PAI1_HUMAN
ID PAI1_HUMAN Reviewed; 402 AA.
AC P05121; B7Z4S0; F8WD53;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 243.
DE RecName: Full=Plasminogen activator inhibitor 1;
DE Short=PAI;
DE Short=PAI-1;
DE AltName: Full=Endothelial plasminogen activator inhibitor;
DE AltName: Full=Serpin E1;
DE Flags: Precursor;
GN Name=SERPINE1; Synonyms=PAI1, PLANH1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=2430793; DOI=10.1002/j.1460-2075.1986.tb04532.x;
RA Pannekoek H., Veerman H., Lambers H., Diergaarde P., Verweij C.L.,
RA van Zonneveld A.-J., van Mourik J.A.;
RT "Endothelial plasminogen activator inhibitor (PAI): a new member of the
RT Serpin gene family.";
RL EMBO J. 5:2539-2544(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2820474; DOI=10.1021/bi00387a004;
RA Loskutoff D.J., Linders M., Keijer J., Veerman H., van Heerikhuizen H.,
RA Pannekoek H.;
RT "Structure of the human plasminogen activator inhibitor 1 gene: nonrandom
RT distribution of introns.";
RL Biochemistry 26:3763-3768(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=3097076; DOI=10.1172/jci112761;
RA Ginsburg D., Zeheb R., Yang A.Y., Rafferty U.M., Andreasen P.A.,
RA Nielsen L., Dano K., Lebo R.V., Gelehrter T.D.;
RT "cDNA cloning of human plasminogen activator-inhibitor from endothelial
RT cells.";
RL J. Clin. Invest. 78:1673-1680(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2612914; DOI=10.1016/0378-1119(89)90519-2;
RA Follo M., Ginsburg D.;
RT "Structure and expression of the human gene encoding plasminogen activator
RT inhibitor, PAI-1.";
RL Gene 84:447-453(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3262512; DOI=10.1111/j.1432-1033.1988.tb14320.x;
RA Strandberg L., Lawrence D., Ny T.;
RT "The organization of the human-plasminogen-activator-inhibitor-1 gene.
RT Implications on the evolution of the serine-protease inhibitor family.";
RL Eur. J. Biochem. 176:609-616(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3132455; DOI=10.1016/s0021-9258(19)76517-x;
RA Bosma P.J., van den Berg E.A., Kooistra T., Siemieniak D.R., Slightom J.L.;
RT "Human plasminogen activator inhibitor-1 gene. Promoter and structural gene
RT nucleotide sequences.";
RL J. Biol. Chem. 263:9129-9141(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Pannekoek H.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-15; ILE-17; PRO-25;
RP HIS-209 AND ASN-255.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-402 (ISOFORM 1).
RX PubMed=3092219; DOI=10.1073/pnas.83.18.6776;
RA Ny T., Sawdey M., Lawrence D., Millan J.L., Loskutoff D.J.;
RT "Cloning and sequence of a cDNA coding for the human beta-migrating
RT endothelial-cell-type plasminogen activator inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6776-6780(1986).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 AND 364-402 (ISOFORM 1).
RX PubMed=3025016; DOI=10.1016/0014-5793(86)81113-9;
RA Andreasen P.A., Riccio A., Welinder K.G., Douglas R., Sartorio R.,
RA Nielsen L.S., Oppenheimer C., Blasi F., Danoe K.;
RT "Plasminogen activator inhibitor type-1: reactive center and amino-terminal
RT heterogeneity determined by protein and cDNA sequencing.";
RL FEBS Lett. 209:213-218(1986).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-402 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=3026837; DOI=10.1016/0014-5793(87)81288-7;
RA Wun T.C., Kretzmer K.K.;
RT "cDNA cloning and expression in E. coli of a plasminogen activator
RT inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell.";
RL FEBS Lett. 210:11-16(1987).
RN [15]
RP FUNCTION, AND INVOLVEMENT IN PAI-1D.
