UROK_PAPCY
ID UROK_PAPCY Reviewed; 433 AA.
AC P16227;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 135.
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 Papio cynocephalus (Yellow baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9556;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thoracic aorta;
RX PubMed=2113276; DOI=10.1093/nar/18.11.3411;
RA Au Y.P.T., Wang T.W., Clowes A.W.;
RT "Nucleotide and deduced amino acid sequences of baboon urokinase-type
RT plasminogen activator.";
RL Nucleic Acids Res. 18:3411-3411(1990).
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-157 and Ser-325 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; X51935; CAA36200.1; -; mRNA.
DR PIR; S14687; UKBAY.
DR AlphaFoldDB; P16227; -.
DR SMR; P16227; -.
DR MEROPS; S01.231; -.
DR PRIDE; P16227; -.
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 Phosphoprotein; Plasminogen activation; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..433
FT /note="Urokinase-type plasminogen activator"
FT /id="PRO_0000028326"
FT CHAIN 21..176
FT /note="Urokinase-type plasminogen activator long chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028327"
FT CHAIN 155..176
FT /note="Urokinase-type plasminogen activator short chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028328"
FT CHAIN 178..433
FT /note="Urokinase-type plasminogen activator chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028329"
FT DOMAIN 26..62
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 69..150
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 178..426
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 33..56
FT /note="Binds urokinase plasminogen activator surface
FT receptor"
FT /evidence="ECO:0000250"
FT REGION 151..177
FT /note="Connecting peptide"
FT ACT_SITE 223
FT /note="Charge relay system"
FT ACT_SITE 274
FT /note="Charge relay system"
FT ACT_SITE 378
FT /note="Charge relay system"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00749"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00749"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..38
FT /evidence="ECO:0000250"
FT DISULFID 32..50
FT /evidence="ECO:0000250"
FT DISULFID 52..61
FT /evidence="ECO:0000250"
FT DISULFID 69..150
FT /evidence="ECO:0000250"
FT DISULFID 90..132
FT /evidence="ECO:0000250"
FT DISULFID 121..145
FT /evidence="ECO:0000250"
FT DISULFID 167..298
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 208..224
FT /evidence="ECO:0000250"
FT DISULFID 216..287
FT /evidence="ECO:0000250"
FT DISULFID 315..384
FT /evidence="ECO:0000250"
FT DISULFID 347..363
FT /evidence="ECO:0000250"
FT DISULFID 374..402
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 48595 MW; 816D22DFEDDC8792 CRC64;
MRALLAHLLL CVLVVSASKG SRELQVPSDC GCLNGGTCMS NKYFSSIHWC NCPKKFGGQH
CEIDKSKTCY EGNGHFYRGK ASTDTMGRSC LAWNSATVLQ QTYHAHRSDA LQLGLGKHNY
CRNPDNRRRP WCYVQVGLKQ RVQECMVHNC ADGKKPSSPP EELQFQCGQR TLRPRFKIVG
GEFTTIENQP WFAAIYRRHR GGSVTYVCGG SLISPCWVVS ATHCFINYPK KEDYIVYLGR
SRLNSNTQGE MKFEVENLIL HEDYSADTLA HHNDIALLKI RSKEGRCAQP SRTIQTICLP
SMYNDPNDPP FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSHQKCQQP HYYGSEVTTK
MLCAADPQWE TDSCQGDSGG PLVCSIQGHM TLTGIVSWGR GCALKDKPGV YTRVSRFLPW
IHSHTREQNG LAL
