:ProtInc. DR GO; GO:0030193; P:regulation of blood coagulation; TAS:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL. DR GO; GO:0009611; P:response to wounding; IDA:BHF-UCL. DR CDD; cd00108; KR; 2. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2. DR Gene3D; 4.10.140.10; Thrombin light chain domain; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR003966; Prothrombin/thrombin. DR InterPro; IPR018992; Thrombin_light_chain. DR InterPro; IPR037111; Thrombin_light_chain_sf. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24254; PROTHROMBIN; 1. DR PANTHER; PTHR24254:SF10; PROTHROMBIN; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00051; Kringle; 2. DR Pfam; PF09396; Thrombin_light; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001149; Thrombin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR PRINTS; PR00018; KRINGLE. DR PRINTS; PR01505; PROTHROMBIN. DR SMART; SM00069; GLA; 1. DR SMART; SM00130; KR; 2. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF57440; Kringle-like; 2. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS00021; KRINGLE_1; 2. DR PROSITE; PS50070; KRINGLE_2; 2. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR SWISS-2DPAGE; P00734; -. DR Genevisible; P00734; HS. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Blood coagulation; Calcium; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disease variant; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; KW Hemostasis; Hydrolase; Kringle; Pharmaceutical; Protease; KW Reference proteome; Repeat; Secreted; Serine protease; Signal; KW Thrombophilia; Zymogen. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT PROPEP 25..43 FT /evidence="ECO:0000269|PubMed:266717, FT ECO:0000269|PubMed:8073540" FT /id="PRO_0000028159" FT CHAIN 44..622 FT /note="Prothrombin" FT /id="PRO_0000028160" FT PEPTIDE 44..198 FT /note="Activation peptide fragment 1" FT /id="PRO_0000028161" FT PEPTIDE 199..327 FT /note="Activation peptide fragment 2" FT /id="PRO_0000028162" FT CHAIN 315..363 FT /note="Thrombin light chain" FT /id="PRO_0000028163" FT CHAIN 364..622 FT /note="Thrombin heavy chain" FT /id="PRO_0000028164" FT DOMAIN 44..89 FT /note="Gla" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463" FT DOMAIN 108..186 FT /note="Kringle 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 213..291 FT /note="Kringle 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 364..618 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 551..573 FT /note="High affinity receptor-binding region which is also FT known as the TP508 peptide" FT ACT_SITE 406 FT /note="Charge relay system" FT ACT_SITE 462 FT /note="Charge relay system" FT ACT_SITE 568 FT /note="Charge relay system" FT SITE 198..199 FT /note="Cleavage; by thrombin" FT SITE 314..315 FT /note="Cleavage; by factor Xa" FT /evidence="ECO:0000269|PubMed:34265300" FT SITE 363..364 FT /note="Cleavage; by factor Xa" FT /evidence="ECO:0000269|PubMed:34265300" FT MOD_RES 49 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407" FT MOD_RES 50 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407" FT MOD_RES 57 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 59 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 62 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 63 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 68 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 69 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 72 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT MOD_RES 75 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:6305407" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320" FT CARBOHYD 416 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923" FT DISULFID 60..65 FT DISULFID 90..103 FT DISULFID 108..186 FT DISULFID 129..169 FT DISULFID 157..181 FT DISULFID 213..291 FT DISULFID 234..274 FT DISULFID 262..286 FT DISULFID 336..482 FT /note="Interchain (between light and heavy chains)" FT DISULFID 391..407 FT DISULFID 536..550 FT /evidence="ECO:0000250" FT DISULFID 564..594 FT /evidence="ECO:0000250" FT VARIANT 72 FT /note="E -> G (in FA2D; Shanghai)" FT /evidence="ECO:0000269|PubMed:14962227" FT /id="VAR_055232" FT VARIANT 165 FT /note="T -> M (confirmed at protein level; dbSNP:rs5896)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:22028381, FT ECO:0000269|Ref.5" FT /id="VAR_011781" FT VARIANT 200 FT /note="E -> K (in FA2D; prothrombin type 3; variant FT confirmed at protein level; dbSNP:rs62623459)" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:6405779" FT /id="VAR_006711" FT VARIANT 314 FT /note="R -> C (in FA2D; Barcelona/Madrid; FT dbSNP:rs121918477)" FT /evidence="ECO:0000269|PubMed:3771562" FT /id="VAR_006712" FT VARIANT 314 FT /note="R -> H (in FA2D; Padua-1; dbSNP:rs754231232)" FT /evidence="ECO:0000269|PubMed:7865694" FT /id="VAR_006713" FT VARIANT 380 FT /note="M -> T (in FA2D; Himi-1; dbSNP:rs121918481)" FT /evidence="ECO:0000269|PubMed:1421398" FT /id="VAR_006714" FT VARIANT 386 FT /note="P -> T (confirmed at protein level; dbSNP:rs5897)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:22028381" FT /id="VAR_011782" FT VARIANT 425 FT /note="R -> C (in FA2D; Quick-1; dbSNP:rs121918479)" FT /evidence="ECO:0000269|PubMed:3242619" FT /id="VAR_006715" FT VARIANT 431 FT /note="R -> H (in FA2D; Himi-2; dbSNP:rs121918482)" FT /evidence="ECO:0000269|PubMed:1421398" FT /id="VAR_006716" FT VARIANT 461 FT /note="R -> W (in FA2D; Tokushima; dbSNP:rs121918478)" FT /evidence="ECO:0000269|PubMed:1349838, FT ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3801671" FT /id="VAR_006717" FT VARIANT 509 FT /note="E -> A (in FA2D; Salakta/Frankfurt)" FT /evidence="ECO:0000269|PubMed:1354985, FT ECO:0000269|PubMed:7792730" FT /id="VAR_006718" FT VARIANT 532 FT /note="E -> Q" FT /evidence="ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:873923" FT /id="VAR_068913" FT VARIANT 601 FT /note="G -> V (in FA2D; Quick-2; dbSNP:rs121918480)" FT /evidence="ECO:0000269|PubMed:2719946" FT /id="VAR_006719" FT MUTAGEN 314 FT /note="R->Q: Loss of cleavage by factor Xa." FT /evidence="ECO:0000269|PubMed:34265300" FT MUTAGEN 363 FT /note="R->Q: Loss of cleavage by factor Xa." FT /evidence="ECO:0000269|PubMed:34265300" FT MUTAGEN 568 FT /note="S->A: Loss of catalytic activity; no effect on FT cleavage at R-198 by factor Xa." FT /evidence="ECO:0000269|PubMed:34265300" FT CONFLICT 9..25 FT /note="Missing (in Ref. 3; BAG64719)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="S -> N (in Ref. 4; BAD96497)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="H -> N (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 121 FT /note="N -> S (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="T -> I (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="T -> N (in Ref. 7; CAA23842)" FT /evidence="ECO:0000305" FT CONFLICT 176 FT /note="V -> A (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="I -> T (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 194..195 FT /note="AM -> MV (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 308 FT /note="D -> DEE (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="G -> R (in Ref. 4; BAD96495)" FT /evidence="ECO:0000305" FT CONFLICT 349 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 398 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 485 FT /note="D -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 494 FT /note="Q -> G (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="W -> Y (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="E -> S (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="W -> V (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="N -> D (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 529..530 FT /note="PI -> AL (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 590..592 FT /note="WGE -> AGA (in Ref. 11; AAR08143)" FT /evidence="ECO:0000305" FT HELIX 47..60 FT /evidence="ECO:0007829|PDB:5EDM" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:5EDM" FT HELIX 77..89 FT /evidence="ECO:0007829|PDB:5EDM" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:5EDM" FT HELIX 97..105 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:5EDM" FT TURN 112..115 FT /evidence="ECO:0007829|PDB:4HZH" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:5EDK" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5EDK" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:4NZQ" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:5EDM" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:4NZQ" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:5EDM" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:3K65" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:4HZH" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:4HZH" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4NZQ" FT HELIX 240..246 FT /evidence="ECO:0007829|PDB:3K65" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:5EDK" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:5EDK" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:3K65" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:3K65" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:3K65" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:3BEI" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:4O03" FT HELIX 329..333 FT /evidence="ECO:0007829|PDB:5NHU" FT TURN 334..337 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 340..342 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 352..358 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:1NO9" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:3SQH" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:3QDZ" FT STRAND 378..383 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 384..387 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 388..395 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 397..403 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:4DY7" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 430..433 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 436..438 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 440..449 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 455..458 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 464..470 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 475..477 FT /evidence="ECO:0007829|PDB:4O03" FT HELIX 486..492 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:5EDM" FT STRAND 498..504 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 507..510 FT /evidence="ECO:0007829|PDB:4UD9" FT TURN 513..515 FT /evidence="ECO:0007829|PDB:4CH2" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:4CH2" FT STRAND 524..530 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 533..538 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:1MH0" FT STRAND 548..551 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 565..569 FT /evidence="ECO:0007829|PDB:3U8O" FT STRAND 571..575 FT /evidence="ECO:0007829|PDB:5AFY" FT TURN 577..579 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 582..590 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 592..595 FT /evidence="ECO:0007829|PDB:5AFY" FT STRAND 596..598 FT /evidence="ECO:0007829|PDB:3K65" FT STRAND 601..605 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 607..609 FT /evidence="ECO:0007829|PDB:5AFY" FT HELIX 610..619 FT /evidence="ECO:0007829|PDB:5AFY" SQ SEQUENCE 622 AA; 70037 MW; 8A25E1DA88208FCF CRC64; MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY GFYTHVFRLK KWIQKVIDQF GE //