RX PubMed=8481516;
RA Lee M.H., Vosburgh E., Anderson K., McDonagh J.;
RT "Deficiency of plasma plasminogen activator inhibitor 1 results in
RT hyperfibrinolytic bleeding.";
RL Blood 81:2357-2362(1993).
RN [16]
RP INTERACTION WITH VTN.
RX PubMed=7522053; DOI=10.1016/0167-4838(94)90166-x;
RA Sigurdardottir O., Wiman B.;
RT "Identification of a PAI-1 binding site in vitronectin.";
RL Biochim. Biophys. Acta 1208:104-110(1994).
RN [17]
RP FUNCTION, AND INVOLVEMENT IN PAI-1D.
RX PubMed=9207454;
RA Fay W.P., Parker A.C., Condrey L.R., Shapiro A.D.;
RT "Human plasminogen activator inhibitor-1 (PAI-1) deficiency:
RT characterization of a large kindred with a null mutation in the PAI-1
RT gene.";
RL Blood 90:204-208(1997).
RN [18]
RP FUNCTION.
RX PubMed=9168821; DOI=10.1006/excr.1997.3540;
RA Kjoeller L., Kanse S.M., Kirkegaard T., Rodenburg K.W., Roenne E.,
RA Goodman S.L., Preissner K.T., Ossowski L., Andreasen P.A.;
RT "Plasminogen activator inhibitor-1 represses integrin- and vitronectin-
RT mediated cell migration independently of its function as an inhibitor of
RT plasminogen activation.";
RL Exp. Cell Res. 232:420-429(1997).
RN [19]
RP FUNCTION.
RX PubMed=9175705; DOI=10.1242/jcs.110.9.1091;
RA Planus E., Barlovatz-Meimon G., Rogers R.A., Bonavaud S., Ingber D.E.,
RA Wang N.;
RT "Binding of urokinase to plasminogen activator inhibitor type-1 mediates
RT cell adhesion and spreading.";
RL J. Cell Sci. 110:1091-1098(1997).
RN [20]
RP INTERACTION WITH LRP1B.
RX PubMed=11384978; DOI=10.1074/jbc.m102727200;
RA Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
RT "The putative tumor suppressor LRP1B, a novel member of the low density
RT lipoprotein (LDL) receptor family, exhibits both overlapping and distinct
RT properties with the LDL receptor-related protein.";
RL J. Biol. Chem. 276:28889-28896(2001).
RN [21]
RP INTERACTION WITH LRP1; PLAT; PLAU; PLAUR AND SORL1.
RX PubMed=15053742; DOI=10.1042/bj20040149;
RA Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C.,
RA Andreasen P.A.;
RT "The mosaic receptor sorLA/LR11 binds components of the plasminogen-
RT activating system and platelet-derived growth factor-BB similarly to LRP1
RT (low-density lipoprotein receptor-related protein), but mediates slow
RT internalization of bound ligand.";
RL Biochem. J. 381:203-212(2004).
RN [22]
RP FUNCTION.
RX PubMed=15001579; DOI=10.1074/jbc.m313004200;
RA Degryse B., Neels J.G., Czekay R.P., Aertgeerts K., Kamikubo Y.,
RA Loskutoff D.J.;
RT "The low density lipoprotein receptor-related protein is a motogenic
RT receptor for plasminogen activator inhibitor-1.";
RL J. Biol. Chem. 279:22595-22604(2004).
RN [23]
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 [24]
RP FUNCTION.
RX PubMed=16862142; DOI=10.1038/ncb1448;
RA Kortlever R.M., Higgins P.J., Bernards R.;
RT "Plasminogen activator inhibitor-1 is a critical downstream target of p53
RT in the induction of replicative senescence.";
RL Nat. Cell Biol. 8:877-884(2006).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF GLN-197 AND GLY-355.
