ID IPSP_HUMAN Reviewed; 406 AA. AC P05154; Q07616; Q9UG30; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 3. DT 24-JAN-2024, entry version 233. DE RecName: Full=Plasma serine protease inhibitor; DE AltName: Full=Acrosomal serine protease inhibitor; DE AltName: Full=Plasminogen activator inhibitor 3; DE Short=PAI-3; DE Short=PAI3; DE AltName: Full=Protein C inhibitor; DE Short=PCI; DE AltName: Full=Serpin A5; DE Flags: Precursor; GN Name=SERPINA5; Synonyms=PCI, PLANH3, PROCI; 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 [MRNA], AND VARIANT ASN-64. RX PubMed=3027058; DOI=10.1016/s0021-9258(19)75827-x; RA Suzuki K., Deyashiki Y., Nishioka J., Kurachi K., Akira M., Yamamoto S., RA Hashimoto S.; RT "Characterization of a cDNA for human protein C inhibitor. A new member of RT the plasma serine protease inhibitor superfamily."; RL J. Biol. Chem. 262:611-616(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-64. RX PubMed=2173165; DOI=10.1016/0049-3848(90)90142-y; RA Meijers J.C.M., Chung D.W.; RT "Evidence for a glycine residue at position 316 in human protein C RT inhibitor."; RL Thromb. Res. 59:389-393(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-64. RX PubMed=1714450; DOI=10.1016/s0021-9258(18)98581-9; RA Meijers J.C.M., Chung D.W.; RT "Organization of the gene coding for human protein C inhibitor (plasminogen RT activator inhibitor-3). Assignment of the gene to chromosome 14."; RL J. Biol. Chem. 266:15028-15034(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8148499; RA Hayashi T., Suzuki K.; RT "Gene organization of human protein C inhibitor, a member of SERPIN family RT proteins encoded in five exons."; RL Int. J. Hematol. 58:213-224(1993). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-55; ASN-64 AND GLU-105. RC TISSUE=Liver; RX PubMed=8713781; RA Radtke K.-P., Greengard J.S., Fernandez J.A., Villoutreix B.O., RA Griffin J.H.; RT "A two-allele polymorphism in protein C inhibitor with varying frequencies RT in different ethnic populations."; RL Thromb. Haemost. 75:62-69(1996). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-44; VAL-55; ASN-64; RP VAL-94; GLU-105; PRO-115 AND ARG-217. RG SeattleSNPs variation discovery resource; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-64. RC TISSUE=Skin; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-406, AND VARIANT ASN-64. RC TISSUE=Testis; RX PubMed=8471250; DOI=10.1002/mrd.1080340308; RA Moore A., Penfold L.M., Johnson J.L., Latchman D.S., Moore H.D.; RT "Human sperm-egg binding is inhibited by peptides corresponding to core RT region of an acrosomal serine protease inhibitor."; RL Mol. Reprod. Dev. 34:280-291(1993). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-406, AND VARIANT ASN-64. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [11] RP PROTEIN SEQUENCE OF 20-39. RX PubMed=2556811; RA Laurell M., Stenflo J.; RT "Protein C inhibitor from human plasma: characterization of native and RT cleaved inhibitor and demonstration of inhibitor complexes with plasma RT kallikrein."; RL Thromb. Haemost. 62:885-891(1989). RN [12] RP FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, AND HETERODIMER WITH RP F2; F5 AND F10. 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 FUNCTION IN BLOOD PLASMA PLAU INHIBITION, AND HETERODIMER WITH PLAU. RX PubMed=3501295; DOI=10.1515/bchm3.1987.368.2.1427; RA Stief T.W., Radtke K.P., Heimburger N.; RT "Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for RT identity of PCI and plasminogen activator inhibitor 3."; RL Biol. Chem. Hoppe-Seyler 368:1427-1433(1987). RN [14] RP FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, AND HETERODIMER WITH RP F5; F11 AND KLKB1. RX PubMed=2844223; DOI=10.1021/bi00412a005; RA Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., RA Bouma B.N.; RT "Inactivation of human plasma kallikrein and factor XIa by protein C RT inhibitor."; RL Biochemistry 27:4231-4237(1988). RN [15] RP FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH