ID ANT3_HUMAN Reviewed; 464 AA. AC P01008; B2R6P0; P78439; P78447; Q13815; Q5TC78; Q7KZ43; Q7KZ97; Q9UC78; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 266. DE RecName: Full=Antithrombin-III; DE Short=ATIII; DE AltName: Full=Serpin C1; DE Flags: Precursor; GN Name=SERPINC1; Synonyms=AT3; ORFNames=PRO0309; 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=6298709; DOI=10.1093/nar/10.24.8113; RA Bock S.C., Wion K.L., Vehar G.A., Lawn R.M.; RT "Cloning and expression of the cDNA for human antithrombin III."; RL Nucleic Acids Res. 10:8113-8125(1982). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6572945; DOI=10.1073/pnas.80.7.1845; RA Chandra T., Stackhouse R., Kidd V.J., Woo S.L.C.; RT "Isolation and sequence characterization of a cDNA clone of human RT antithrombin III."; RL Proc. Natl. Acad. Sci. U.S.A. 80:1845-1848(1983). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT3D MET-438. RA Tsuji H., Takada O., Nakagawa M., Tanaka S., Hashimoto-Gotoh T.; RT "Hereditary antithrombin III deficiency: identification of an arginine-406 RT to methionine point mutation near protease reactive site."; RL (In) Yoshida T.O., Wilson J.M. (eds.); RL Molecular approaches to the study and treatment of Human diseases, RL pp.51-55, Elsevier, Amsterdam (1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8476848; DOI=10.1021/bi00067a008; RA Olds R.J., Lane D.A., Chowdhury V., de Stefano V., Leone G., Thein S.L.; RT "Complete nucleotide sequence of the antithrombin gene: evidence for RT homologous recombination causing thrombophilia."; RL Biochemistry 32:4216-4224(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., RA Gao F., Liu M., He F.; RT "Functional prediction of the coding sequences of 75 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-30 AND ALA-147. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP PROTEIN SEQUENCE OF 33-464, GLYCOSYLATION AT ASN-128; ASN-167; ASN-187 AND RP ASN-224, AND DISULFIDE BONDS. RA Petersen T.E., Dudek-Wojciechowska G., Sottrup-Jensen L., Magnusson S.; RT "Primary structure of antithrombin-III (heparin cofactor). Partial homology RT between alpha-1-antitrypsin and antithrombin-III."; RL (In) Collen D., Wiman B., Verstraete M. (eds.); RL The physiological inhibitors of blood coagulation and fibrinolysis, RL pp.43-54, Elsevier, Amsterdam (1979). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-464. RX PubMed=6305982; DOI=10.1016/s0021-9258(20)82077-8; RA Prochownik E.V., Markham A.F., Orkin S.H.; RT "Isolation of a cDNA clone for human antithrombin III."; RL J. Biol. Chem. 258:8389-8394(1983). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-208, AND VARIANT AT3D LEU-439. RX PubMed=3191114; DOI=10.1021/bi00416a052; RA Bock S.C., Marrinan J.A., Radziejewska E.; RT "Antithrombin III Utah: proline-407 to leucine mutation in a highly RT conserved region near the inhibitor reactive site."; RL Biochemistry 27:6171-6178(1988). RN [13] RP PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, AND VARIANT AT3D THR-414. RC TISSUE=Plasma; RX PubMed=7734359; DOI=10.1111/j.1365-2141.1995.tb08368.x; RA Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F., RA Panico M., Morris H.R.; RT "Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency RT undergoes the S-to-R transition and is associated with a plasma-inactive RT high-molecular-weight complex of aggregated antithrombin."; RL Br. J. Haematol. 89:589-601(1995). RN [14] RP REACTIVE SITE. RX PubMed=7238875; DOI=10.1016/0014-5793(81)80255-4; RA Bjoerk I., Danielsson A., Fenton J.W. II, Joernvall H.; RT "The site in human antithrombin for functional proteolytic cleavage by RT human thrombin."; RL FEBS Lett. 126:257-260(1981). RN [15] RP HEPARIN-BINDING SITE. RX PubMed=6693405; DOI=10.1016/s0021-9258(17)43548-4; RA Blackburn M.N., Smith R.L., Carson J., Sibley C.C.; RT "The heparin-binding site of antithrombin III. Identification of a critical RT tryptophan in the amino acid sequence."; RL J. Biol. Chem. 259:939-941(1984). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., RA Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187. 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 [18] RP FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND RP HETERODIMER WITH TMPRSS7. RX PubMed=15853774; DOI=10.1042/bj20050299; RA Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.; RT "Matriptase-3 is a novel phylogenetically preserved membrane-anchored RT serine protease with broad serpin reactivity."; RL Biochem. J. 390:231-242(2005). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-187 AND ASN-224. 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 [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187. 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 [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND STRUCTURE OF RP CARBOHYDRATES. 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY RP 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 [25] RP PHOSPHORYLATION AT THR-63 AND SER-68. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [26] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=8087553; DOI=10.1016/s0969-2126(00)00028-9; RA Carrell R.W., Stein P.E., Fermi G., Wardell M.R.; RT "Biological implications of a 3 A structure of dimeric antithrombin."; RL Structure 2:257-270(1994). RN [27] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). RX PubMed=7656006; DOI=10.1038/nsb0194-48; RA Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M., RA Grootenhuis P.D.J., Hol W.G.J.; RT "The intact and cleaved human antithrombin III complex as a model for RT serpin-proteinase interactions."; RL Nat. Struct. Biol. 1:48-54(1994). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=9067613; DOI=10.1006/jmbi.1996.0798; RA Skinner R., Abrahams J.P., Whisstock J.C., Lesk A.M., Carrel R.W., RA Wardell M.R.; RT "The 2.6 A structure of antithrombin indicates a conformational change at RT the heparin binding site."; RL J. Mol. Biol. 266:601-609(1997). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=9761669; DOI=10.1006/jmbi.1998.2083; RA Skinner R., Chang W.-S.W., Jin L., Pei X.Y., Huntington J.A., RA Abrahams J.P., Carrell R.W., Lomas D.A.; RT "Implications for function and therapy of a 2.9 A structure of binary- RT complexed antithrombin."; RL J. Mol. Biol. 283:9-14(1998). RN [30] RP REVIEW. RX PubMed=2126464; DOI=10.1016/0300-9084(90)90123-x; RA Mourey L., Samama J.