RX PubMed=17912461;
RA Jankun J., Aleem A.M., Selman S.H., Skrzypczak-Jankun E.,
RA Lysiak-Szydlowska W., Grafos N., Fryer H.J., Greenfield R.S.;
RT "Highly stable plasminogen activator inhibitor type one (VLHL PAI-1)
RT protects fibrin clots from tissue plasminogen activator-mediated
RT fibrinolysis.";
RL Int. J. Mol. Med. 20:683-687(2007).
RN [26]
RP FUNCTION.
RX PubMed=18386027; DOI=10.1007/s00403-008-0845-2;
RA Providence K.M., Higgins S.P., Mullen A., Battista A., Samarakoon R.,
RA Higgins C.E., Wilkins-Port C.E., Higgins P.J.;
RT "SERPINE1 (PAI-1) is deposited into keratinocyte migration 'trails' and
RT required for optimal monolayer wound repair.";
RL Arch. Dermatol. Res. 300:303-310(2008).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [28]
RP FUNCTION.
RX PubMed=25808697; DOI=10.1089/ten.tea.2014.0399;
RA Jin H., Choung H.W., Lim K.T., Jin B., Jin C., Chung J.H., Choung P.H.;
RT "Recombinant human plasminogen activator inhibitor-1 promotes cementogenic
RT differentiation of human periodontal ligament stem cells.";
RL Tissue Eng. Part A 21:2817-2828(2015).
RN [29]
RP FUNCTION.
RX PubMed=27046084; DOI=10.1089/ten.tea.2015.0273;
RA Jin B., Choung P.H.;
RT "Recombinant human plasminogen activator inhibitor-1 accelerates
RT odontoblastic differentiation of human stem cells from apical papilla.";
RL Tissue Eng. Part A 22:721-732(2016).
RN [30]
RP INTERACTION WITH PPP1CB.
RX PubMed=28296156; DOI=10.1111/jcmm.13127;
RA Yao H., He G., Chen C., Yan S., Lu L., Song L., Vijayan K.V., Li Q.,
RA Xiong L., Miao X., Deng X.;
RT "PAI1: a novel PP1-interacting protein that mediates human plasma's anti-
RT apoptotic effect in endothelial cells.";
RL J. Cell. Mol. Med. 21:2068-2076(2017).
RN [31]
RP INVOLVEMENT IN PAI-1D.
RX PubMed=29152572; DOI=10.1126/sciadv.aao1617;
RA Khan S.S., Shah S.J., Klyachko E., Baldridge A.S., Eren M., Place A.T.,
RA Aviv A., Puterman E., Lloyd-Jones D.M., Heiman M., Miyata T., Gupta S.,
RA Shapiro A.D., Vaughan D.E.;
RT "A null mutation in SERPINE1 protects against biological aging in humans.";
RL Sci. Adv. 3:1-8(2017).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=1731226; DOI=10.1038/355270a0;
RA Mottonen J., Strand A., Symersky J., Sweet R.M., Danley D.E.,
RA Geoghegan K.F., Gerard R.D., Goldsmith E.J.;
RT "Structural basis of latency in plasminogen activator inhibitor-1.";
RL Nature 355:270-273(1992).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7552714; DOI=10.1038/nsb1095-891;
RA Aertgeerts K., de Bondt H.L., de Ranter C.J., Declerck P.J.;
RT "Mechanisms contributing to the conformational and functional flexibility
RT of plasminogen activator inhibitor-1.";
RL Nat. Struct. Biol. 2:891-897(1995).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=9634700; DOI=10.1016/s0969-2126(98)00064-1;
RA Xue Y., Bjoerquist P., Inghardt T., Linschoten M., Musil D., Sjoelin L.,
RA Deinum J.;
RT "Interfering with the inhibitory mechanism of serpins: crystal structure of
RT a complex formed between cleaved plasminogen activator inhibitor type 1 and
RT a reactive-centre loop peptide.";
RL Structure 6:627-636(1998).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS).
