UPAR_CHLAE
ID UPAR_CHLAE Reviewed; 335 AA.
AC Q9GK79;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Urokinase plasminogen activator surface receptor;
DE Short=U-PAR;
DE Short=uPAR;
DE AltName: CD_antigen=CD87;
DE Flags: Precursor;
GN Name=PLAUR; Synonyms=UPAR;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11347891; DOI=10.1515/bc.2001.053;
RA Engelholm L.H., Behrendt N.;
RT "Differential binding of urokinase and peptide antagonists to the urokinase
RT receptor: evidence from characterization of the receptor in four primate
RT species.";
RL Biol. Chem. 382:435-442(2001).
CC -!- FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays
CC a role in localizing and promoting plasmin formation. Mediates the
CC proteolysis-independent signal transduction activation effects of U-PA.
CC It is subject to negative-feedback regulation by U-PA which cleaves it
CC into an inactive form (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer (Probable). Interacts (via the UPAR/Ly6 domains) with
CC SRPX2. Interacts with MRC2. Interacts with FAP (seprase); the
CC interaction occurs at the cell surface of invadopodia membrane.
CC Interacts with SORL1 (via N-terminal ectodomain); this interaction
CC decreases PLAUR internalization (By similarity). The ternary complex
CC composed of PLAUR-PLAU-SERPINE1 also interacts with SORL1 (By
CC similarity). {ECO:0000250|UniProtKB:Q03405, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03405}.
CC Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q03405}.
CC Cell membrane {ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P49616}. Note=Colocalized with FAP (seprase)
CC preferentially at the cell surface of invadopodia membrane in a
CC cytoskeleton-, integrin- and vitronectin-dependent manner.
CC {ECO:0000250|UniProtKB:Q03405}.
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DR EMBL; AF302072; AAG40760.1; -; mRNA.
DR AlphaFoldDB; Q9GK79; -.
DR SMR; Q9GK79; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030377; F:urokinase plasminogen activator receptor activity; IEA:InterPro.
DR GO; GO:0030162; P:regulation of proteolysis; IEA:InterPro.
DR CDD; cd00117; LU; 3.
DR Gene3D; 2.10.60.10; -; 3.
DR InterPro; IPR018363; CD59_antigen_CS.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR033084; U-PAR.
DR PANTHER; PTHR10624:SF6; PTHR10624:SF6; 1.
DR Pfam; PF00021; UPAR_LY6; 2.
DR SMART; SM00134; LU; 3.
DR SUPFAM; SSF57302; SSF57302; 3.
DR PROSITE; PS00983; LY6_UPAR; 3.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..?305
FT /note="Urokinase plasminogen activator surface receptor"
FT /id="PRO_0000036088"
FT PROPEP ?306..335
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036089"
FT DOMAIN 23..114
FT /note="UPAR/Ly6 1"
FT DOMAIN 115..213
FT /note="UPAR/Ly6 2"
FT DOMAIN 214..305
FT /note="UPAR/Ly6 3"
FT SITE 105..106
FT /note="Cleavage; by U-PA"
FT /evidence="ECO:0000250"
FT SITE 111..112
FT /note="Cleavage; by U-PA"
FT /evidence="ECO:0000250"
FT LIPID 305
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..46
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 28..34
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 39..67
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 93..98
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 117..144
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 120..127
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 137..169
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 175..192
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 193..198
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 216..244
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 219..227
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 237..263
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 269..287
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 288..293
FT /evidence="ECO:0000250|UniProtKB:Q03405"
SQ SEQUENCE 335 AA; 37187 MW; 9974EA89D1F47CEC CRC64;
MGHPLLLPLL LLLHTCVPAS WGLRCMQCKS NGDCRVEECA LGQDLCRTTI VRMWEEGEEL
ELVEKSCTHS EKTNRTMSYR TGLKITSLTE VVCGLDLCNQ GNSGRAVTFS RSRYLECISC
GSSDMSCERG RHQSLQCRSP EEQCLDMVTH WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG
FHNNDTFHFL KCCNTTKCNE GPILELENLP QNGHQCYSCK GNSTHGCSSE ETFLIDCRGP
MNQCLVATGT YEPKNQSYMV RGCVTASMCQ RAHLGDAFSM NHINVFCCTE SGCNHPDLDV
QYRKGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT
