PAI1_BOVIN
ID PAI1_BOVIN Reviewed; 402 AA.
AC P13909; Q3ZBB9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 162.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2587231; DOI=10.1093/nar/17.21.8872;
RA Mimuro J., Sawdey M., Hatiori M., Loskutoff D.J.;
RT "cDNA for bovine type 1 plasminogen activator inhibitor (PAI-1).";
RL Nucleic Acids Res. 17:8872-8872(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 24-63.
RX PubMed=3262060; DOI=10.1111/j.1432-1033.1988.tb14253.x;
RA Katagiri K., Okada K., Hattori H., Yano M.;
RT "Bovine endothelial cell plasminogen activator inhibitor. Purification and
RT heat activation.";
RL Eur. J. Biochem. 176:81-87(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 153-235.
RC TISSUE=Adrenal cortex;
RX PubMed=1696269; DOI=10.1083/jcb.111.2.743;
RA Pepper M.S., Belin D., Montesano R., Orci L., Vassalli J.-D.;
RT "Transforming growth factor-beta 1 modulates basic fibroblast growth
RT factor-induced proteolytic and angiogenic properties of endothelial cells
RT in vitro.";
RL J. Cell Biol. 111:743-755(1990).
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 -!- TISSUE SPECIFICITY: Vascular endothelial cells may be the primary site
CC of synthesis of plasma PAI1.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; X16383; CAA34419.1; -; mRNA.
DR EMBL; BT025406; ABF57362.1; -; mRNA.
DR EMBL; BC103451; AAI03452.1; -; mRNA.
DR EMBL; X52906; CAA37094.1; -; mRNA.
DR PIR; S06745; S06745.
DR RefSeq; NP_776562.1; NM_174137.2.
DR RefSeq; XP_010817781.1; XM_010819479.2.
DR AlphaFoldDB; P13909; -.
DR SMR; P13909; -.
DR STRING; 9913.ENSBTAP00000019232; -.
DR MEROPS; I04.020; -.
DR PaxDb; P13909; -.
DR PRIDE; P13909; -.
DR GeneID; 281375; -.
DR KEGG; bta:281375; -.
DR CTD; 5054; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; P13909; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF352620; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:AgBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0035375; F:zymogen binding; IPI:AgBase.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3262060"
FT CHAIN 24..402
FT /note="Plasminogen activator inhibitor 1"
FT /id="PRO_0000032498"
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"
FT CONFLICT 50
FT /note="S -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45371 MW; 9053617333C7D130 CRC64;
MRMSPVFACL ALGLALIFGE GSASYQPQSA AASLATDFGV KVFQQVVRAS KDRNVVFSPY
GVASVLAMLQ LTTGGETRQQ IQEAMQFKIE EKGMAPAFHR LYKELMGPWN KDEISTADAI
FVQRDLELVH GFMPNFFRLF RTTVKQVDFS EVERARFIVN DWVKRHTKGM ISDLLGEGAV
DQLTRLVLVN ALYFNGQWKM PFPESNTHHR LFHKSDGSTI SVPMMAQTNK FNYTEFTTPD
GRYYDILELP YHGNTLSMLI AAPYEKEVPL SALTSILDAE LISQWKGNMT RLTRLLVLPK
FSLETEIDLR RPLENLGMTD MFRPSQADFS SFSDQEFLYV SQALQKVKIE VNESGTLASS
STALVVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM EP