RX PubMed=10368279; DOI=10.1016/s0969-2126(99)80018-5;
RA Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B.,
RA Ginsburg D., Lawrence D.A., Read R.J.;
RT "The active conformation of plasminogen activator inhibitor 1, a target for
RT drugs to control fibrinolysis and cell adhesion.";
RL Structure 7:111-118(1999).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10731421; DOI=10.1006/jmbi.2000.3604;
RA Nar H., Bauer M., Stassen J.M., Lang D., Gils A., Declerck P.J.;
RT "Plasminogen activator inhibitor 1. Structure of the native serpin,
RT comparison to its other conformers and implications for serpin
RT inactivation.";
RL J. Mol. Biol. 297:683-695(2000).
RN [37]
RP VARIANT THR-15.
RX PubMed=9194591; DOI=10.1002/elps.1150180505;
RA Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W.,
RA Creutzburg S., Graeff H., Magdolen V.;
RT "Mutational analysis of the genes encoding urokinase-type plasminogen
RT activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer.";
RL Electrophoresis 18:686-689(1997).
RN [38]
RP VARIANTS THR-15 AND ILE-17.
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 [39]
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: Serine protease inhibitor. Inhibits TMPRSS7
CC (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen
CC activator (PLAT) and urokinase-type plasminogen activator (PLAU). As
CC PLAT inhibitor, it is required for fibrinolysis down-regulation and is
CC responsible for the controlled degradation of blood clots
CC (PubMed:8481516, PubMed:9207454, PubMed:17912461). As PLAU inhibitor,
CC it is involved in the regulation of cell adhesion and spreading
CC (PubMed:9175705). Acts as a regulator of cell migration, independently
CC of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It
CC is required for stimulation of keratinocyte migration during cutaneous
CC injury repair (PubMed:18386027). It is involved in cellular and
CC replicative senescence (PubMed:16862142). Plays a role in alveolar type
CC 2 cells senescence in the lung (By similarity). Is involved in the
CC regulation of cementogenic differentiation of periodontal ligament stem
CC cells, and regulates odontoblast differentiation and dentin formation
CC during odontogenesis (PubMed:25808697, PubMed:27046084).
CC {ECO:0000250|UniProtKB:P22777, ECO:0000269|PubMed:15001579,
CC ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:16862142,
CC ECO:0000269|PubMed:17912461, ECO:0000269|PubMed:18386027,
CC ECO:0000269|PubMed:25808697, ECO:0000269|PubMed:27046084,
CC ECO:0000269|PubMed:8481516, ECO:0000269|PubMed:9168821,
CC ECO:0000269|PubMed:9175705, ECO:0000269|PubMed:9207454}.
CC -!- SUBUNIT: Forms a heterodimer with TMPRSS7 (PubMed:15853774). Interacts
CC with VTN (PubMed:7522053). Binds LRP1B; binding is followed by
CC internalization and degradation (PubMed:11384978). Interacts with
CC PPP1CB (PubMed:28296156). In complex with PLAU/uPA, interacts with
CC PLAUR/uPAR (PubMed:15053742). Interacts with SORL1 and LRP1, either
CC alone or in complex with PLAU; these interactions are abolished in the
CC presence of LRPAP1/RAP (PubMed:15053742). The ternary complex composed
CC of PLAUR-PLAU-PAI1 also interacts with SORL1 (PubMed:15053742). Also
CC interacts with SORL1, when complexed to PLAT/tPA (PubMed:15053742).
CC {ECO:0000269|PubMed:11384978, ECO:0000269|PubMed:15053742,
CC ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:28296156,
CC ECO:0000269|PubMed:7522053}.
