ID   PAI1_NEOVI              Reviewed;         400 AA.
AC   P50449;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=PAI-1, PAI1, PLANH1;
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Neogale.
OX   NCBI_TaxID=452646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=7557448; DOI=10.1016/0378-1119(95)00261-4;
RA   Chuang T.H., Hamilton R.T., Nilsen-Hamilton M.;
RT   "Cloning of the mink plasminogen activator inhibitor type-1 messenger RNA:
RT   an mRNA with a short half life.";
RL   Gene 162:303-308(1995).
CC   -!- FUNCTION: Serine protease inhibitor. Inhibits TMPRSS7. Is a primary
CC       inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-
CC       type plasminogen activator (PLAU). As PLAT inhibitor, it is required
CC       for fibrinolysis down-regulation and is responsible for the controlled
CC       degradation of blood clots. As PLAU inhibitor, it is involved in the
CC       regulation of cell adhesion and spreading. Acts as a regulator of cell
CC       migration, independently of its role as protease inhibitor. It is
CC       required for stimulation of keratinocyte migration during cutaneous
CC       injury repair. It is involved in cellular and replicative senescence
CC       (By similarity). Plays a role in alveolar type 2 cells senescence in
CC       the lung (By similarity). Is involved in the regulation of cementogenic
CC       differentiation of periodontal ligament stem cells, and regulates
CC       odontoblast differentiation and dentin formation during odontogenesis
CC       (By similarity). {ECO:0000250|UniProtKB:P05121,
CC       ECO:0000250|UniProtKB:P22777}.
CC   -!- SUBUNIT: Forms a heterodimer with TMPRSS7. Interacts with VTN. Binds
CC       LRP1B; binding is followed by internalization and degradation.
CC       Interacts with PPP1CB. In complex with PLAU/uPA, interacts with
CC       PLAUR/uPAR (By similarity). Interacts with SORL1 and LRP1, either alone
CC       or in complex with PLAU; these interactions are abolished in the
CC       presence of LRPAP1/RAP (By similarity). The ternary complex composed of
CC       PLAUR-PLAU-PAI1 also interacts with SORL1 (By similarity). Also
CC       interacts with SORL1, when complexed to PLAT/tPA (By similarity).
CC       {ECO:0000250|UniProtKB:P05121}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05121}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; X58541; CAA41433.1; -; mRNA.
DR   PIR; JC4265; JC4265.
DR   AlphaFoldDB; P50449; -.
DR   SMR; P50449; -.
DR   MEROPS; I04.020; -.
DR   Proteomes; UP000694425; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090399; P:replicative senescence; 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   2: Evidence at transcript level;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..400
FT                   /note="Plasminogen activator inhibitor 1"
FT                   /id="PRO_0000032501"
FT   SITE            367..368
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  45153 MW;  DF45E0694DE28401 CRC64;
     MQMSTVCLAL GLALVFGEAS ASYLHETRAA ELATDFGVKV FKQVAQASKD RNMVFSPYGL
     ASVLAMLQLT TAGETRQQIQ EAMRFQIDEK GMAPALRQLY KELMGPWNKD EISTADAIFV
     QRDLKLVHGF MPYFFRLFQT TVKQVDFSEV ERARFIINDW VKRHTKGMIG DLLGRGTVDQ
     LTRLMLVNAL YFNGQWKTPF PKSGTHHRLF HKSDGSTVSV PMMAQTNKFN YTEFSTPEGR
     YYDILELPYH GDTLSMFIAA PYEKDVPLSA LTNILDAQLI SQWKGNMTRR LRLLVLPKFS
     LESEVNLRGP LENLGMTDMF RPNQADFSSL SDQEALYVSQ ALQKVKIEVN ESGTVASSST
     AIIVSARMAP EEIIMDRPFL FVVRHNPTGT VLFMGQVMEP