KLK3, AND RP SUBCELLULAR LOCATION. RX PubMed=1725227; DOI=10.1016/0049-3848(91)90002-e; RA Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.; RT "Functionally active protein C inhibitor/plasminogen activator inhibitor-3 RT (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations RT in human seminal plasma and complexes with prostate-specific antigen."; RL Thromb. Res. 64:309-320(1991). RN [16] RP TISSUE SPECIFICITY. RX PubMed=1372913; DOI=10.1172/jci115689; RA Laurell M., Christensson A., Abrahamsson P.A., Stenflo J., Lilja H.; RT "Protein C inhibitor in human body fluids. Seminal plasma is rich in RT inhibitor antigen deriving from cells throughout the male reproductive RT system."; RL J. Clin. Invest. 89:1094-1101(1992). RN [17] RP FUNCTION IN SEMINAL PLASMA ACR INHIBITION, HETERODIMER WITH ACR, AND RP SUBCELLULAR LOCATION. RX PubMed=7521127; DOI=10.1152/ajpcell.1994.267.2.c466; RA Zheng X., Geiger M., Ecke S., Bielek E., Donner P., Eberspacher U., RA Schleuning W.D., Binder B.R.; RT "Inhibition of acrosin by protein C inhibitor and localization of protein C RT inhibitor to spermatozoa."; RL Am. J. Physiol. 267:C466-C472(1994). RN [18] RP FUNCTION IN SERINE PROTEASE INHIBITION, AND MUTAGENESIS OF THR-371; RP PHE-372; ARG-373 AND ARG-376. RX PubMed=7548057; DOI=10.1021/bi00040a009; RA Cooper S.T., Whinna H.C., Jackson T.P., Boyd J.M., Church F.C.; RT "Intermolecular interactions between protein C inhibitor and coagulation RT proteases."; RL Biochemistry 34:12991-12997(1995). RN [19] RP FUNCTION IN SEMINAL PLASMA AND URINE KALLIKREIN INHIBITION, HETERODIMER RP WITH TISSUE KALLIKREIN, AND SUBCELLULAR LOCATION. RX PubMed=8536714; DOI=10.1111/j.1432-1033.1995.641_b.x; RA Espana F., Fink E., Sanchez-Cuenca J., Gilabert J., Estelles A., RA Witzgall K.; RT "Complexes of tissue kallikrein with protein C inhibitor in human semen and RT urine."; RL Eur. J. Biochem. 234:641-649(1995). RN [20] RP FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH F5, AND RP INTERACTION WITH SEMG2. RX PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x; RA Kise H., Nishioka J., Kawamura J., Suzuki K.; RT "Characterization of semenogelin II and its molecular interaction with RT prostate-specific antigen and protein C inhibitor."; RL Eur. J. Biochem. 238:88-96(1996). RN [21] RP FUNCTION IN BLOOD PLASMA F5 INHIBITION. RX PubMed=9473218; RA Elisen M.G., von dem Borne P.A., Bouma B.N., Meijers J.C.; RT "Protein C inhibitor acts as a procoagulant by inhibiting the RT thrombomodulin-induced activation of protein C in human plasma."; RL Blood 91:1542-1547(1998). RN [22] RP FUNCTION IN FERTILIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9510955; DOI=10.1095/biolreprod58.3.670; RA Elisen M.G., van Kooij R.J., Nolte M.A., Marquart J.A., Lock T.M., RA Bouma B.N., Meijers J.C.; RT "Protein C inhibitor may modulate human sperm-oocyte interactions."; RL Biol. Reprod. 58:670-677(1998). RN [23] RP FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9556620; DOI=10.1074/jbc.273.18.11281; RA Nishioka J., Ning M., Hayashi T., Suzuki K.; RT "Protein C inhibitor secreted from activated platelets efficiently inhibits RT activated protein C on phosphatidylethanolamine of platelet membrane and RT microvesicles."; RL J. Biol. Chem. 273:11281-11287(1998). RN [24] RP FUNCTION IN SEMINAL PLASMA SERINE PROTEASES INHIBITION, AND HETERODIMER RP WITH PLAT AND PLAU. RX PubMed=10340997; DOI=10.1093/molehr/5.6.513; RA He S., Lin Y.L., Liu Y.X.; RT "Functionally inactive protein C inhibitor in seminal plasma may be RT associated with infertility."; RL Mol. Hum. Reprod. 5:513-519(1999). RN [25] RP FUNCTION IN RETINOIC ACID TRANSPORT. RX PubMed=11722589; DOI=10.1046/j.0014-2956.2001.02560.x; RA Jerabek I., Zechmeister-Machhart M., Binder B.R., Geiger M.; RT "Binding of retinoic acid by the inhibitory serpin protein C inhibitor."; RL Eur. J. Biochem. 