CC -!- INTERACTION:
CC P05121; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-953978, EBI-1052304;
CC P05121; P02763: ORM1; NbExp=4; IntAct=EBI-953978, EBI-976767;
CC P05121; P78337: PITX1; NbExp=3; IntAct=EBI-953978, EBI-748265;
CC P05121; O43765: SGTA; NbExp=6; IntAct=EBI-953978, EBI-347996;
CC P05121; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-953978, EBI-744081;
CC P05121; O43711: TLX3; NbExp=3; IntAct=EBI-953978, EBI-3939165;
CC P05121; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-953978, EBI-10982110;
CC P05121; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-741480;
CC P05121; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-953978, EBI-10173939;
CC P05121; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-953978, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2430793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05121-2; Sequence=VSP_045493;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells (PubMed:2430793,
CC PubMed:3097076). Found in plasma, platelets, and hepatoma and
CC fibrosarcoma cells. {ECO:0000269|PubMed:2430793,
CC ECO:0000269|PubMed:3097076}.
CC -!- PTM: Inactivated by proteolytic attack of the urokinase-type (u-PA) and
CC the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.
CC -!- DISEASE: Plasminogen activator inhibitor-1 deficiency (PAI-1D)
CC [MIM:613329]: A hematologic disorder characterized by increased
CC bleeding after trauma, injury, or surgery. Affected females have
CC menorrhagia. The bleeding defect is due to increased fibrinolysis of
CC fibrin blood clots due to deficiency of plasminogen activator
CC inhibitor-1, which inhibits tissue and urinary activators of
CC plasminogen. {ECO:0000269|PubMed:8481516, ECO:0000269|PubMed:9207454}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry. A rare PAI-1D mutation resulting in a frameshift and
CC protein truncation has been found in an Old Order Amish community.
CC Homozygous mutation carriers suffer from episodes of major hemorrhage,
CC while heterozygous carriers do not manifest abnormal bleeding
CC (PubMed:9207454). Heterozygosity for the mutation is associated with
CC longer leukocyte telomere length, lower fasting insulin levels, lower
CC prevalence of diabetes mellitus, and a longer life span
CC (PubMed:29152572). {ECO:0000269|PubMed:29152572,
CC ECO:0000269|PubMed:9207454}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Plasminogen activator inhibitor-1
CC entry;
CC URL="https://en.wikipedia.org/wiki/Plasminogen_activator_inhibitor-1";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/serpine1/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Giving in to time - Issue
CC 203 of May 2018;
CC URL="https://web.expasy.org/spotlight/back_issues/203/";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; X04429; CAA28025.1; -; mRNA.
DR EMBL; M14083; AAA60008.1; -; mRNA.
DR EMBL; X04729; CAA28438.1; -; mRNA.
DR EMBL; X04731; CAA28442.1; -; mRNA.
DR EMBL; M16006; AAA60003.1; -; mRNA.
DR EMBL; M22321; AAA60009.1; -; Genomic_DNA.
DR EMBL; M22314; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22315; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22316; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22317; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22318; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22319; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; M22320; AAA60009.1; JOINED; Genomic_DNA.
DR EMBL; X13323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X13338; CAA31722.1; -; Genomic_DNA.
DR EMBL; X13339; CAB51639.1; -; Genomic_DNA.
DR EMBL; X13340; CAB51737.1; -; Genomic_DNA.
DR EMBL; X13341; CAB51606.1; -; Genomic_DNA.
DR EMBL; X13342; CAB51607.1; -; Genomic_DNA.
DR EMBL; X13343; CAB51738.1; -; Genomic_DNA.
DR EMBL; X13344; CAB51739.1; -; Genomic_DNA.
DR EMBL; X13345; CAA31729.1; -; Genomic_DNA.
DR EMBL; J03764; AAA60007.1; -; Genomic_DNA.
DR EMBL; X12701; CAA31208.1; -; mRNA.
DR EMBL; AF386492; AAK60338.1; -; Genomic_DNA.
DR EMBL; AK297728; BAH12656.1; -; mRNA.
DR EMBL; AC004876; AAD45828.1; -; Genomic_DNA.
