IPSP_HUMAN
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 03-AUG-2022, entry version 225.
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/";
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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; 32.
DR CORUM; P05154; -.
DR DIP; DIP-29869N; -.
DR IntAct; P05154; 55.
DR MINT; P05154; -.
DR STRING; 9606.ENSP00000333203; -.
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 GlyGen; P05154; 4 sites, 19 N-linked glycans (1 site), 2 O-linked glycans (1 site).
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; P05154; -.
DR PeptideAtlas; P05154; -.
DR PRIDE; P05154; -.
DR ProteomicsDB; 51805; -.
DR Antibodypedia; 27096; 541 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 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; YYYFLDR; -.
DR OrthoDB; 755773at2759; -.
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; 17 hits in 1078 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 144 other tissues.
DR ExpressionAtlas; P05154; baseline and differential.
DR Genevisible; P05154; HS.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
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
