ID F1SU38_PIG Unreviewed; 442 AA.
AC F1SU38;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Urokinase-type plasminogen activator {ECO:0000256|ARBA:ARBA00019414};
DE EC=3.4.21.73 {ECO:0000256|ARBA:ARBA00013183};
GN Name=PLAU {ECO:0000313|Ensembl:ENSSSCP00000010995.2,
GN ECO:0000313|VGNC:VGNC:91511};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000010995.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000010995.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000010995.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000010995.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC active enzyme plasmin. {ECO:0000256|ARBA:ARBA00004018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.73; Evidence={ECO:0000256|ARBA:ARBA00000942};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; F1SU38; -.
DR SMR; F1SU38; -.
DR Ensembl; ENSSSCT00000011287.4; ENSSSCP00000010995.2; ENSSSCG00000010312.4.
DR VGNC; VGNC:91511; PLAU.
DR GeneTree; ENSGT01050000244971; -.
DR HOGENOM; CLU_006842_18_4_1; -.
DR InParanoid; F1SU38; -.
DR OMA; WPWCYVQ; -.
DR TreeFam; TF329901; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-75205; Dissolution of Fibrin Clot.
DR Proteomes; UP000008227; Chromosome 14.
DR Bgee; ENSSSCG00000010312; Expressed in caecum and 41 other cell types or tissues.
DR ExpressionAtlas; F1SU38; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0097180; C:serine protease inhibitor complex; IEA:Ensembl.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042730; P:fibrinolysis; IBA:GO_Central.
DR GO; GO:0031639; P:plasminogen activation; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:2000097; P:regulation of smooth muscle cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR PANTHER; PTHR24264:SF38; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..442
FT /note="Urokinase-type plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014571388"
FT DOMAIN 29..65
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 71..153
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 190..435
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 55..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 442 AA; 49144 MW; 9F4C49BAC733800D CRC64;
MRVLRACLLL CVLVVSDSKG SHELHQESGA SNCGCLNGGK CVSYKYFSNI QRCSCPKKFQ
GEHCEIDTSQ TCFEGNGHSY RGKANTNTGG RPCLPWNSAT VLLNTYHAHR PDALQLGLGK
HNYCRNPDNQ RRPWCYVQVG LKQLVQECMV PNCSGGESHR PAYDGKNPFS TPEKVEFQCG
QKALRPRFKI VGGKSTTIEN QPWFAAIYRR HRGGSVTYVC GGSLISPCWV VSATHCFINY
QQKEDYIVYL GRQTLHSSTR GEMEFEVEKL ILHEDYSADS LAHHNDIALL KIRTDKGQCA
QPSRSIQTIC LPPVNGDAHF GASCEIVGFG KEDPSDYLYP EQLKMTVVKL VSHRECQQPH
YYGSEVTTKM LCAADPQWKT DSCQGDSGGP LVCSTQGRLT LTGIVSWGRE CAMKDKPGVY
TRVSHFLTWI HTHVGGENGL AH
//