DR EMBL; BC010860; AAH10860.1; -; mRNA.
DR EMBL; X04744; CAA28444.1; -; mRNA.
DR CCDS; CCDS5711.1; -. [P05121-1]
DR PIR; A28107; ITHUP1.
DR RefSeq; NP_000593.1; NM_000602.4. [P05121-1]
DR PDB; 1A7C; X-ray; 1.95 A; A=24-402.
DR PDB; 1B3K; X-ray; 2.99 A; A/B/C/D=24-402.
DR PDB; 1C5G; X-ray; 2.60 A; A=1-402.
DR PDB; 1DB2; X-ray; 2.70 A; A/B=26-402.
DR PDB; 1DVM; X-ray; 2.40 A; A/B/C/D=24-402.
DR PDB; 1DVN; X-ray; 2.10 A; A=24-402.
DR PDB; 1LJ5; X-ray; 1.80 A; A=24-402.
DR PDB; 1OC0; X-ray; 2.28 A; A=24-402.
DR PDB; 3CVM; X-ray; 2.02 A; A/B=21-402.
DR PDB; 3EOX; X-ray; 2.61 A; A=24-402.
DR PDB; 3PB1; X-ray; 2.30 A; I=24-402.
DR PDB; 3Q02; X-ray; 2.30 A; A/B=24-402.
DR PDB; 3Q03; X-ray; 2.64 A; A/B=24-402.
DR PDB; 3R4L; X-ray; 2.70 A; A=24-402.
DR PDB; 3UT3; X-ray; 2.42 A; A/B/C/D=28-402.
DR PDB; 4AQH; X-ray; 2.40 A; A/B/C=24-402.
DR PDB; 4G8O; X-ray; 2.71 A; A/B/C/D=28-402.
DR PDB; 4G8R; X-ray; 2.19 A; A/B=28-402.
DR PDB; 4IC0; X-ray; 2.32 A; A/B/C/D=24-402.
DR PDB; 5BRR; X-ray; 3.16 A; I=24-402.
DR PDB; 5ZLZ; X-ray; 3.58 A; I=29-402.
DR PDB; 6GWN; X-ray; 2.03 A; A=24-402.
DR PDB; 6GWP; X-ray; 2.28 A; A=24-402.
DR PDB; 6GWQ; X-ray; 2.32 A; A=24-402.
DR PDB; 6I8S; X-ray; 2.90 A; A/B/C/D=24-402.
DR PDB; 6ZRV; X-ray; 1.88 A; A=24-402.
DR PDB; 7AQF; X-ray; 1.77 A; A/B=24-402.
DR PDB; 7AQG; X-ray; 2.27 A; A=24-402.
DR PDB; 9PAI; X-ray; 2.70 A; A=24-369, B=370-402.
DR PDBsum; 1A7C; -.
DR PDBsum; 1B3K; -.
DR PDBsum; 1C5G; -.
DR PDBsum; 1DB2; -.
DR PDBsum; 1DVM; -.
DR PDBsum; 1DVN; -.
DR PDBsum; 1LJ5; -.
DR PDBsum; 1OC0; -.
DR PDBsum; 3CVM; -.
DR PDBsum; 3EOX; -.
DR PDBsum; 3PB1; -.
DR PDBsum; 3Q02; -.
DR PDBsum; 3Q03; -.
DR PDBsum; 3R4L; -.
DR PDBsum; 3UT3; -.
DR PDBsum; 4AQH; -.
DR PDBsum; 4G8O; -.
DR PDBsum; 4G8R; -.
DR PDBsum; 4IC0; -.
DR PDBsum; 5BRR; -.
DR PDBsum; 5ZLZ; -.
DR PDBsum; 6GWN; -.
DR PDBsum; 6GWP; -.
DR PDBsum; 6GWQ; -.
DR PDBsum; 6I8S; -.
DR PDBsum; 6ZRV; -.
