PAI1_PIG
ID PAI1_PIG Reviewed; 402 AA.
AC P79335;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 104.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9157595;
RA Bijnens A.P., Knockaert I., Cousin E., Kruithof E.K.O., Declerck P.J.;
RT "Expression and characterization of recombinant porcine plasminogen
RT activator inhibitor-1.";
RL Thromb. Haemost. 77:350-356(1997).
RN [2]
RP ERRATUM OF PUBMED:9157595.
RA Bijnens A.P., Knockaert I., Cousin E., Kruithof E.K.O., Declerck P.J.;
RL Thromb. Haemost. 77:1046-1046(1997).
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; Y11347; CAA72182.1; -; mRNA.
DR RefSeq; NP_999075.1; NM_213910.1.
DR AlphaFoldDB; P79335; -.
DR SMR; P79335; -.
DR STRING; 9823.ENSSSCP00000026436; -.
DR MEROPS; I04.020; -.
DR PeptideAtlas; P79335; -.
DR PRIDE; P79335; -.
DR Ensembl; ENSSSCT00065108289; ENSSSCP00065048379; ENSSSCG00065078203.
DR GeneID; 396945; -.
DR KEGG; ssc:396945; -.
DR CTD; 5054; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P79335; -.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IBA:GO_Central.
DR GO; GO:0061044; P:negative regulation of vascular wound healing; IBA:GO_Central.
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..23
FT /evidence="ECO:0000250"
FT CHAIN 24..402
FT /note="Plasminogen activator inhibitor 1"
FT /id="PRO_0000032502"
FT SITE 369..370
FT /note="Reactive bond"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 402 AA; 45450 MW; 13F60E5F4F8FE405 CRC64;
MRMSLVFACL AMGLALTFAE GSASSHHQSL AARLATDFGV KVFRQVVQAS KDRNVVFSPY
GVASVLAMLQ LTTAGDTQQQ IQEAMQFKIE EKGMAPALRQ LYKELMGPWN KDEISTADAI
FVQRDLKLVQ GFMPYFFRLF RTTVKQVDFS EMDRARFIIN DWVKRHTKGM INDLLGQGAV
DQLTRLVLVN ALYFNGQWKT PFPEKSTHHR LFHKSDGSTV SVPMMAQTNK FNYTEFSTPD
GHYYDILELP YHGNTLSMFI AAPYEKEVPL SALTSILDAQ LISQWKGNMT RLTRLLVLPK
FSLESEVDLR RPLENLGMTD MFRPNQADFS SLSDQELLYM SQALQKVKIE VNESGTVASS
STAIIVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM EP
