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Database: UniProt
Entry: Q5RF29
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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   10-APR-2019, entry version 99.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to
CC         form plasmin.; EC=3.4.21.73;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: Found in high and low molecular mass forms. Each consists
CC       of two chains, A and B. The high molecular mass form contains a
CC       long chain A which is cleaved to yield a short chain A. Forms
CC       heterodimer with SERPINA5. Binds LRP1B; binding is followed by
CC       internalization and degradation. Interacts with MRC2. Interacts
CC       with PLAUR (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive
CC       ability but does not interfere with receptor binding.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; CR857332; CAH89628.1; -; mRNA.
DR   RefSeq; NP_001124729.1; NM_001131257.2.
DR   ProteinModelPortal; Q5RF29; -.
DR   SMR; Q5RF29; -.
DR   STRING; 9601.ENSPPYP00000002700; -.
DR   MEROPS; S01.231; -.
DR   PRIDE; Q5RF29; -.
DR   Ensembl; ENSPPYT00000002791; ENSPPYP00000002700; ENSPPYG00000002324.
DR   GeneID; 100171578; -.
DR   KEGG; pon:100171578; -.
DR   CTD; 5328; -.
DR   eggNOG; ENOG410IGFI; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00950000182667; -.
DR   HOVERGEN; HBG008633; -.
DR   InParanoid; Q5RF29; -.
DR   KO; K01348; -.
DR   OMA; KFQGEHC; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF329901; -.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 2.40.20.10; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
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; 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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Kringle; Phosphoprotein; Plasminogen activation; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    431       Urokinase-type plasminogen activator.
FT                                /FTId=PRO_0000285896.
FT   CHAIN        21    177       Urokinase-type plasminogen activator long
FT                                chain A. {ECO:0000250}.
FT                                /FTId=PRO_0000285897.
FT   CHAIN       156    177       Urokinase-type plasminogen activator
FT                                short chain A. {ECO:0000250}.
FT                                /FTId=PRO_0000285898.
FT   CHAIN       179    431       Urokinase-type plasminogen activator
FT                                chain B. {ECO:0000250}.
FT                                /FTId=PRO_0000285899.
FT   DOMAIN       27     63       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       69    151       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      179    424       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION       34     57       Binds urokinase plasminogen activator
FT                                surface receptor. {ECO:0000250}.
FT   REGION      152    178       Connecting peptide. {ECO:0000250}.
FT   ACT_SITE    224    224       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    275    275       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    376    376       Charge relay system. {ECO:0000250}.
FT   MOD_RES     158    158       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00749}.
FT   MOD_RES     323    323       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00749}.
FT   CARBOHYD    322    322       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     31     39       {ECO:0000250}.
FT   DISULFID     33     51       {ECO:0000250}.
FT   DISULFID     53     62       {ECO:0000250}.
FT   DISULFID     70    151       {ECO:0000250}.
FT   DISULFID     91    133       {ECO:0000250}.
FT   DISULFID    122    146       {ECO:0000250}.
FT   DISULFID    168    299       Interchain (between A and B chains).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000255|PROSITE-ProRule:PRU00121,
FT                                ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    209    225       {ECO:0000250}.
FT   DISULFID    217    288       {ECO:0000250}.
FT   DISULFID    313    382       {ECO:0000250}.
FT   DISULFID    345    361       {ECO:0000250}.
FT   DISULFID    372    400       {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
//
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