DR PDBsum; 7AQF; -.
DR PDBsum; 7AQG; -.
DR PDBsum; 9PAI; -.
DR AlphaFoldDB; P05121; -.
DR SASBDB; P05121; -.
DR SMR; P05121; -.
DR BioGRID; 111091; 34.
DR ComplexPortal; CPX-475; Vitronectin-PAI-1 complex.
DR ComplexPortal; CPX-483; uPA-PAI-1 complex.
DR ComplexPortal; CPX-494; tPA-PAI-1 complex.
DR IntAct; P05121; 20.
DR MINT; P05121; -.
DR STRING; 9606.ENSP00000223095; -.
DR BindingDB; P05121; -.
DR ChEMBL; CHEMBL3475; -.
DR DrugBank; DB00009; Alteplase.
DR DrugBank; DB00029; Anistreplase.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00055; Drotrecogin alfa.
DR DrugBank; DB05254; Fibrinolysin.
DR DrugBank; DB00015; Reteplase.
DR DrugBank; DB00031; Tenecteplase.
DR DrugBank; DB00197; Troglitazone.
DR DrugBank; DB00013; Urokinase.
DR DrugCentral; P05121; -.
DR MEROPS; I04.020; -.
DR GlyConnect; 639; 4 N-Linked glycans (1 site).
DR GlyGen; P05121; 6 sites, 8 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; P05121; -.
DR PhosphoSitePlus; P05121; -.
DR BioMuta; SERPINE1; -.
DR DMDM; 129576; -.
DR OGP; P05121; -.
DR SWISS-2DPAGE; P05121; -.
DR CPTAC; non-CPTAC-1150; -.
DR EPD; P05121; -.
DR jPOST; P05121; -.
DR MassIVE; P05121; -.
DR MaxQB; P05121; -.
DR PaxDb; P05121; -.
DR PeptideAtlas; P05121; -.
DR PRIDE; P05121; -.
DR ProteomicsDB; 31379; -.
DR ProteomicsDB; 51802; -. [P05121-1]
DR ABCD; P05121; 4 sequenced antibodies.
DR Antibodypedia; 3747; 1420 antibodies from 45 providers.
DR DNASU; 5054; -.
DR Ensembl; ENST00000223095.5; ENSP00000223095.4; ENSG00000106366.9. [P05121-1]
DR GeneID; 5054; -.
DR KEGG; hsa:5054; -.
DR MANE-Select; ENST00000223095.5; ENSP00000223095.4; NM_000602.5; NP_000593.1.
DR UCSC; uc003uxt.4; human. [P05121-1]
DR CTD; 5054; -.
DR DisGeNET; 5054; -.
DR GeneCards; SERPINE1; -.
DR GeneReviews; SERPINE1; -.
DR HGNC; HGNC:8583; SERPINE1.
DR HPA; ENSG00000106366; Tissue enhanced (gallbladder, liver, placenta, urinary bladder).
DR MalaCards; SERPINE1; -.
DR MIM; 173360; gene.
DR MIM; 613329; phenotype.
DR neXtProt; NX_P05121; -.
DR OpenTargets; ENSG00000106366; -.
DR Orphanet; 465; Congenital plasminogen activator inhibitor type 1 deficiency.
DR PharmGKB; PA261; -.
DR VEuPathDB; HostDB:ENSG00000106366; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000160621; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; P05121; -.
DR OMA; AMQFKIE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P05121; -.
DR TreeFam; TF352620; -.
DR PathwayCommons; P05121; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR SignaLink; P05121; -.
DR SIGNOR; P05121; -.
DR BioGRID-ORCS; 5054; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; SERPINE1; human.
DR EvolutionaryTrace; P05121; -.
DR GeneWiki; Plasminogen_activator_inhibitor-1; -.
DR GenomeRNAi; 5054; -.
DR Pharos; P05121; Tchem.