268:5989-5996(2001). RN [26] RP FUNCTION AS REGULATOR OF TUMOR CELL INVASION, HETERODIMER WITH PLAU, AND RP TISSUE SPECIFICITY. RX PubMed=14696115; DOI=10.1002/ijc.11594; RA Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., RA Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.; RT "Regulation of carcinoma cell invasion by protein C inhibitor whose RT expression is decreased in renal cell carcinoma."; RL Int. J. Cancer 108:516-523(2004). RN [27] RP FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS11E INHIBITION, RP HETERODIMER WITH TMPRSS11E, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF RP THR-360 AND ARG-373. RX PubMed=15328353; DOI=10.1074/jbc.m403299200; RA Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., RA Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.; RT "Mouse DESC1 is located within a cluster of seven DESC1-like genes and RT encodes a type II transmembrane serine protease that forms serpin RT inhibitory complexes."; RL J. Biol. Chem. 279:46981-46994(2004). RN [28] RP FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5, AND TISSUE RP SPECIFICITY. RX PubMed=15140131; DOI=10.1111/j.1538-7836.2004.00733.x; RA Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C., RA Ido M., Suzuki K.; RT "Characterization of a novel human protein C inhibitor (PCI) gene RT transgenic mouse useful for studying the role of PCI in physiological and RT pathological conditions."; RL J. Thromb. Haemost. 2:949-961(2004). RN [29] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249. 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 [30] 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 [31] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-262 AND ASN-338. 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 [32] RP TISSUE SPECIFICITY. RX PubMed=17706750; DOI=10.1016/j.acthis.2007.04.007; RA Zhang C., Li X., Lian X., Wang Y., Zeng Y., Yang K., Yu J., Gao Q., RA Yang T.; RT "Immunolocalization of protein C inhibitor in differentiation of human RT epidermal keratinocytes."; RL Acta Histochem. 109:461-467(2007). RN [33] RP FUNCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-249; ASN-262 AND RP ASN-338, STRUCTURE OF CARBOHYDRATES, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18467335; DOI=10.1074/jbc.m800608200; RA Sun W., Parry S., Panico M., Morris H.R., Kjellberg M., Engstrom A., RA Dell A., Schedin-Weiss S.; RT "N-glycans and the N terminus of protein C inhibitor affect the cofactor- RT enhanced rates of thrombin inhibition."; RL J. Biol. Chem. 283:18601-18611(2008). RN [34] RP MUTAGENESIS OF ARG-253; GLU-272; LYS-274; LYS-285; ARG-288; LYS-289; RP LYS-292 AND ARG-381. 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 [35] RP GLYCOSYLATION AT THR-39, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=21056543; DOI=10.1016/j.bbrc.2010.11.005; RA Sun W., Parry S., Ubhayasekera W., Engstrom A., Dell A., Schedin-Weiss S.; RT "Further insight into the roles of the glycans attached to human blood RT protein C inhibitor."; RL Biochem. Biophys. Res. Commun. 403:198-202(2010). RN [36] RP GLYCOSYLATION AT THR-39, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY RP 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 [37] RP 3D-STRUCTURE MODELING. RX PubMed=2172989; DOI=10.1073/pnas.87.21.8506; RA Kuhn L.A., Griffin J.H., Fisher C.L., Greengard J.S., Bouma B.N., RA Espana F., Tainer J.A.; RT "Elucidating the structural chemistry of glycosaminoglycan recognition by RT protein C inhibitor."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8506-8510(1990). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-406, AND GLYCOSYLATION AT RP ASN-262. RX PubMed=12575940; DOI=10.1016/s0969-2126(02)00944-9; RA Huntington J.A., Kjellberg M., Stenflo J.; RT "Crystal structure of protein C inhibitor provides insights into hormone RT binding and heparin activation."; RL Structure 11:205-215(2003). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 36-406. RX PubMed=17337440; DOI=10.1074/jbc.m701074200; RA Li W., Adams T.E., Kjellberg M., Stenflo J., Huntington J.A.; RT "Structure of native protein C inhibitor provides insight into its multiple RT functions."; RL J. Biol. Chem. 282:13759-13768(2007). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 37-406 IN COMPLEX WITH SYNTHETIC RP HEPARIN, HEPARIN-BINDING SITES, AND MUTAGENESIS OF ARG-248; LYS-285; RP ARG-288; LYS-289 AND LYS-292. RX PubMed=18974053; DOI=10.1074/jbc.m805974200; RA Li W., Huntington J.A.; RT "The heparin binding site of protein C inhibitor is protease-dependent."; RL J. Biol. Chem. 283:36039-36045(2008). RN [41] RP VARIANTS VAL-55; ASN-64; GLU-105; ALA-121 AND ARG-217. 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 [42] 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). CC -!- FUNCTION: Heparin-dependent serine protease inhibitor acting in body CC fluids and secretions. Inactivates serine proteases by binding CC irreversibly to their serine activation site. Involved in the CC regulation of intravascular and extravascular proteolytic activities. CC Plays hemostatic roles in the blood plasma. Acts as a procoagulant and CC pro-inflammatory factor by inhibiting the anticoagulant activated CC protein C factor as well as the generation of activated protein C CC factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant CC factor by inhibiting blood coagulation factors like prothrombin, factor CC XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as CC tissue- and urinary-type plasminogen activators. In seminal plasma, CC inactivates several serine proteases implicated in the reproductive CC system. Inhibits the serpin acrosin; indirectly protects component of CC the male genital tract from being degraded by excessive released CC acrosin. Inhibits tissue- and urinary-type plasminogen activator, CC prostate-specific antigen and kallikrein activities; has a control on CC the sperm motility and fertilization. Inhibits the activated protein C- CC catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of CC semenogelin during the process of transfer of spermatozoa from the male CC reproductive tract into the female tract. In urine, inhibits urinary- CC type plasminogen activator and kallikrein activities. Inactivates CC membrane-anchored serine proteases activities such as MPRSS7 and CC TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor CC cell invasion and metastasis. May also play a non-inhibitory role in CC seminal plasma and urine as a hydrophobic hormone carrier by its CC binding to retinoic acid. {ECO:0000269|PubMed:10340997, CC ECO:0000269|PubMed:11722589, ECO:0000269|PubMed:14696115, CC ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:15328353, CC ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:1725227, CC ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:2844223, CC ECO:0000269|PubMed:3501295, ECO:0000269|PubMed:6323392, CC ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:7548057, CC ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:8665956, CC ECO:0000269|PubMed:9473218, ECO:0000269|PubMed:9510955, CC ECO:0000269|PubMed:9556620}. CC -!- ACTIVITY REGULATION: Its inhibitory activity is greatly enhanced in the CC presence of glycosaminoglycans, heparin, thrombomodulin and CC phospholipids vesicles. CC -!- SUBUNIT: Forms protease inhibiting heterodimers in extracellular body CC fluids with serine proteases such as activated protein C/coagulation CC factor V/F5, acrosin/ACR, chymotrypsinogen B/CTRB1, prothrombin/F2, CC factor Xa/F10, factor XI/F11, kallikrein/KLKB1, tissue kallikrein, CC trypsin/PRSS1, prostate specific antigen/KLK3, tissue plasminogen CC activator/PLAT and urinary plasminogen activator/PLAU. Forms membrane- CC anchored serine proteases inhibiting heterodimers with TMPRSS7 and CC TMPRSS11E. Interacts with SEMG2. {ECO:0000269|PubMed:18974053, CC ECO:0000269|PubMed:8665956}. CC -!- INTERACTION: CC P05154; P02751: FN1; NbExp=3; IntAct=EBI-722597, EBI-1220319; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335, CC ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:8536714, CC ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}. Note=Localized CC on the plasma membrane overlying the acrosomal head of spermatozoa of CC ependymal spermatozoa and ejaculated sperm. Localized at the equatorial CC segment of acrosome-reacted spermatozoa. Localized in alpha granules in CC resting platelets and on the external plasma membrane and within the CC surface-connected cannalicular system in activated platelets. CC -!- TISSUE SPECIFICITY: Predominantly expressed in the epithelium of CC seminal vesicles. Expressed in the proximal tubular epithelium of the CC kidney. Expressed in the superficial and more differentiated epidermal CC keratinocytes of the skin. Expressed in megakaryocytes and platelets. CC Expressed poorly in kidney tumor cells compared to non tumor kidney CC tissues. Expressed in spermatozoa. Present in very high concentration CC in seminal plasma. Present in high concentration in plasma, synovial CC and Graaf follicle fluids. Present in low concentration in breast milk CC and in amniotic fluids. Present in very low concentration in urine, CC cerebrospinal fluids, saliva and tears (at protein level). Strongly CC expressed in liver. Expressed in kidney, spleen, pancreas, skeletal CC muscle, heart, testes, ovary, interstitial Leydig cells, epididymal CC glands, seminal vesicles and prostate. {ECO:0000269|PubMed:1372913, CC ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:15140131, CC ECO:0000269|PubMed:17706750, ECO:0000269|PubMed:18467335, CC ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the CC protein and directs binding to the target protease. The protease CC cleaves the serpin at the reactive site within the RCL, establishing a CC covalent linkage between the carboxyl group of the serpin reactive site CC and the serine hydroxyl of the protease. The resulting inactive serpin- CC protease complex is highly stable. CC -!- PTM: N- and O-glycosylated. N-glycosylation consists of a mixture of CC sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra- CC antennary complex-type chains; affects the maximal heparin- and CC thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated CC with core 1 or possibly core 8 glycans. Further modified with 2 sialic CC acid residues. {ECO:0000269|PubMed:12575940, CC ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:21056543, CC ECO:0000269|PubMed:22171320}. CC -!- PTM: Proteolytically cleaved. Inhibition of proteases is accompanied by CC formation of a stable enzyme-inhibitor complex and by degradation of CC the serpin to lower molecular weight derivatives. Proteolytically CC cleaved at the N-terminus; inhibits slightly the heparin- and CC thrombomodulin-enhanced rates of thrombin inhibition. CC {ECO:0000269|PubMed:15328353, ECO:0000269|PubMed:18467335}. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/serpina5/"; 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; J02639; AAA35688.1; -; mRNA. DR EMBL; M68516; AAA02811.1; -; Genomic_DNA. DR EMBL; S69366; AAB30461.1; -; Genomic_DNA. DR EMBL; S69364; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; S69574; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; S69365; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; U35464; AAB60386.1; -; mRNA. DR EMBL; AF361796; AAK27240.1; -; Genomic_DNA. DR EMBL; AL049839; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008915; AAH08915.1; -; mRNA. DR EMBL; S58545; AAB26244.2; -; mRNA. DR EMBL; AL080185; CAB45766.1; -; mRNA. DR CCDS; CCDS9928.1; -. DR PIR; A39339; A39339. DR RefSeq; NP_000615.3; NM_000624.5. DR PDB; 1LQ8; X-ray; 2.40 A; A/C/E/G=30-375, B/D/F/H=376-406. DR PDB; 2HI9; X-ray; 2.30 A; A/B/C=44-406. DR PDB; 2OL2; X-ray; 2.00 A; A/B=36-406. DR PDB; 3DY0; X-ray; 1.55 A; A=37-372, B=379-406. DR PDBsum; 1LQ8; -. DR PDBsum; 2HI9; -. DR PDBsum; 2OL2; -. DR PDBsum; 3DY0; -. DR