UROK_RAT
ID UROK_RAT Reviewed; 432 AA.
AC P29598; Q6LBK5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 169.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RX PubMed=1568219;
RA Henderson B.R., Tansey W.P., Phillips S.M., Ramshaw I.A., Kefford R.F.;
RT "Transcriptional and posttranscriptional activation of urokinase
RT plasminogen activator gene expression in metastatic tumor cells.";
RL Cancer Res. 52:2489-2496(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Rabbani S.A.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-62, AND IDENTIFICATION OF UROKINASE
RP PLASMINOGEN ACTIVATOR SURFACE RECEPTOR BINDING DOMAIN.
RX PubMed=1321734; DOI=10.1016/0014-5793(92)80998-v;
RA Ragno P., Cassano S., Degen J., Kessler C., Blasi F., Rossi G.;
RT "The receptor for the plasminogen activator of urokinase type is up-
RT regulated in transformed rat thyroid cells.";
RL FEBS Lett. 306:193-198(1992).
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 -!- 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; X63434; CAA45028.1; -; mRNA.
DR EMBL; X65651; CAA46601.1; -; mRNA.
DR EMBL; X66907; CAA47356.1; -; Genomic_DNA.
DR PIR; S24604; S18932.
DR AlphaFoldDB; P29598; -.
DR SMR; P29598; -.
DR STRING; 10116.ENSRNOP00000014273; -.
DR BindingDB; P29598; -.
DR ChEMBL; CHEMBL1075245; -.
DR MEROPS; S01.231; -.
DR PhosphoSitePlus; P29598; -.
DR PaxDb; P29598; -.
DR UCSC; RGD:3343; rat.
DR RGD; 3343; Plau.
DR eggNOG; ENOG502QRMI; Eukaryota.
DR InParanoid; P29598; -.
DR PhylomeDB; P29598; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR PRO; PR:P29598; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; ISO:RGD.
DR GO; GO:0097180; C:serine protease inhibitor complex; ISO:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:RGD.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
DR GO; GO:0072734; P:cellular response to staurosporine; IEP:RGD.
DR GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR GO; GO:0042730; P:fibrinolysis; ISO:RGD.
DR GO; GO:0070997; P:neuron death; IMP:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000345; P:regulation of hepatocyte proliferation; IMP:RGD.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISO:RGD.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; ISO:RGD.
DR GO; GO:2000097; P:regulation of smooth muscle cell-matrix adhesion; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0035728; P:response to hepatocyte growth factor; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:RGD.
DR GO; GO:0014909; P:smooth muscle cell migration; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
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; 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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..432
FT /note="Urokinase-type plasminogen activator"
FT /id="PRO_0000028333"
FT CHAIN 20..177
FT /note="Urokinase-type plasminogen activator long chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028334"
FT CHAIN 156..177
FT /note="Urokinase-type plasminogen activator short chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028335"
FT CHAIN 179..432
FT /note="Urokinase-type plasminogen activator chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028336"
FT DOMAIN 27..63
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 70..151
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 179..425
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 34..57
FT /note="Binds urokinase plasminogen activator surface
FT receptor"
FT REGION 152..178
FT /note="Connecting peptide"
FT ACT_SITE 225
FT /note="Charge relay system"
FT ACT_SITE 276
FT /note="Charge relay system"
FT ACT_SITE 377
FT /note="Charge relay system"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00749"
FT DISULFID 31..39
FT /evidence="ECO:0000250"
FT DISULFID 33..51
FT /evidence="ECO:0000250"
FT DISULFID 53..62
FT /evidence="ECO:0000250"
FT DISULFID 70..151
FT /evidence="ECO:0000250"
FT DISULFID 91..133
FT /evidence="ECO:0000250"
FT DISULFID 122..146
FT /evidence="ECO:0000250"
FT DISULFID 168..300
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 210..226
FT /evidence="ECO:0000250"
FT DISULFID 218..289
FT /evidence="ECO:0000250"
FT DISULFID 314..383
FT /evidence="ECO:0000250"
FT DISULFID 346..362
FT /evidence="ECO:0000250"
FT DISULFID 373..401
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="N -> H (in Ref. 2; CAA46601)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="E -> G (in Ref. 2; CAA46601)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="D -> N (in Ref. 2; CAA46601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47957 MW; 4EB1B96C716244C8 CRC64;
MRVWLASLFL CALVANSEGG SELEASDESN CGCQNGGVCV SYKYFSSIRR CSCPKKFKGE
HCEIDTSKTC YHGNGQSYRG KANTDTKGRP CLAWNSPAVL QQTYNAHRSD ALSLGLGKHN
YCRNPDNQRR PWCYVQIGLK QFVQECMVQD CSLSKKPSST VDQQGFQCGQ KALRPRFKIV
GGEFTVVENQ PWFAAIYLKN KGGSPPSFKC GGSLISPCWV ASATHCFVNQ PKKEEYVVYL
GQSKRNSYNP GEMKFEVEQL ILHEDFSDET LAFHNDIALL KIRTSTGQCA QPSRTIQTIC
LPPRFGDAPF GSDCEITGFG QESATDYFYP KDLKMSVVKI ISHEQCKQPH YYGSEINYKM
LCAADPEWKT DSCSGDSGGP LICNIDGRPT LSGIVSWGSG CAEKNKPGVY TRVSYFLNWI
QSHIGEENGL AF