DR PRO; PR:P05121; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P05121; protein.
DR Bgee; ENSG00000106366; Expressed in vena cava and 152 other tissues.
DR ExpressionAtlas; P05121; baseline and differential.
DR Genevisible; P05121; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:1904090; C:peptidase inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0097180; C:serine protease inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:BHF-UCL.
DR GO; GO:0097187; P:dentinogenesis; IDA:UniProtKB.
DR GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IC:BHF-UCL.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; IDA:BHF-UCL.
DR GO; GO:0061044; P:negative regulation of vascular wound healing; IGI:BHF-UCL.
DR GO; GO:0061045; P:negative regulation of wound healing; IC:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:BHF-UCL.
DR GO; GO:0035491; P:positive regulation of leukotriene production involved in inflammatory response; IMP:BHF-UCL.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IMP:BHF-UCL.
DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; IDA:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0090399; P:replicative senescence; IMP:UniProtKB.
DR DisProt; DP00320; -.
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; Alternative splicing; Direct protein sequencing;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT CHAIN 24..402
FT /note="Plasminogen activator inhibitor 1"
FT /id="PRO_0000032499"
FT SITE 369..370
FT /note="Reactive bond"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 31..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045493"
FT VARIANT 15
FT /note="A -> T (in dbSNP:rs6092)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:9194591, ECO:0000269|Ref.8"
FT /id="VAR_007099"
FT VARIANT 17
FT /note="V -> I (in dbSNP:rs6090)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.8"
FT /id="VAR_011750"
FT VARIANT 25
FT /note="H -> P (in dbSNP:rs2227647)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_013086"
FT VARIANT 209
FT /note="R -> H (in dbSNP:rs2227669)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_013087"
FT VARIANT 255
FT /note="T -> N (in dbSNP:rs2227685)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_013088"
FT MUTAGEN 197
FT /note="Q->C: Increased half-life of the active form when
FT associated with C-355."
FT /evidence="ECO:0000269|PubMed:17912461"
FT MUTAGEN 355
FT /note="G->C: Increased half-life of the active form when
FT associated with C-197."
FT /evidence="ECO:0000269|PubMed:17912461"
FT CONFLICT 53
FT /note="R -> A (in Ref. 7; CAA31208)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> L (in Ref. 2; AAA60009)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> V (in Ref. 7; CAA31208)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="R -> K (in Ref. 7; CAA31208)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> V (in Ref. 9; BAH12656)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..282
FT /note="QLI -> HVM (in Ref. 7; CAA31208)"
FT /evidence="ECO:0000305"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1DB2"
FT HELIX 30..48
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6ZRV"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1LJ5"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6ZRV"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3UT3"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:9PAI"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1C5G"
FT STRAND 219..237
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1C5G"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:7AQF"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1LJ5"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 353..368
FT /evidence="ECO:0007829|PDB:1LJ5"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:7AQF"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:7AQF"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:7AQF"
SQ SEQUENCE 402 AA; 45060 MW; A2E181ED28DD6082 CRC64;
MQMSPALTCL VLGLALVFGE GSAVHHPPSY VAHLASDFGV RVFQQVAQAS KDRNVVFSPY
GVASVLAMLQ LTTGGETQQQ IQAAMGFKID DKGMAPALRH LYKELMGPWN KDEISTTDAI
FVQRDLKLVQ GFMPHFFRLF RSTVKQVDFS EVERARFIIN DWVKTHTKGM ISNLLGKGAV
DQLTRLVLVN ALYFNGQWKT PFPDSSTHRR LFHKSDGSTV SVPMMAQTNK FNYTEFTTPD
GHYYDILELP YHGDTLSMFI AAPYEKEVPL SALTNILSAQ LISHWKGNMT RLPRLLVLPK
FSLETEVDLR KPLENLGMTD MFRQFQADFT SLSDQEPLHV AQALQKVKIE VNESGTVASS
STAVIVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM EP