AlphaFoldDB; P05154; -. DR SMR; P05154; -. DR BioGRID; 111135; 33. DR CORUM; P05154; -. DR DIP; DIP-29869N; -. DR IntAct; P05154; 55. DR MINT; P05154; -. DR STRING; 9606.ENSP00000333203; -. DR BindingDB; P05154; -. DR DrugBank; DB00055; Drotrecogin alfa. DR DrugBank; DB05961; PPL-100. DR DrugBank; DB05413; Tifuvirtide. DR DrugBank; DB00013; Urokinase. DR MEROPS; I04.004; -. DR GlyConnect; 663; 12 N-Linked glycans (1 site), 1 O-Linked glycan (1 site). DR GlyCosmos; P05154; 4 sites, 19 glycans. DR GlyGen; P05154; 5 sites, 19 N-linked glycans (1 site), 3 O-linked glycans (2 sites). DR iPTMnet; P05154; -. DR PhosphoSitePlus; P05154; -. DR BioMuta; SERPINA5; -. DR DMDM; 322510122; -. DR CPTAC; non-CPTAC-1149; -. DR EPD; P05154; -. DR jPOST; P05154; -. DR MassIVE; P05154; -. DR MaxQB; P05154; -. DR PaxDb; 9606-ENSP00000333203; -. DR PeptideAtlas; P05154; -. DR ProteomicsDB; 51805; -. DR Antibodypedia; 27096; 624 antibodies from 34 providers. DR DNASU; 5104; -. DR Ensembl; ENST00000329597.12; ENSP00000333203.7; ENSG00000188488.14. DR Ensembl; ENST00000553780.5; ENSP00000450837.1; ENSG00000188488.14. DR Ensembl; ENST00000554276.1; ENSP00000451610.1; ENSG00000188488.14. DR Ensembl; ENST00000554866.5; ENSP00000451126.1; ENSG00000188488.14. DR GeneID; 5104; -. DR KEGG; hsa:5104; -. DR MANE-Select; ENST00000329597.12; ENSP00000333203.7; NM_000624.6; NP_000615.3. DR UCSC; uc001ydm.3; human. DR AGR; HGNC:8723; -. DR CTD; 5104; -. DR DisGeNET; 5104; -. DR GeneCards; SERPINA5; -. DR HGNC; HGNC:8723; SERPINA5. DR HPA; ENSG00000188488; Tissue enhanced (adrenal gland, liver, testis). DR MIM; 601841; gene. DR neXtProt; NX_P05154; -. DR OpenTargets; ENSG00000188488; -. DR VEuPathDB; HostDB:ENSG00000188488; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000162217; -. DR HOGENOM; CLU_023330_2_1_1; -. DR InParanoid; P05154; -. DR OMA; QVPMMNR; -. DR OrthoDB; 3218836at2759; -. DR PhylomeDB; P05154; -. DR TreeFam; TF343201; -. DR PathwayCommons; P05154; -. DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation. DR SABIO-RK; P05154; -. DR SignaLink; P05154; -. DR SIGNOR; P05154; -. DR BioGRID-ORCS; 5104; 18 hits in 1156 CRISPR screens. DR ChiTaRS; SERPINA5; human. DR EvolutionaryTrace; P05154; -. DR GeneWiki; Protein_C_inhibitor; -. DR GenomeRNAi; 5104; -. DR Pharos; P05154; Tbio. DR PRO; PR:P05154; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P05154; Protein. DR Bgee; ENSG00000188488; Expressed in right adrenal gland cortex and 146 other cell types or tissues. DR ExpressionAtlas; P05154; baseline and differential. DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB. DR GO; GO:0031094; C:platelet dense tubular network; IDA:UniProtKB. DR GO; GO:0097181; C:protein C inhibitor-coagulation factor V complex; IDA:UniProtKB. DR GO; GO:0097182; C:protein C inhibitor-coagulation factor Xa complex; IDA:UniProtKB. DR GO; GO:0097183; C:protein C inhibitor-coagulation factor XI complex; IDA:UniProtKB. DR GO; GO:0036029; C:protein C inhibitor-KLK3 complex; IDA:UniProtKB. DR GO; GO:0036030; C:protein C inhibitor-plasma kallikrein complex; IDA:UniProtKB. DR GO; GO:0036026; C:protein C inhibitor-PLAT complex; IDA:UniProtKB. DR GO; GO:0036027; C:protein C inhibitor-PLAU complex; IDA:UniProtKB. DR GO; GO:0036028; C:protein C inhibitor-thrombin complex; IDA:UniProtKB. DR GO; GO:0036025; C:protein C inhibitor-TMPRSS11E complex; IDA:UniProtKB. DR GO; GO:0036024; C:protein C inhibitor-TMPRSS7 complex; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0032190; F:acrosin binding; IPI:UniProtKB. DR GO; GO:0005539; F:glycosaminoglycan binding; TAS:UniProtKB. DR GO; GO:0008201; F:heparin binding; TAS:UniProtKB. DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; NAS:UniProtKB. