ID   UROK_BOVIN              Reviewed;         433 AA.
AC   Q05589; A7E3W6; Q0IIG3; Q28209;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Urokinase-type plasminogen activator;
DE            Short=U-plasminogen activator;
DE            Short=uPA;
DE            EC=3.4.21.73;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator long chain A;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator short chain A;
DE   Contains:
DE     RecName: Full=Urokinase-type plasminogen activator chain B;
DE   Flags: Precursor;
GN   Name=PLAU;
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].
RC   TISSUE=Aortic endothelium;
RX   PubMed=8385052; DOI=10.1016/0378-1119(93)90325-w;
RA   Kraetzschmar J., Haendler B., Kojima S., Rifkin D.B., Schleuning W.-D.;
RT   "Bovine urokinase-type plasminogen activator and its receptor: cloning and
RT   induction by retinoic acid.";
RL   Gene 125:177-183(1993).
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 skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-433.
RC   TISSUE=Kidney;
RX   AGRICOLA=IND20546782; DOI=10.1016/0958-6946(94)00034-M;
RA   Ravn P., Berglund L., Petersen T.E.;
RT   "Cloning and characterization of the bovine plasminogen activators uPA and
RT   tPA.";
RL   Int. Dairy J. 5:605-617(1995).
CC   -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC       active enzyme plasmin. {ECO:0000250|UniProtKB:P00749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC         plasmin.; EC=3.4.21.73;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SUBUNIT: Found in high and low molecular mass forms. Each consists of
CC       two chains, A and B. The high molecular mass form contains a long chain
CC       A which is cleaved to yield a short chain A. Forms heterodimer with
CC       SERPINA5. Binds LRP1B; binding is followed by internalization and
CC       degradation. Interacts with MRC2. Interacts with PLAUR. In complex with
CC       SERPINE1, interacts with PLAUR/uPAR. Interacts with SORL1 and LRP1,
CC       either alone or in complex with SERPINE1; these interactions are
CC       abolished in the presence of LRPAP1/RAP. The ternary complex composed
CC       of PLAUR-PLAU-PAI1 also interacts with SORLA.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00749}.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA),
CC       is processed into the active disulfide-linked two-chain form of
CC       PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4.
CC       {ECO:0000250|UniProtKB:P00749}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; L03546; AAA51419.1; -; mRNA.
DR   EMBL; BT030737; ABS45053.1; -; mRNA.
DR   EMBL; BC122657; AAI22658.1; -; mRNA.
DR   EMBL; X85801; CAA59796.1; -; mRNA.
DR   PIR; JN0560; JN0560.
DR   RefSeq; NP_776572.1; NM_174147.2.
DR   RefSeq; XP_005226381.1; XM_005226324.1.
DR   RefSeq; XP_015316474.1; XM_015460988.1.
DR   AlphaFoldDB; Q05589; -.
DR   SMR; Q05589; -.
DR   STRING; 9913.ENSBTAP00000073210; -.
DR   MEROPS; S01.231; -.
DR   PaxDb; 9913-ENSBTAP00000007806; -.
DR   Ensembl; ENSBTAT00000007806.3; ENSBTAP00000007806.2; ENSBTAG00000005947.3.
DR   Ensembl; ENSBTAT00000076172.1; ENSBTAP00000068333.1; ENSBTAG00000005947.3.
DR   GeneID; 281408; -.
DR   KEGG; bta:281408; -.
DR   CTD; 5328; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005947; -.
DR   VGNC; VGNC:32975; PLAU.
DR   eggNOG; ENOG502QRMI; Eukaryota.
DR   GeneTree; ENSGT01050000244971; -.
DR   HOGENOM; CLU_006842_18_4_1; -.
DR   InParanoid; Q05589; -.
DR   OMA; WPWCYVQ; -.
DR   OrthoDB; 4629979at2759; -.
DR   TreeFam; TF329901; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000005947; Expressed in urethra and 105 other cell types or tissues.
DR   ExpressionAtlas; Q05589; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
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   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Hydrolase; Kringle; Phosphoprotein;
KW   Plasminogen activation; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT   CHAIN           21..433
FT                   /note="Urokinase-type plasminogen activator"
FT                   /id="PRO_0000028315"
FT   CHAIN           21..179
FT                   /note="Urokinase-type plasminogen activator long chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028316"
FT   CHAIN           158..179
FT                   /note="Urokinase-type plasminogen activator short chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285895"
FT   CHAIN           181..433
FT                   /note="Urokinase-type plasminogen activator chain B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028317"
FT   DOMAIN          29..65
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          72..153
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          181..426
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          36..59
FT                   /note="Binds urokinase plasminogen activator surface
FT                   receptor"
FT                   /evidence="ECO:0000250"
FT   REGION          154..180
FT                   /note="Connecting peptide"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        378
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00749"
FT   DISULFID        33..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..153
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..148
FT                   /evidence="ECO:0000250"
FT   DISULFID        170..301
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000255|PROSITE-ProRule:PRU00121, ECO:0000255|PROSITE-
FT                   ProRule:PRU00274"
FT   DISULFID        211..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..384
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..402
FT                   /evidence="ECO:0000250"
FT   CONFLICT        189
FT                   /note="A -> T (in Ref. 4; CAA59796)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   433 AA;  48730 MW;  4DE1B8D4DA47027A CRC64;
     MRVLLACLLV CALVVSDSDG SNEVHKESGE SNCGCLNGGK CVTYKYFSNI QRCSCPKKFQ
     GEHCEIDTSK TCYQGNGHSY RGKANRDLSG RPCLAWDSPT VLLKMYHAHR SDAIQLGLGK
     HNYCRNPDNQ RRPWCYVQIG LKQFVQFCMV QDCSVGKSPS SPREKEEFQC GQKALRPRFK
     IVGGQVTNAE NQPWFAAIYR RHRGGSITYL CGGSLISPCW VVSATHCFID HPKKENYIVY
     LGQSRLNSDT RGEMQFEVEK LILHEDYSAE SLAHHNDIAL LKIRTSRGQC AQPSRSIQTI
     CLPPEHEDAH SRTRCEITGF GKENPSDYRY SDELKMTFVS LVSHEVCQQP HYYGAEVTDK
     MLCAADPQWE TDSCQGDSGG PLVCTIQGRL TLTGIVSWGR DCAMKYKPGV YTRVSKFLPW
     INTHTRGEIN LVL
//