-P., Delarue M., Choay J., Lormeau J.C., Petitou M., RA Moras D.; RT "Antithrombin III: structural and functional aspects."; RL Biochimie 72:599-608(1990). RN [31] RP REVIEW ON VARIANTS. RX PubMed=8236149; RA Lane D.A., Olds R.J., Boisclair M., Chowdhury V., Thein S.L., Cooper D.N., RA Blajchman M., Perry D., Emmerich J., Aiach M.; RT "Antithrombin III mutation database: first update. For the Thrombin and its RT Inhibitors Subcommittee of the Scientific and Standardization Committee of RT the International Society on Thrombosis and Haemostasis."; RL Thromb. Haemost. 70:361-369(1993). RN [32] RP REVIEW ON VARIANTS. RX PubMed=7749926; DOI=10.1038/nsb0295-96; RA Stein P.E., Carrell R.W.; RT "What do dysfunctional serpins tell us about molecular mobility and RT disease?"; RL Nat. Struct. Biol. 2:96-113(1995). RN [33] RP REVIEW ON VARIANTS. RX PubMed=8664906; RX DOI=10.1002/(sici)1098-1004(1996)7:1<7::aid-humu2>3.0.co;2-b; RA Perry D.J., Carrell R.W.; RT "Molecular genetics of human antithrombin deficiency."; RL Hum. Mutat. 7:7-22(1996). RN [34] RP VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79; RP SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112; RP PHE-131; VAL-131; LYS-133; 138-PHE-LYS-139 DEL; PRO-148; PRO-150; PRO-158; RP TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219; LYS-219; ARG-257; RP LYS-269; ILE-283; ASN-316; LYS-334; ARG-412; THR-414; PRO-416; SER-416; RP VAL-419; ASP-424; CYS-425; HIS-425; PRO-425; LEU-426; CYS-434; LEU-434; RP SER-434; THR-436; LYS-437; GLY-438; MET-438; LEU-439; THR-439; THR-453; RP ARG-456; THR-457; ASP-459; LEU-461 AND PHE-462, AND VARIANTS GLU-30; THR-52 RP AND CYS-190. RX PubMed=9031473; RG The plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis; RA Lane D.A., Bayston T., Olds R.J., Fitches A.C., Cooper D.N., Millar D.S., RA Jochmans K., Perry D.J., Okajima K., Thein S.L., Emmerich J.; RT "Antithrombin mutation database: 2nd (1997) update."; RL Thromb. Haemost. 77:197-211(1997). RN [35] RP VARIANT AT3D CYS-79. RX PubMed=6582486; DOI=10.1073/pnas.81.2.289; RA Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N.; RT "Antithrombin III Toyama: replacement of arginine-47 by cysteine in RT hereditary abnormal antithrombin III that lacks heparin-binding ability."; RL Proc. Natl. Acad. Sci. U.S.A. 81:289-293(1984). RN [36] RP VARIANT AT3D LEU-73, AND CHARACTERIZATION OF VARIANT AT3D LEU-73. RX PubMed=3080419; DOI=10.1016/s0021-9258(17)36071-4; RA Chang J.Y., Tran T.H.; RT "Antithrombin III Basel. Identification of a Pro-Leu substitution in a RT hereditary abnormal antithrombin with impaired heparin cofactor activity."; RL J. Biol. Chem. 261:1174-1176(1986). RN [37] RP VARIANT AT3D LEU-426. RX PubMed=3805013; DOI=10.1016/s0021-9258(19)75747-0; RA Stephens A.W., Thalley B.S., Hirs C.H.W.; RT "Antithrombin-III Denver, a reactive site variant."; RL J. Biol. Chem. 262:1044-1048(1987). RN [38] RP VARIANT AT3D THR-414. RX PubMed=3179438; RA Devrak-Kizuk R., Chui D.H.K., Prochownik E.V., Carter C.J., Ofosu F.A., RA Blajchman M.A.; RT "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to RT adenine) in codon 382 causing impaired serine protease reactivity."; RL Blood 72:1518-1523(1988). RN [39] RP VARIANTS AT3D CYS-425 AND HIS-425. RX PubMed=3162733; DOI=10.1016/s0021-9258(18)60605-2; RA Erdjument H., Laned D.A., Panico M., di Marzo V., Morris H.R.; RT "Single amino acid substitutions in the reactive site of antithrombin RT leading to thrombosis. Congenital substitution of arginine 393 to cysteine RT in antithrombin Northwick Park and to histidine in antithrombin Glasgow."; RL J. Biol. Chem. 263:5589-5593(1988). RN [40] RP VARIANT AT3D HIS-425. RX PubMed=2781509; DOI=10.1016/0049-3848(89)90127-8; RA Erdjument H., Lane D.A., Panico M., di Marzo V., Morris H.R., Bauer K., RA Rosenberg R.D.; RT "Antithrombin Chicago, amino acid substitution of arginine 393 to RT histidine."; RL Thromb. Res. 54:613-619(1989). RN [41] RP VARIANT AT3D CYS-56. RX PubMed=2365065; DOI=10.1016/0014-5793(90)81530-2; RA Borg J.Y., Brennan S.O., Carrell R.W., George P., Perry D.J., Shaw J.; RT "Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution to RT heparin binding."; RL FEBS Lett. 266:163-166(1990). RN [42] RP VARIANT GLU-30. RX PubMed=1977621; DOI=10.1016/0014-5793(90)81057-u; RA Daly M., Bruce D., Perry D.J., Price J., Harper P.L., O'Meara A., RA Carrell R.W.; RT "Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has an RT aberrant signal peptidase cleavage site."; RL FEBS Lett. 273:87-90(1990). RN [43] RP VARIANT AT3D GLN-161. RX PubMed=2229057; DOI=10.1016/s0021-9258(17)30614-2; RA Gandrille S., Aiach M., Lane D.A., Vidaud D., Molho-Sabatier P., Caso R., RA de Moerloose P., Fiessinger J.-N., Clauser E.; RT "Important role of arginine 129 in heparin-binding site of antithrombin RT III. Identification of a novel mutation arginine 129 to glutamine."; RL J. Biol. Chem. 265:18997-19001(1990). RN [44] RP CHARACTERIZATION OF VARIANT AT3D THR-414, AND MUTAGENESIS OF ALA-414. RX PubMed=2013320; DOI=10.1016/0014-5793(91)80305-m; RA Austin R.C., Rachubinski R.A., Blachjman M.A.; RT "Site-directed mutagenesis of alanine-382 of human antithrombin III."; RL FEBS Lett. 280:254-258(1991). RN [45] RP VARIANT AT3D SER-416. RX PubMed=1906811; DOI=10.1016/0014-5793(91)80809-h; RA Perry D.J., Daly M., Harper P.L., Tait R.C., Price J., Walker I.D., RA Carrell R.W.; RT "Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of RT the reactive centre loop in the inhibitory function of the serpins."; RL FEBS Lett. 285:248-250(1991). RN [46] RP VARIANT AT3D PHE-131. RX PubMed=1555650; DOI=10.1016/0014-5793(92)80854-a; RA Olds R.J., Lane D.A., Boisclair M., Sas G., Bock S.C., Thein S.L.; RT "Antithrombin Budapest 3. An antithrombin variant with reduced heparin RT affinity resulting from the substitution L99F."; RL FEBS Lett. 300:241-246(1992). RN [47] RP VARIANT AT3D ASP-424. RX PubMed=1547341; RA Blajchman M.A., Fernandez-Rachubinski F., Sheffield W.P., Austin R.C., RA Schulman S.; RT "Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with normal RT heparin binding and impaired serine protease reactivity."; RL Blood 79:1428-1434(1992). RN [48] RP VARIANT AT3D PRO-148. RX PubMed=8443391; RA Okajima K., Abe H., Maeda S., Motomura M., Tsujihata M., Nagataki S., RA Okabe H., Takatsuki K.; RT "Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with RT defective heparin binding associated with thrombosis."; RL Blood 81:1300-1305(1993). RN [49] RP VARIANT AT3D 138-PHE-LYS-139 DEL. RX PubMed=8486379; DOI=10.1006/geno.1993.1184; RA Olds R.J., Lane D.A., Beresford C.H., Abildgaard U., Hughes P.M., RA Thein S.L.; RT "A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), RT identified by DNA heteroduplex detection."; RL Genomics 16:298-299(1993). RN [50] RP VARIANTS AT3D HIS-79 AND TYR-160. RX PubMed=7981186; DOI=10.1161/01.atv.14.12.1958; RA Emmerich J., Vidaud D., Alhenc-Gelas M., Chadeuf G., Gouault-Heilmann M., RA Aillaud M.-F., Aiach M.; RT "Three novel mutations of antithrombin inducing high-molecular-mass RT compounds."; RL Arterioscler. Thromb. 14:1958-1965(1994). RN [51] RP VARIANTS AT3D THR-112; TYR-152 AND ILE-283, AND VARIANT CYS-190. RX PubMed=7959685; DOI=10.1007/bf00211016; RA Millar D.S., Wacey A.I., Ribando J., Melissari E., Laursen B., Woods P., RA Kakkar V.V., Cooper D.N.; RT "Three novel missense mutations in the antithrombin III (AT3) gene causing RT recurrent venous thrombosis."; RL Hum. Genet. 94:509-512(1994). RN [52] RP VARIANT AT3D ARG-456. RX PubMed=8274732; RA Jochmans K., Lissens W., Vervoort R., Peeters S., de Waelwe M., RA Liebaers I.; RT "Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 RT antithrombin deficiency and neonatal thrombosis."; RL Blood 83:146-151(1994). RN [53] RP VARIANTS AT3D SER-95; THR-453 AND PHE-462. RX PubMed=7994035; RA van Boven H.H., Olds R.J., Thein S.L., Reitsma P.H., Lane D.A., Briet E., RA Vandenbroucke J.P., Rosendaal F.R.; RT "Hereditary antithrombin deficiency: heterogeneity of the molecular basis RT and mortality in Dutch families."; RL Blood 84:4209-4213(1994). RN [54] RP VARIANT AT3D ASP-219. RX PubMed=7989582; DOI=10.1172/jci117589; RA Bruce D., Perry D.J., Borg J.-Y., Carrell R.W., Wardell M.R.; RT "Thromboembolic disease due to thermolabile conformational changes of RT antithrombin Rouen-VI (187 Asn-->Asp)."; RL J. Clin. Invest. 94:2265-2274(1994). RN [55] RP VARIANTS AT3D VAL-131 AND PRO-150. RA Chowdhury V., Olds R.J., Lane D.A., Mille B., Pabinger I., Thein S.L.; RT "Two novel antithrombin variants (L99V and Q118P) which alter the heparin RT binding domain."; RL Nouv. Rev. Fr. Hematol. 86:268-268(1994). RN [56] RP VARIANT AT3D 273-LYS--LYS-307 DEL. RX PubMed=7878627; RA Emmerich J., Chadeuf G., Alhenc-Gelas M., Gouault-Heilman M., Toulon P., RA Fiessinger J.-N., Aiach M.; RT "Molecular basis of antithrombin type I deficiency: the first large in- RT frame deletion and two novel mutations in exon 6."; RL Thromb. Haemost. 72:534-539(1994). RN [57] RP VARIANT AT3D HIS-425. RX PubMed=7832187; DOI=10.1002/ajh.2830480104; RA Okajima K., Abe H., Wagatsuma M., Okabe H., Takatsuki K.; RT "Antithrombin III Kumamoto II; a single mutation at Arg393-His increased RT the affinity of antithrombin III for heparin."; RL Am. J. Hematol. 48:12-18(1995). RN [58] RP VARIANT AT3D ARG-127. RX PubMed=9157604; RA Ozawa T., Takikawa Y., Niiya K., Fujiwara T., Suzuki K., Sato S., RA Sakuragawa N.; RT "Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing type RT I antithrombin deficiency."; RL Thromb. Haemost. 77:403-403(1997). RN [59] RP VARIANT AT3D PRO-23. RX PubMed=9845533; RA Fitches A.C., Appleby R., Lane D.A., De Stefano V., Leone G., Olds R.J.; RT "Impaired cotranslational processing as a mechanism for type I antithrombin RT deficiency."; RL Blood 92:4671-4676(1998). RN [60] RP VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412. RX PubMed=9759613; RA Jochmans K., Lissens W., Seneca S., Capel P., Chatelain B., Meeus P., RA Osselaer J.C., Peerlinck K., Seghers J., Slacmeulder M., Stibbe J., RA van de Loo J., Vermylen J., Liebaers I., De Waele M.; RT "The molecular basis of antithrombin deficiency in Belgian and Dutch RT families."; RL Thromb. Haemost. 80:376-381(1998). RN [61] RP VARIANT THR-167. RX PubMed=10361121; RA Bayston T.A., Tripodi A., Mannucci P.M., Thompson E., Ireland H., RA Fitches A.C., Hananeia L., Olds R.J., Lane D.A.; RT "Familial overexpression of beta-antithrombin caused by an Asn135-to-Thr RT substitution."; RL Blood 93:4242-4247(1999). RN [62] RP VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397. RX PubMed=10997988; DOI=10.1046/j.1365-2141.2000.02245.x; RA Picard V., Bura A., Emmerich J., Alhenc-Gelas M., Biron C., RA Houbouyan-Reveillard L.L., Molho P., Labatide-Alanore A., Sie P., RA Toulon P., Verdy E., Aiach M.; RT "Molecular bases of antithrombin deficiency in French families: RT identification of seven novel mutations in the antithrombin gene."; RL Br. J. Haematol. 110:731-734(2000). RN [63] RP VARIANT AT3D 152-HIS--PHE-154 DEL. RX PubMed=11794707; DOI=10.1007/bf02982095; RA Niiya K., Kiguchi T., Dansako H., Fujimura K., Fujimoto T., Iijima K., RA Tanimoto M., Harada M.; RT "Two novel gene mutations in type I antithrombin deficiency."; RL Int. J. Hematol. 74:469-472(2001). RN [64] RP VARIANT AT3D PRO-223. RX PubMed=11713457; DOI=10.1067/mpd.2001.118191; RA Baud O., Picard V., Durand P., Duchemin J., Proulle V., Alhenc-Gelas M., RA Devictor D., Dreyfus M.; RT "Intracerebral hemorrhage associated with a novel antithrombin gene RT mutation in a neonate."; RL J. Pediatr. 139:741-743(2001). RN [65] RP VARIANT AT3D GLU-146. RX PubMed=12353073; DOI=10.1267/THRO88030436; RA Mushunje A., Zhou A., Huntington J.A., Conard J., Carrell R.W.; RT "Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin RT affinity."; RL Thromb. Haemost. 88:436-443(2002). RN [66] RP VARIANT AT3D LEU-261. RX PubMed=12595305; DOI=10.1182/blood-2002-11-3391; RA Picard V., Dautzenberg M.-D., Villoutreix B.O., Orliaguet G., RA Alhenc-Gelas M., Aiach M.; RT "Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous RT antithrombin polymerization in vivo associated with severe childhood RT thrombosis."; RL Blood 102:919-925(2003). RN [67] RP VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441. RX PubMed=12894857; DOI=10.1007/bf02983246; RA Nagaizumi K., Inaba H., Amano K., Suzuki M., Arai M., Fukutake K.; RT "Five novel and four recurrent point mutations in the antithrombin gene RT causing venous thrombosis."; RL Int. J. Hematol. 