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:UniProtKB. DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl. DR GO; GO:0061107; P:seminal vesicle development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR CDD; cd19553; serpinA5_PCI; 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; 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:SF274; PLASMA SERINE PROTEASE INHIBITOR; 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 Genevisible; P05154; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Fertilization; Glycoprotein; KW Heparin-binding; Lipid transport; Protease inhibitor; Reference proteome; KW Secreted; Serine protease inhibitor; Signal; Transport. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:2556811" FT PROPEP 20..25 FT /note="Removed in mature form" FT /id="PRO_0000414091" FT CHAIN 26..406 FT /note="Plasma serine protease inhibitor" FT /id="PRO_0000032427" FT SITE 373..374 FT /note="Reactive bond" FT CARBOHYD 39 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:21056543, FT ECO:0000269|PubMed:22171320" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:18467335" FT CARBOHYD 262 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12575940, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18467335" FT CARBOHYD 338 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:18467335" FT VARIANT 44 FT /note="S -> G (in dbSNP:rs2069975)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_013080" FT VARIANT 55 FT /note="A -> V (in allele PCI*B; dbSNP:rs6118)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:8713781, ECO:0000269|Ref.6" FT /id="VAR_007100" FT VARIANT 64 FT /note="S -> N (in dbSNP:rs6115)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1714450, FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:2173165, FT ECO:0000269|PubMed:3027058, ECO:0000269|PubMed:8471250, FT ECO:0000269|PubMed:8713781, ECO:0000269|Ref.6" FT /id="VAR_013081" FT VARIANT 94 FT /note="G -> V (in dbSNP:rs2069976)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_013082" FT VARIANT 105 FT /note="K -> E (in allele PCI*B; dbSNP:rs6119)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:8713781, ECO:0000269|Ref.6" FT /id="VAR_007101" FT VARIANT 115 FT /note="L -> P (in dbSNP:rs2069999)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_013083" FT VARIANT 121 FT /note="P -> A (in dbSNP:rs6120)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013900" FT VARIANT 217 FT /note="G -> R (in dbSNP:rs6114)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.6" FT /id="VAR_013084" FT MUTAGEN 248 FT /note="R->E: Does not change the rate of thrombin or FT activated protein C/F5 inhibition in the presence or FT absence of heparin. Strongly reduces the rate of thrombin FT inhibition in the presence of heparin." FT /evidence="ECO:0000269|PubMed:18974053" FT MUTAGEN 253 FT /note="R->E: Inhibits strongly thrombomodulin-enhanced rate FT of thrombin inhibition in presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344" FT MUTAGEN 272 FT /note="E->K: Does not inhibit thrombomodulin-enhanced rate FT of thrombin inhibition in presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344" FT MUTAGEN 274 FT /note="K->E: Does not inhibit thrombomodulin-enhanced rate FT of thrombin inhibition in presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344" FT MUTAGEN 285 FT /note="K->E: Does not change the rate of thrombin or FT activated protein C/F5 inhibition in the presence or FT absence of heparin. Slightly reduces the rate of thrombin FT inhibition in the presence of heparin. Does not inhibit FT thrombomodulin-enhanced rate of thrombin inhibition in FT presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344, FT ECO:0000269|PubMed:18974053" FT MUTAGEN 288 FT /note="R->E: Does not change the rate of thrombin or FT activated protein C/F5 inhibition in the presence or FT absence of heparin. Slightly reduces the rate of thrombin FT inhibition in the presence of heparin. Does not inhibit FT thrombomodulin-enhanced rate of thrombin inhibition in FT presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344, FT ECO:0000269|PubMed:18974053" FT MUTAGEN 289 FT /note="K->E: Does not change the rate of thrombin or FT