UROK_PONAB
ID UROK_PONAB Reviewed; 431 AA.
AC Q5RF29;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive
CC ability but does not interfere with receptor binding. {ECO:0000250}.
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; CR857332; CAH89628.1; -; mRNA.
DR RefSeq; NP_001124729.1; NM_001131257.2.
DR AlphaFoldDB; Q5RF29; -.
DR BMRB; Q5RF29; -.
DR SMR; Q5RF29; -.
DR STRING; 9601.ENSPPYP00000002700; -.
DR MEROPS; S01.231; -.
DR GeneID; 100171578; -.
DR KEGG; pon:100171578; -.
DR CTD; 5328; -.
DR eggNOG; ENOG502QRMI; Eukaryota.
DR HOGENOM; CLU_006842_18_4_1; -.
DR InParanoid; Q5RF29; -.
DR OMA; WIAGIFQ; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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; IEA:UniProtKB-EC.
DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010469; P:regulation of signaling receptor activity; 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; 2.40.10.10; -; 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 Phosphoprotein; Plasminogen activation; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..431
FT /note="Urokinase-type plasminogen activator"
FT /id="PRO_0000285896"
FT CHAIN 21..177
FT /note="Urokinase-type plasminogen activator long chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285897"
FT CHAIN 156..177
FT /note="Urokinase-type plasminogen activator short chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285898"
FT CHAIN 179..431
FT /note="Urokinase-type plasminogen activator chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285899"
FT DOMAIN 27..63
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 69..151
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 179..424
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 /evidence="ECO:0000250"
FT REGION 152..178
FT /note="Connecting peptide"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00749"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00749"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..299
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 209..225
FT /evidence="ECO:0000250"
FT DISULFID 217..288
FT /evidence="ECO:0000250"
FT DISULFID 313..382
FT /evidence="ECO:0000250"
FT DISULFID 345..361
FT /evidence="ECO:0000250"
FT DISULFID 372..400
FT /evidence="ECO:0000250"
SQ SEQUENCE 431 AA; 48482 MW; 62E7E952C870408F CRC64;
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ
HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLAWNSATVL QQTYHAHRSD ALQLGLGKHN
YCRNPDNRWR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKIV
GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVV SATHCFIDYP KKEDYIVYLG
RSRLNSHTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IHSKEGRCAQ PSRTIQTICL
PSMYNDPPFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML
CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSYFLPWIR
SHTKEENGLA L
