UROK_BOVIN
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 03-AUG-2022, entry version 172.
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.ENSBTAP00000007806; -.
DR MEROPS; S01.231; -.
DR PaxDb; Q05589; -.
DR Ensembl; ENSBTAT00000007806; ENSBTAP00000007806; ENSBTAG00000005947.
DR Ensembl; ENSBTAT00000076172; ENSBTAP00000068333; ENSBTAG00000005947.
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; WIAGIFQ; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000005947; Expressed in urethra and 105 other tissues.
DR ExpressionAtlas; Q05589; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IBA:GO_Central.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.20.10; -; 1.
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 InterPro; IPR034814; Urokinase.
DR PANTHER; PTHR24264:SF38; PTHR24264:SF38; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 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