activated protein C/F5 inhibition in the presence or FT absence of heparin. Slightly reduces the rate of thrombin FT inhibition in the presence of heparin. Inhibits weakly FT thrombomodulin-enhanced rate of thrombin inhibition in FT presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344, FT ECO:0000269|PubMed:18974053" FT MUTAGEN 292 FT /note="K->E: Does not change the rate of thrombin or FT activated protein C/F5 inhibition in the presence or FT absence of heparin. Slightly reduces the rate of thrombin FT inhibition in the presence of heparin. Does not inhibit FT thrombomodulin-enhanced rate of thrombin inhibition in FT presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344, FT ECO:0000269|PubMed:18974053" FT MUTAGEN 360 FT /note="T->R: Inhibits heterodimer formation with FT TMPRSS11E." FT /evidence="ECO:0000269|PubMed:15328353" FT MUTAGEN 371 FT /note="T->R: Increases inhibition of activated protein C/F5 FT and factor XI/F11 activities. Decreases inhibition of FT thrombin activity." FT /evidence="ECO:0000269|PubMed:7548057" FT MUTAGEN 372 FT /note="F->P,G: Increases inhibition of thrombin activity." FT /evidence="ECO:0000269|PubMed:7548057" FT MUTAGEN 373 FT /note="R->P: Increases inhibition of thrombin activity. FT Inhibits heterodimer formation with TMPRSS11E." FT /evidence="ECO:0000269|PubMed:15328353, FT ECO:0000269|PubMed:7548057" FT MUTAGEN 376 FT /note="R->P: Does not change inhibition of thrombin, FT activated protein C/F5 and factor XI/F11 activities." FT /evidence="ECO:0000269|PubMed:7548057" FT MUTAGEN 381 FT /note="R->E: Does not inhibit thrombomodulin-enhanced rate FT of thrombin inhibition in presence of heparin." FT /evidence="ECO:0000269|PubMed:18362344" FT CONFLICT 28 FT /note="K -> E (in Ref. 10; CAB45766)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="Q -> L (in Ref. 9; AAB26244)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="G -> R (in Ref. 1; AAA35688 and 9; AAB26244)" FT /evidence="ECO:0000305" FT CONFLICT 384 FT /note="F -> S (in Ref. 9; AAB26244)" FT /evidence="ECO:0000305" FT HELIX 48..59 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 69..81 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 85..94 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 101..117 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 123..135 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 143..153 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 165..179 FT /evidence="ECO:0007829|PDB:3DY0" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 195..211 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 219..228 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 230..247 FT /evidence="ECO:0007829|PDB:3DY0" FT TURN 248..251 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 252..262 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 264..270 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 284..293 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 295..304 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 306..313 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:3DY0" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:3DY0" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:1LQ8" FT STRAND 343..355 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 357..371 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:2OL2" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:3DY0" FT STRAND 388..404 FT /evidence="ECO:0007829|PDB:3DY0" SQ SEQUENCE 406 AA; 45675 MW; 2A8FF3DC33C77E04 CRC64; MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF DLYRALASAA PSQSIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ KSSEKELHRG FQQLLQELNQ PRDGFQLSLG NALFTDLVVD LQDTFVSAMK TLYLADTFPT NFRDSAGAMK QINDYVAKQT KGKIVDLLKN LDSNAVVIMV NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED QYHYLLDRNL SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK AVVEVDESGT RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL GKVNRP //