78:79-83(2003). RN [68] RP VARIANTS AT3D LEU-179; CYS-425 AND LEU-426. RX PubMed=15164384; DOI=10.1002/ajh.20067; RA David D., Ribeiro S., Ferrao L., Gago T., Crespo F.; RT "Molecular basis of inherited antithrombin deficiency in Portuguese RT families: identification of genetic alterations and screening for RT additional thrombotic risk factors."; RL Am. J. Hematol. 76:163-171(2004). RN [69] RP VARIANTS AT3D SER-112 AND ARG-456, CHARACTERIZATION OF VARIANTS AT3D RP SER-112 AND ARG-456, AND FUNCTION. RX PubMed=15140129; DOI=10.1111/j.1538-7836.2004.00749.x; RA Corral J., Huntington J.A., Gonzalez-Conejero R., Mushunje A., Navarro M., RA Marco P., Vicente V., Carrell R.W.; RT "Mutations in the shutter region of antithrombin result in formation of RT disulfide-linked dimers and severe venous thrombosis."; RL J. Thromb. Haemost. 2:931-939(2004). RN [70] RP VARIANT AT3D HIS-398. RX PubMed=16908819; DOI=10.1001/archopht.124.8.1165; RA Kuhli C., Jochmans K., Scharrer I., Luechtenberg M., Hattenbach L.-O.; RT "Retinal vein occlusion associated with antithrombin deficiency secondary RT to a novel G9840C missense mutation."; RL Arch. Ophthalmol. 124:1165-1169(2006). RN [71] RP VARIANT AT3D 241-GLU-LEU-242 DELINS RP VAL-LEU-VAL-LEU-VAL-ASN-THR-ARG-THR-SER, AND CHARACTERIZATION OF VARIANT RP AT3D 241-GLU-LEU-242 DELINS VAL-LEU-VAL-LEU-VAL-ASN-THR-ARG-THR-SER. RX PubMed=22758787; DOI=10.1111/j.1538-7836.2012.04839.x; RA Martinez-Martinez I., Johnson D.J., Yamasaki M., Navarro-Fernandez J., RA Ordonez A., Vicente V., Huntington J.A., Corral J.; RT "Type II antithrombin deficiency caused by a large in-frame insertion: RT structural, functional and pathological relevance."; RL J. Thromb. Haemost. 10:1859-1866(2012). RN [72] RP VARIANTS AT3D PHE-53; LEU-73; ASP-125; PRO-170; ASN-218; GLY-248; PRO-293; RP ARG-401; CYS-425; GLY-438 AND ALA-439, AND VARIANT GLU-30. RX PubMed=23910795; DOI=10.1111/jth.12364; RA Puurunen M., Salo P., Engelbarth S., Javela K., Perola M.; RT "Type II antithrombin deficiency caused by a founder mutation Pro73Leu in RT the Finnish population: clinical picture."; RL J. Thromb. Haemost. 11:1844-1849(2013). RN [73] RP VARIANT AT3D VAL-PHE-LEU-PRO-384 INS. RX PubMed=30046692; DOI=10.1002/rth2.12025; RA de la Morena-Barrio M.E., Lopez-Galvez R., Martinez-Martinez I., Asenjo S., RA Sevivas T.S., Lopez M.F., Wypasek E., Entrena L., Vicente V., Corral J.; RT "Defects of splicing in antithrombin deficiency."; RL Res. Pract. Thromb. Haemost. 1:216-222(2017). CC -!- FUNCTION: Most important serine protease inhibitor in plasma that CC regulates the blood coagulation cascade (PubMed:15853774, CC PubMed:15140129). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as CC well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory CC activity is greatly enhanced in the presence of heparin. CC {ECO:0000269|PubMed:15140129, ECO:0000269|PubMed:15853774}. CC -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7. CC -!- INTERACTION: CC P01008; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-1039832, EBI-7147442; CC P01008; P01008: SERPINC1; NbExp=2; IntAct=EBI-1039832, EBI-1039832; CC PRO_0000032489; PRO_0000028160 [P00734]: F2; NbExp=2; IntAct=EBI-26959093, EBI-26959170; CC PRO_0000032489; PRO_0000032489 [P01008]: SERPINC1; NbExp=2; IntAct=EBI-26959093, EBI-26959093; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- TISSUE SPECIFICITY: Found in plasma. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000269|PubMed:26091039}. CC -!- MASS SPECTROMETRY: Mass=57863; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:7734359}; CC -!- MASS SPECTROMETRY: Mass=57911; Method=Electrospray; Note=Variant Thr- CC 414.; Evidence={ECO:0000269|PubMed:7734359}; CC -!- DISEASE: Antithrombin III deficiency (AT3D) [MIM:613118]: An important CC risk factor for hereditary thrombophilia, a hemostatic disorder CC characterized by a tendency to recurrent thrombosis. Antithrombin-III CC deficiency is classified into 4 types. Type I: characterized by a 50% CC decrease in antigenic and functional levels. Type II: has defects CC affecting the thrombin-binding domain. Type III: alteration of the CC heparin-binding domain. Plasma AT-III antigen levels are normal in type CC II and III. Type IV: consists of miscellaneous group of unclassifiable CC mutations. {ECO:0000269|PubMed:10997988, ECO:0000269|PubMed:11713457, CC ECO:0000269|PubMed:11794707, ECO:0000269|PubMed:12353073, CC ECO:0000269|PubMed:12595305, ECO:0000269|PubMed:12894857, CC ECO:0000269|PubMed:15140129, ECO:0000269|PubMed:15164384, CC ECO:0000269|PubMed:1547341, ECO:0000269|PubMed:1555650, CC ECO:0000269|PubMed:16908819, ECO:0000269|PubMed:1906811, CC ECO:0000269|PubMed:2013320, ECO:0000269|PubMed:2229057, CC ECO:0000269|PubMed:22758787, ECO:0000269|PubMed:2365065, CC ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:2781509, CC ECO:0000269|PubMed:30046692, ECO:0000269|PubMed:3080419, CC ECO:0000269|PubMed:3162733, ECO:0000269|PubMed:3179438, CC ECO:0000269|PubMed:3191114, ECO:0000269|PubMed:3805013, CC ECO:0000269|PubMed:6582486, ECO:0000269|PubMed:7734359, CC ECO:0000269|PubMed:7832187, ECO:0000269|PubMed:7878627, CC ECO:0000269|PubMed:7959685, ECO:0000269|PubMed:7981186, CC ECO:0000269|PubMed:7989582, ECO:0000269|PubMed:7994035, CC ECO:0000269|PubMed:8274732, ECO:0000269|PubMed:8443391, CC ECO:0000269|PubMed:8486379, ECO:0000269|PubMed:9031473, CC ECO:0000269|PubMed:9157604, ECO:0000269|PubMed:9759613, CC ECO:0000269|PubMed:9845533, ECO:0000269|Ref.3, ECO:0000269|Ref.55}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Antithrombin entry; CC URL="https://en.wikipedia.org/wiki/Antithrombin"; CC -!