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Database: UniProt
Entry: P04185
LinkDB: P04185
Original site: P04185 
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   16-JAN-2019, entry version 142.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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.
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   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Ssc.11194; -.
DR   ProteinModelPortal; 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; ENOG410IGFI; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG008633; -.
DR   InParanoid; P04185; -.
DR   KO; K01348; -.
DR   OrthoDB; 1314811at2759; -.
DR   PRO; PR:P04185; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 2.40.20.10; -; 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; Plasminogen activation; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     20       {ECO:0000250}.
FT   CHAIN        21    442       Urokinase-type plasminogen activator.
FT                                /FTId=PRO_0000028330.
FT   CHAIN        21    188       Urokinase-type plasminogen activator long
FT                                chain A. {ECO:0000250}.
FT                                /FTId=PRO_0000028331.
FT   CHAIN       167    188       Urokinase-type plasminogen activator
FT                                short chain A. {ECO:0000250}.
FT                                /FTId=PRO_0000285900.
FT   CHAIN       190    442       Urokinase-type plasminogen activator
FT                                chain B. {ECO:0000250}.
FT                                /FTId=PRO_0000028332.
FT   DOMAIN       29     65       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       72    153       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      190    435       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION       36     59       Binds urokinase plasminogen activator
FT                                surface receptor. {ECO:0000250}.
FT   REGION      154    189       Connecting peptide.
FT   ACT_SITE    235    235       Charge relay system.
FT   ACT_SITE    286    286       Charge relay system.
FT   ACT_SITE    387    387       Charge relay system.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33     41       {ECO:0000250}.
FT   DISULFID     35     53       {ECO:0000250}.
FT   DISULFID     55     64       {ECO:0000250}.
FT   DISULFID     72    153       {ECO:0000250}.
FT   DISULFID     93    135       {ECO:0000250}.
FT   DISULFID    124    148       {ECO:0000250}.
FT   DISULFID    179    310       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    220    236       {ECO:0000250}.
FT   DISULFID    228    299       {ECO:0000250}.
FT   DISULFID    324    393       {ECO:0000250}.
FT   DISULFID    356    372       {ECO:0000250}.
FT   DISULFID    383    411       {ECO:0000250}.
FT   CONFLICT    241    241       Q -> H (in Ref. 1; CAA25806).
FT                                {ECO:0000305}.
FT   CONFLICT    242    242       Q -> H (in Ref. 1; CAA26511).
FT                                {ECO:0000305}.
FT   CONFLICT    288    288       A -> GS (in Ref. 1; CAA25806).
FT                                {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
//
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