UROK_PIG
ID UROK_PIG Reviewed; 442 AA.
AC P04185;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 151.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Kidney;
RX PubMed=6096832; DOI=10.1093/nar/12.24.9525;
RA Nagamine Y., Pearson D., Altus M.S., Reich E.;
RT "cDNA and gene nucleotide sequence of porcine plasminogen activator.";
RL Nucleic Acids Res. 12:9525-9541(1984).
RN [2]
RP SEQUENCE REVISION TO 241.
RA Nagamine Y.;
RL Submitted (DEC-1986) to the PIR data bank.
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; X01648; CAA25806.1; -; Genomic_DNA.
DR EMBL; X02724; CAA26511.1; -; mRNA.
DR PIR; A00932; UKPG.
DR RefSeq; NP_999110.1; NM_213945.1.
DR AlphaFoldDB; P04185; -.
DR SMR; P04185; -.
DR STRING; 9823.ENSSSCP00000010995; -.
DR ChEMBL; CHEMBL1075030; -.
DR MEROPS; S01.231; -.
DR PaxDb; P04185; -.
DR PRIDE; P04185; -.
DR GeneID; 396985; -.
DR KEGG; ssc:396985; -.
DR CTD; 5328; -.
DR eggNOG; ENOG502QRMI; Eukaryota.
DR InParanoid; P04185; -.
DR OrthoDB; 1314811at2759; -.
DR PRO; PR:P04185; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
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; Glycoprotein; Hydrolase; Kringle;
KW Plasminogen activation; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..442
FT /note="Urokinase-type plasminogen activator"
FT /id="PRO_0000028330"
FT CHAIN 21..188
FT /note="Urokinase-type plasminogen activator long chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028331"
FT CHAIN 167..188
FT /note="Urokinase-type plasminogen activator short chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285900"
FT CHAIN 190..442
FT /note="Urokinase-type plasminogen activator chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028332"
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 190..435
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..189
FT /note="Connecting peptide"
FT ACT_SITE 235
FT /note="Charge relay system"
FT ACT_SITE 286
FT /note="Charge relay system"
FT ACT_SITE 387
FT /note="Charge relay system"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 179..310
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 220..236
FT /evidence="ECO:0000250"
FT DISULFID 228..299
FT /evidence="ECO:0000250"
FT DISULFID 324..393
FT /evidence="ECO:0000250"
FT DISULFID 356..372
FT /evidence="ECO:0000250"
FT DISULFID 383..411
FT /evidence="ECO:0000250"
FT CONFLICT 241
FT /note="Q -> H (in Ref. 1; CAA25806)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="Q -> H (in Ref. 1; CAA26511)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> GS (in Ref. 1; CAA25806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49117 MW; EE32FCEF501321EE CRC64;
MRVLRACLSL CVLVVSDSKG SHELHQESGA SNCGCLNGGK CVSYKYFSNI QRCSCPKKFQ
GEHCEIDTSQ TCFEGNGHSY RGKANTNTGG RPCLPWNSAT VLLNTYHAHR PDALQLGLGK
HNYCRNPDNQ RRPWCYVQVG LKQLVQECMV PNCSGGESHR PAYDGKNPFS TPEKVEFQCG
QKALRPRFKI VGGKSTTIEN QPWFAAIYRR HRGGSVTYVC GGSLISPCWV VSATHCFINY
QQKEDYIVYL GRQTLHSSTH GEMKFEVEKL ILHEDYSADS LAHHNDIALL KIRTDKGQCA
QPSRSIQTIC LPPVNGDAHF GASCEIVGFG KEDPSDYLYP EQLKMTVVKL VSHRECQQPH
YYGSEVTTKM LCAADPQWKT DSCQGDSGGP LVCSTQGRLT LTGIVSWGRE CAMKDKPGVY
TRVSRFLTWI HTHVGGENGL AH