- WEB RESOURCE: Name=Antithrombin mutation database; CC URL="https://www1.imperial.ac.uk/departmentofmedicine/divisions/experimentalmedicine/haematology/coag/antithrombin/"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/serpinc1/"; 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; L00185; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L00186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L00190; AAB40025.1; -; Genomic_DNA. DR EMBL; D29832; BAA06212.1; -; mRNA. DR EMBL; X68793; CAA48690.1; -; Genomic_DNA. DR EMBL; AF130100; AAG35525.1; -; mRNA. DR EMBL; AK312654; BAG35537.1; -; mRNA. DR EMBL; AF386078; AAK60337.1; -; Genomic_DNA. DR EMBL; AL136170; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90969.1; -; Genomic_DNA. DR EMBL; M21643; AAA51793.1; -; Genomic_DNA. DR EMBL; M21644; AAA51794.1; -; Genomic_DNA. DR EMBL; M21643; AAA51794.1; JOINED; Genomic_DNA. DR EMBL; M21642; AAA51796.1; -; Genomic_DNA. DR EMBL; M21636; AAA51796.1; JOINED; Genomic_DNA. DR EMBL; M21637; AAA51796.1; JOINED; Genomic_DNA. DR EMBL; M21638; AAA51796.1; JOINED; Genomic_DNA. DR EMBL; M21640; AAA51796.1; JOINED; Genomic_DNA. DR EMBL; M21641; AAA51796.1; JOINED; Genomic_DNA. DR CCDS; CCDS1313.1; -. DR PIR; A49494; XHHU3. DR RefSeq; NP_000479.1; NM_000488.3. DR PDB; 1ANT; X-ray; 3.00 A; I/L=33-464. DR PDB; 1ATH; X-ray; 3.20 A; A/B=33-464. DR PDB; 1AZX; X-ray; 2.90 A; I/L=33-464. DR PDB; 1BR8; X-ray; 2.90 A; I/L=33-464. DR PDB; 1DZG; X-ray; 2.80 A; I/L=33-464. DR PDB; 1DZH; X-ray; 2.85 A; I/L=33-464. DR PDB; 1E03; X-ray; 2.90 A; I/L=33-464. DR PDB; 1E04; X-ray; 2.60 A; I/L=33-464. DR PDB; 1E05; X-ray; 2.62 A; I/L=33-464. DR PDB; 1JVQ; X-ray; 2.60 A; I/L=33-464. DR PDB; 1LK6; X-ray; 2.80 A; I/L=33-464. DR PDB; 1NQ9; X-ray; 2.60 A; I/L=33-464. DR PDB; 1OYH; X-ray; 2.62 A; I/L=33-464. DR PDB; 1R1L; X-ray; 2.70 A; I/L=33-464. DR PDB; 1SR5; X-ray; 3.10 A; A=33-464. DR PDB; 1T1F; X-ray; 2.75 A; A/B/C=33-464. DR PDB; 1TB6; X-ray; 2.50 A; I=33-464. DR PDB; 2ANT; X-ray; 2.60 A; I/L=33-464. DR PDB; 2B4X; X-ray; 2.80 A; I/L=37-463. DR PDB; 2B5T; X-ray; 2.10 A; I=33-464. DR PDB; 2BEH; X-ray; 2.70 A; I/L=33-464. DR PDB; 2GD4; X-ray; 3.30 A; C/I=22-464. DR PDB; 2HIJ; X-ray; 2.90 A; I/L=33-464. DR PDB; 2ZNH; X-ray; 2.80 A; A/B=33-464. DR PDB; 3EVJ; X-ray; 3.00 A; I/L=33-464. DR PDB; 3KCG; X-ray; 1.70 A; I=33-464. DR PDB; 4EB1; X-ray; 2.80 A; I/L=33-464. DR PDBsum; 1ANT; -. DR PDBsum; 1ATH; -. DR PDBsum; 1AZX; -. DR PDBsum; 1BR8; -. DR PDBsum; 1DZG; -. DR PDBsum; 1DZH; -. DR PDBsum; 1E03; -. DR PDBsum; 1E04; -. DR PDBsum; 1E05; -. DR PDBsum; 1JVQ; -. DR PDBsum; 1LK6; -. DR PDBsum; 1NQ9; -. DR PDBsum; 1OYH; -. DR PDBsum; 1R1L; -. DR PDBsum; 1SR5; -. DR PDBsum; 1T1F; -. DR PDBsum; 1TB6; -. DR PDBsum; 2ANT; -. DR PDBsum; 2B4X; -. DR PDBsum; 2B5T; -. DR PDBsum; 2BEH; -. DR PDBsum; 2GD4; -. DR PDBsum; 2HIJ; -. DR PDBsum; 2ZNH; -. DR PDBsum; 3EVJ; -. DR PDBsum; 3KCG; -. DR PDBsum; 4EB1; -. DR AlphaFoldDB; P01008; -. DR PCDDB; P01008; -. DR SMR; P01008; -. DR BioGRID; 106953; 39. DR DIP; DIP-38009N; -. DR IntAct; P01008; 20. DR MINT; P01008; -. DR STRING; 9606.ENSP00000356671; -. DR BindingDB; P01008; -. DR ChEMBL; CHEMBL1950; -. DR DrugBank; DB11598; Antithrombin III human. DR DrugBank; DB00407; Ardeparin. DR DrugBank; DB09258; Bemiparin. DR DrugBank; DB09130; Copper. DR DrugBank; DB06779; Dalteparin. DR DrugBank; DB06754; Danaparoid. DR DrugBank; DB01225; Enoxaparin. DR DrugBank; DB00569; Fondaparinux. DR DrugBank; DB01109; Heparin. DR DrugBank; DB04464; N-Formylmethionine. DR DrugBank; DB08813; Nadroparin. DR DrugBank; DB09141; Protamine sulfate. DR DrugBank; DB05361; SR-123781A. DR DrugBank; DB06271; Sulodexide. DR DrugBank; DB06822; Tinzaparin. DR DrugCentral; P01008; -. DR GuidetoPHARMACOLOGY; 2632; -. DR MEROPS; I04.018; -. DR CarbonylDB; P01008; -. DR GlyConnect; 766; 21 N-Linked glycans (4 sites). DR GlyCosmos; P01008; 6 sites, 25 glycans. DR GlyGen; P01008; 7 sites, 25 N-linked glycans (4 sites), 2 O-linked glycans (1 site). DR iPTMnet; P01008; -. DR PhosphoSitePlus; P01008; -. DR BioMuta; SERPINC1; -. DR DMDM; 113936; -. DR DOSAC-COBS-2DPAGE; P01008; -. DR REPRODUCTION-2DPAGE; P01008; -. DR CPTAC; non-CPTAC-1070; -. DR CPTAC; non-CPTAC-1071; -. DR CPTAC; non-CPTAC-1072; -. DR EPD; P01008; -. DR jPOST; P01008; -. DR MassIVE; P01008; -. DR MaxQB; P01008; -. DR PaxDb; 9606-ENSP00000356671; -. DR PeptideAtlas; P01008; -. DR PRIDE; P01008; -. DR ProteomicsDB; 51299; -. DR Antibodypedia; 793; 908 antibodies from 42 providers. DR DNASU; 462; -. DR Ensembl; ENST00000367698.4; ENSP00000356671.3; ENSG00000117601.15. DR GeneID; 462; -. DR KEGG; hsa:462; -. DR MANE-Select; ENST00000367698.4; ENSP00000356671.3; NM_000488.4; NP_000479.1. DR UCSC; uc001gjt.4; human. DR AGR; HGNC:775; -. DR CTD; 462; -. DR DisGeNET; 462; -. DR GeneCards; SERPINC1; -. DR HGNC; HGNC:775; SERPINC1. DR HPA; ENSG00000117601; Tissue enriched (liver). DR MalaCards; SERPINC1; -. DR MIM; 107300; gene. DR MIM; 613118; phenotype. DR neXtProt; NX_P01008; -. DR OpenTargets; ENSG00000117601; -. DR Orphanet; 82; Hereditary thrombophilia due to congenital antithrombin deficiency. DR PharmGKB; PA35026; -. DR VEuPathDB; HostDB:ENSG00000117601; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000157967; -. DR HOGENOM; CLU_023330_0_2_1; -. DR InParanoid; P01008; -. DR OMA; CQVPTMY; -. DR OrthoDB; 3218836at2759; -. DR PhylomeDB; P01008; -. DR TreeFam; TF343094; -. DR PathwayCommons; P01008; -. 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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SignaLink; P01008; -. DR SIGNOR; P01008; -. DR BioGRID-ORCS; 462; 13 hits in 1152 CRISPR screens. DR ChiTaRS; SERPINC1; human. DR EvolutionaryTrace; P01008; -. DR GeneWiki; Antithrombin; -. DR GenomeRNAi; 462; -. DR Pharos; P01008; Tclin. DR PRO; PR:P01008; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P01008; Protein. DR Bgee; ENSG00000117601; Expressed in right lobe of liver and 100 other cell types or tissues. DR ExpressionAtlas; P01008; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. 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:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0030193; P:regulation of blood coagulation; IEA:InterPro. DR CDD; cd02045; serpinC1_AT3; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR InterPro; IPR033829; Antithrombin_3_serpin_domain. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR InterPro; IPR036186; Serpin_sf. DR InterPro; IPR042178; Serpin_sf_1. DR InterPro; IPR042185; Serpin_sf_2. DR PANTHER; PTHR11461:SF53; ANTITHROMBIN-III; 1. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. DR SWISS-2DPAGE; P01008; -. DR Genevisible; P01008; HS. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; Hemostasis; Heparin-binding; KW Phosphoprotein; Protease inhibitor; Reference proteome; Secreted; KW Serine protease inhibitor; Signal; Thrombophilia. FT SIGNAL 1..32 FT /evidence="ECO:0000269|Ref.10" FT CHAIN 33..464 FT /note="Antithrombin-III" FT /id="PRO_0000032489" FT BINDING 81 FT /ligand="heparin" FT /ligand_id="ChEBI:CHEBI:28304" FT BINDING 161 FT /ligand="heparin" FT /ligand_id="ChEBI:CHEBI:28304" FT BINDING 177 FT /ligand="heparin" FT /ligand_id="ChEBI:CHEBI:28304" FT SITE 425..426 FT /note="Reactive bond" FT /evidence="ECO:0000269|PubMed:7238875" FT MOD_RES 63 FT /note="Phosphothreonine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 68 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:24275569" FT CARBOHYD 128 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, FT ECO:0000269|Ref.10" FT CARBOHYD 167 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|Ref.10" FT CARBOHYD 187 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, FT ECO:0000269|Ref.10" FT CARBOHYD 224 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16263699, FT ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10" FT DISULFID 40..160 FT /evidence="ECO:0000269|Ref.10" FT DISULFID 53..127 FT /evidence="ECO:0000269|Ref.10" FT DISULFID 279..462 FT /evidence="ECO:0000269|Ref.10" FT VARIANT 17 FT /note="Y -> S (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_027450" FT VARIANT 23 FT /note="L -> P (in AT3D; type-I; does not undergo FT post-translational glycosylation; dbSNP:rs387906575)" FT /evidence="ECO:0000269|PubMed:9031473, FT ECO:0000269|PubMed:9845533" FT /id="VAR_012748" FT VARIANT 30 FT /note="V -> E (in Dublin; dbSNP:rs2227624)" FT /evidence="ECO:0000269|PubMed:1977621, FT ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:9031473, FT ECO:0000269|Ref.7" FT /id="VAR_007032" FT VARIANT 32 FT /note="C -> R (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9759613" FT /id="VAR_027451" FT VARIANT 39 FT /note="I -> N (in AT3D; type-II; Rouen-3; lack of FT heparin-binding properties; dbSNP:rs121909558)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007033" FT VARIANT 52 FT /note="M -> T (previously Whitechapel; dbSNP:rs892712171)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007034" FT VARIANT 53 FT /note="C -> F (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071199" FT VARIANT 56 FT /note="R -> C (in AT3D; type-II; Rouen-4; lack of FT heparin-binding properties; dbSNP:rs28929469)" FT /evidence="ECO:0000269|PubMed:2365065, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007035" FT VARIANT 73 FT /note="P -> L (in AT3D; type-II; lacks heparin-binding FT ability; dbSNP:rs121909551)" FT /evidence="ECO:0000269|PubMed:23910795, FT ECO:0000269|PubMed:3080419, ECO:0000269|PubMed:9031473, FT ECO:0000269|PubMed:9759613" FT /id="VAR_007036" FT VARIANT 79 FT /note="R -> C (in AT3D; FT Tours/Alger/Amiens/Toyama/Paris-1/Paris-2/Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; FT lacks heparin-binding ability; dbSNP:rs121909547)" FT /evidence="ECO:0000269|PubMed:6582486, FT ECO:0000269|PubMed:9031473, ECO:0000269|PubMed:9759613" FT /id="VAR_007037" FT VARIANT 79 FT /note="R -> H (in AT3D; type-II; FT Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding FT properties; dbSNP:rs121909552)" FT /evidence="ECO:0000269|PubMed:7981186, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007038" FT VARIANT 79 FT /note="R -> S (in AT3D; type-II; Rouen-2; lack of FT heparin-binding properties; dbSNP:rs121909547)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007039" FT VARIANT 87 FT /note="Missing (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007040" FT VARIANT 89 FT /note="R -> C (in AT3D; type-I; dbSNP:rs147266200)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007041" FT VARIANT 90 FT /note="F -> L (in AT3D; type-I; Budapest-6)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007042" FT VARIANT 95 FT /note="Y -> C (in AT3D; type-I; dbSNP:rs907768931)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_027452" FT VARIANT 95 FT /note="Y -> S (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7994035, FT ECO:0000269|PubMed:9031473" FT /id="VAR_012316" FT VARIANT 98 FT /note="L -> P (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_027453" FT VARIANT 108..109 FT /note="Missing (in AT3D; type-I)" FT /id="VAR_007043" FT VARIANT 112 FT /note="P -> S (in AT3D; severely decreased antithrombin FT activity)" FT /evidence="ECO:0000269|PubMed:15140129" FT /id="VAR_086227" FT VARIANT 112 FT /note="P -> T (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7959685, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007044" FT VARIANT 121 FT /note="M -> K (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:12894857" FT /id="VAR_027454" FT VARIANT 125 FT /note="G -> D (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071200" FT VARIANT 127 FT /note="C -> R (in AT3D; type-I; dbSNP:rs121909573)" FT /evidence="ECO:0000269|PubMed:9157604" FT /id="VAR_027455" FT VARIANT 131 FT /note="L -> F (in AT3D; type-II; Budapest-3/Budapest-7; FT dbSNP:rs121909567)" FT /evidence="ECO:0000269|PubMed:1555650, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007045" FT VARIANT 131 FT /note="L -> V (in AT3D; type-II; Southport)" FT /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.55" FT /id="VAR_007046" FT VARIANT 133 FT /note="Q -> K (in AT3D; type I; dbSNP:rs1411331203)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007047" FT VARIANT 138..139 FT /note="Missing (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:8486379" FT /id="VAR_007048" FT VARIANT 146 FT /note="K -> E (in AT3D; Dreux; complete loss af heparin FT binding; dbSNP:rs1170430756)" FT /evidence="ECO:0000269|PubMed:12353073" FT /id="VAR_027456" FT VARIANT 147 FT /note="T -> A (in dbSNP:rs2227606)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_013085" FT VARIANT 148 FT /note="S -> P (in AT3D; type-II; Nagasaki; defective FT heparin binding associated with thrombosis; FT dbSNP:rs121909569)" FT /evidence="ECO:0000269|PubMed:8443391, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007049" FT VARIANT 150 FT /note="Q -> P (in AT3D; type-II; Vienna; FT dbSNP:rs765445413)" FT /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.55" FT /id="VAR_007050" FT VARIANT 152..154 FT /note="Missing (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:11794707" FT /id="VAR_012749" FT VARIANT 152 FT /note="H -> Y (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7959685" FT /id="VAR_007051" FT VARIANT 153 FT /note="Missing (in AT3D; type-I)" FT /id="VAR_007052" FT VARIANT 158 FT /note="L -> P (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007053" FT VARIANT 160 FT /note="C -> Y (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7981186, FT ECO:0000269|PubMed:9031473" FT /id="VAR_027457" FT VARIANT 161 FT /note="R -> Q (in AT3D; type-II; Geneva; FT dbSNP:rs121909563)" FT /evidence="ECO:0000269|PubMed:2229057, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007054" FT VARIANT 167 FT /note="N -> T (in dbSNP:rs121909570)" FT /evidence="ECO:0000269|PubMed:10361121" FT /id="VAR_012750" FT VARIANT 170 FT /note="S -> P (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071201" FT VARIANT 178 FT /note="L -> H (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:12894857" FT /id="VAR_027458" FT VARIANT 179 FT /note="F -> L (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:15164384" FT /id="VAR_027459" FT VARIANT 190 FT /note="Y -> C (in AT3D; uncertain significance)" FT /evidence="ECO:0000269|PubMed:7959685, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007055" FT VARIANT 198 FT /note="Y -> C (in AT3D; type-I and -II; Whitechapel; FT dbSNP:rs1425532034)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007056" FT VARIANT 198 FT /note="Y -> H (in AT3D; type-I; dbSNP:rs1572090114)" FT /evidence="ECO:0000269|PubMed:9031473, FT ECO:0000269|PubMed:9759613" FT /id="VAR_027460" FT VARIANT 214 FT /note="S -> F (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:10997988" FT /id="VAR_027461" FT VARIANT 214 FT /note="S -> Y (in AT3D; type-I; dbSNP:rs483352854)" FT /id="VAR_007057" FT VARIANT 218 FT /note="I -> N (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071202" FT VARIANT 218 FT /note="Missing (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_027462" FT VARIANT 219 FT /note="N -> D (in AT3D; type-II; Rouen-6; increases FT affinity for heparin; dbSNP:rs121909571)" FT /evidence="ECO:0000269|PubMed:7989582, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007059" FT VARIANT 219 FT /note="N -> K (in AT3D; type-II; Glasgow-3)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007058" FT VARIANT 223 FT /note="S -> P (in AT3D; type-I; dbSNP:rs121909572)" FT /evidence="ECO:0000269|PubMed:10997988, FT ECO:0000269|PubMed:11713457" FT /id="VAR_027463" FT VARIANT 241..242 FT /note="EL -> VLVLVNTRTS (in AT3D; severely decreased FT antithrombin activity; low affinity for heparin)" FT /evidence="ECO:0000269|PubMed:22758787" FT /id="VAR_086197" FT VARIANT 243 FT /note="T -> I (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:10997988" FT /id="VAR_027464" FT VARIANT 248 FT /note="V -> G (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071203" FT VARIANT 251 FT /note="I -> T (in AT3D; type-I; dbSNP:rs1423630663)" FT /evidence="ECO:0000269|PubMed:10997988" FT /id="VAR_027465" FT VARIANT 257 FT /note="W -> R (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473, FT ECO:0000269|PubMed:9759613" FT /id="VAR_027466" FT VARIANT 261 FT /note="F -> L (in AT3D)" FT /evidence="ECO:0000269|PubMed:12595305" FT /id="VAR_027467" FT VARIANT 269 FT /note="E -> K (in AT3D; type-II; Truro; increases affinity FT for heparin; dbSNP:rs758087836)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007060" FT VARIANT 273..307 FT /note="Missing (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7878627" FT /id="VAR_007061" FT VARIANT 283 FT /note="M -> I (in AT3D; type-II)" FT /evidence="ECO:0000269|PubMed:7959685, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007062" FT VARIANT 283 FT /note="M -> V (in AT3D; type-II)" FT /evidence="ECO:0000269|PubMed:10997988" FT /id="VAR_027468" FT VARIANT 293 FT /note="R -> P (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071204" FT VARIANT 302 FT /note="L -> P (in AT3D; type-I)" FT /id="VAR_007063" FT VARIANT 316 FT /note="I -> N (in AT3D; type-II; Haslar/Whitechapel)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007064" FT VARIANT 323 FT /note="S -> P (in AT3D)" FT /id="VAR_027469" FT VARIANT 334 FT /note="E -> K (in AT3D; type-II)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007065" FT VARIANT 344 FT /note="Missing (in AT3D; type-I)" FT /id="VAR_007066" FT VARIANT 381 FT /note="S -> P (in AT3D; type-I; dbSNP:rs121909565)" FT /id="VAR_007067" FT VARIANT 384 FT /note="P -> PVFLP (in AT3D)" FT /evidence="ECO:0000269|PubMed:30046692" FT /id="VAR_086198" FT VARIANT 391 FT /note="R -> Q (in dbSNP:rs201541724)" FT /id="VAR_007068" FT VARIANT 397 FT /note="S -> P (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:10997988" FT /id="VAR_027470" FT VARIANT 398 FT /note="D -> H (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:16908819" FT /id="VAR_027471" FT VARIANT 401 FT /note="H -> R (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071205" FT VARIANT 412 FT /note="S -> R (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:9031473, FT ECO:0000269|PubMed:9759613" FT /id="VAR_027472" FT VARIANT 414 FT /note="A -> T (in AT3D; type-II; Hamilton/Glasgow-2; FT reduces interaction with thrombin by 90%; FT dbSNP:rs121909557)" FT /evidence="ECO:0000269|PubMed:2013320, FT ECO:0000269|PubMed:3179438, ECO:0000269|PubMed:7734359, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007069" FT VARIANT 416 FT /note="A -> P (in AT3D; type-II; FT Charleville/Sudbury/Vicenza/Cambridge-1; FT dbSNP:rs121909548)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007070" FT VARIANT 416 FT /note="A -> S (in AT3D; type-II; Cambridge-2; FT dbSNP:rs121909548)" FT /evidence="ECO:0000269|PubMed:1906811, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007071" FT VARIANT 419 FT /note="A -> V (in AT3D; type-I; dbSNP:rs121909568)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007072" FT VARIANT 424 FT /note="G -> D (in AT3D; type-II; Stockholm; FT dbSNP:rs121909566)" FT /evidence="ECO:0000269|PubMed:1547341, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007073" FT VARIANT 425 FT /note="R -> C (in AT3D; type-II; dbSNP:rs121909554)" FT /evidence="ECO:0000269|PubMed:12894857, FT ECO:0000269|PubMed:15164384, ECO:0000269|PubMed:23910795, FT ECO:0000269|PubMed:3162733, ECO:0000269|PubMed:9031473" FT /id="VAR_007075" FT VARIANT 425 FT /note="R -> H (in AT3D; type-II; FT Glasgow/Sheffield/Chicago/Avranches/Kumamoto-2; increases FT affinity for heparin; deprived of inhibitory activity; FT dbSNP:rs121909549)" FT /evidence="ECO:0000269|PubMed:12894857, FT ECO:0000269|PubMed:2781509, ECO:0000269|PubMed:3162733, FT ECO:0000269|PubMed:7832187, ECO:0000269|PubMed:9031473" FT /id="VAR_007074" FT VARIANT 425 FT /note="R -> P (in AT3D; type-II; Pescara; deprived of FT inhibitory of activity; dbSNP:rs121909549)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007076" FT VARIANT 426 FT /note="S -> L (in AT3D; type-II; Denver/Milano-2; deprived FT of inhibitory activity; dbSNP:rs121909550)" FT /evidence="ECO:0000269|PubMed:15164384, FT ECO:0000269|PubMed:3805013, ECO:0000269|PubMed:9031473" FT /id="VAR_007077" FT VARIANT 434 FT /note="F -> C (in AT3D; type-II; Rosny; FT dbSNP:rs1572084546)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007078" FT VARIANT 434 FT /note="F -> L (in AT3D; type-II; Maisons-Laffite)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007080" FT VARIANT 434 FT /note="F -> S (in AT3D; type-II; Torino)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007079" FT VARIANT 436 FT /note="A -> T (in AT3D; type-II; Oslo/Paris-3; FT dbSNP:rs121909546)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007081" FT VARIANT 437 FT /note="N -> K (in AT3D; type-II; La Rochelle; FT dbSNP:rs1301351856)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007082" FT VARIANT 438 FT /note="R -> G (in AT3D; type I and type-II)" FT /evidence="ECO:0000269|PubMed:23910795, FT ECO:0000269|PubMed:9031473" FT /id="VAR_009258" FT VARIANT 438 FT /note="R -> M (in AT3D; type-II; Kyoto)" FT /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.3" FT /id="VAR_007083" FT VARIANT 439 FT /note="P -> A (in AT3D)" FT /evidence="ECO:0000269|PubMed:23910795" FT /id="VAR_071206" FT VARIANT 439 FT /note="P -> L (in AT3D; type-II; Utah; deprived of FT inhibitory activity; dbSNP:rs121909555)" FT /evidence="ECO:0000269|PubMed:3191114, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007084" FT VARIANT 439 FT /note="P -> T (in AT3D; type-II; Budapest-5; FT dbSNP:rs1487411568)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007085" FT VARIANT 441 FT /note="L -> P (in AT3D; type-II; dbSNP:rs1188571702)" FT /evidence="ECO:0000269|PubMed:12894857" FT /id="VAR_027473" FT VARIANT 453 FT /note="I -> T (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7994035, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007086" FT VARIANT 456 FT /note="G -> R (in AT3D; type-I; severely decreased FT antithrombin activity)" FT /evidence="ECO:0000269|PubMed:15140129, FT ECO:0000269|PubMed:8274732, ECO:0000269|PubMed:9031473" FT /id="VAR_007087" FT VARIANT 457 FT /note="R -> T (in AT3D; type-II)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007088" FT VARIANT 459..461 FT /note="Missing (in AT3D; type-I)" FT /id="VAR_007089" FT VARIANT 459 FT /note="A -> D (in AT3D; type-I; dbSNP:rs1572084448)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007090" FT VARIANT 461 FT /note="P -> L (in AT3D; type-II; Budapest; FT dbSNP:rs121909564)" FT /evidence="ECO:0000269|PubMed:9031473" FT /id="VAR_007091" FT VARIANT 462 FT /note="C -> F (in AT3D; type-I)" FT /evidence="ECO:0000269|PubMed:7994035, FT ECO:0000269|PubMed:9031473" FT /id="VAR_007092" FT MUTAGEN 414 FT /note="A->K: Reduces interaction with thrombin by 99%." FT /evidence="ECO:0000269|PubMed:2013320" FT MUTAGEN 414 FT /note="A->Q: Reduces interaction with thrombin by 80%." FT /evidence="ECO:0000269|PubMed:2013320" FT CONFLICT 69..70 FT /note="EQ -> QE (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="N -> NN (in Ref. 3; BAA06212)" FT /evidence="ECO:0000305" FT CONFLICT 97 FT /note="H -> R (in Ref. 5; AAG35525)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="A -> T (in Ref. 6; BAG35537)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="T -> A (in Ref. 6; BAG35537)" FT /evidence="ECO:0000305" FT CONFLICT 247..249 FT /note="Missing (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="Missing (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 395 FT /note="Y -> YA (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1OYH" FT HELIX 78..101 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:1DZG" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:2B5T" FT HELIX 145..149 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 151..166 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 170..181 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:1E04" FT HELIX 188..198 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 207..225 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:2B4X" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1DZG" FT STRAND 245..255 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 267..272 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:2B5T" FT STRAND 278..294 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 309..317 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:2B5T" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 333..342 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 344..353 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 355..362 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 364..369 FT /evidence="ECO:0007829|PDB:3KCG" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 378..380 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 398..407 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 409..413 FT /evidence="ECO:0007829|PDB:2B5T" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:1E04" FT STRAND 423..426 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 432..435 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 440..446 FT /evidence="ECO:0007829|PDB:3KCG" FT TURN 447..450 FT /evidence="ECO:0007829|PDB:3KCG" FT STRAND 451..459 FT /evidence="ECO:0007829|PDB:3KCG" SQ SEQUENCE 464 AA; 52602 MW; 9A4E324F00683D9D CRC64; MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK //