ID   I3WWD7_ONCMY            Unreviewed;       391 AA.
AC   I3WWD7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Plasminogen activator inhibitor 1 {ECO:0000256|ARBA:ARBA00040523};
DE   AltName: Full=Endothelial plasminogen activator inhibitor {ECO:0000256|ARBA:ARBA00041825};
DE   AltName: Full=Serpin E1 {ECO:0000256|ARBA:ARBA00043166};
GN   Name=serpine1 {ECO:0000313|EMBL:AFL47815.1};
GN   Synonyms=PAI {ECO:0000313|EMBL:AFL47815.1}, PAI-1
GN   {ECO:0000313|EMBL:AFL47815.1}, PAI1 {ECO:0000313|EMBL:AFL47815.1},
GN   PLANH1 {ECO:0000313|EMBL:AFL47815.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:AFL47815.1};
RN   [1] {ECO:0000313|EMBL:AFL47815.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bager R., Johansen J.S., Jensen J.K., Stensballe A., Jendroszek A.,
RA   Sorensen H.P., Andreasen P.A.;
RT   "Characterization of Fish PAI-1.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4KDS}
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 15-391.
RX   PubMed=23702291; DOI=10.1016/j.jmb.2013.05.007;
RA   Bager R., Johansen J.S., Jensen J.K., Stensballe A., Jendroszek A.,
RA   Buxbom L., Sorensen H.P., Andreasen P.A.;
RT   "Protein conformational change delayed by steric hindrance from an N-linked
RT   glycan.";
RL   J. Mol. Biol. 425:2867-2877(2013).
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; JQ801453; AFL47815.1; -; mRNA.
DR   PDB; 4KDS; X-ray; 1.67 A; A=15-391.
DR   PDBsum; 4KDS; -.
DR   AlphaFoldDB; I3WWD7; -.
DR   SMR; I3WWD7; -.
DR   MEROPS; I04.020; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd02051; serpinE1_PAI-1; 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:SF49; PLASMINOGEN ACTIVATOR INHIBITOR 1; 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.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4KDS}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..391
FT                   /note="Plasminogen activator inhibitor 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012610149"
FT   DOMAIN          29..388
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   391 AA;  43428 MW;  5A6FFC801ECEEFE7 CRC64;
     MLCLYVGFFL GLSGAAISNL QEKQTDFGMR VFSQVAQNSK GSNLAFSPYG VATILAMAQL
     GAGGNTLKTL NAKLGFSLQE RGMARQQRLL QRDISSEEGV ELASGVMVER KMALEKGFRR
     GLGKAFQASP HQLDFSRPDQ ALDIINAWVS DHTAGTIPSF LSSGALTDET RMVLLNALHF
     QGLWKVPFDP KMTEERLFHC ANGSSVPVPM MRLTHRFKYG EFVTPDGVDY DVIEVPYEGE
     SLSMLLVSPF EPETPVSSLS SELTTQRLQQ WRQEMRSVKR QLVLPRFTLD SEVELKSILI
     QMGLGDMFNL AKADFTRITT EQPLCVSKVL QKVKIEVNEE GTKASAATAA ILFSRMAVEE
     ITMNRPFLFL IHHKSTGAVL FMGQVNQPQQ H
//