UPAR_AOTTR
ID UPAR_AOTTR Reviewed; 336 AA.
AC Q9GK77;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=9505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Engelholm L.H., Behrendt N.;
RT "Characterization of the urokinase plasminogen activator receptor on
RT primate cell lines.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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; AF302074; AAG40762.1; -; mRNA.
DR AlphaFoldDB; Q9GK77; -.
DR SMR; Q9GK77; -.
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; 3.
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..23
FT /evidence="ECO:0000250"
FT CHAIN 24..?
FT /note="Urokinase plasminogen activator surface receptor"
FT /id="PRO_0000318202"
FT PROPEP ?..336
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000318203"
FT DOMAIN 24..111
FT /note="UPAR/Ly6 1"
FT DOMAIN 116..208
FT /note="UPAR/Ly6 2"
FT DOMAIN 215..302
FT /note="UPAR/Ly6 3"
FT SITE 112..113
FT /note="Cleavage; by U-PA"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..47
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 29..35
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 40..68
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 94..99
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 118..145
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 121..128
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 138..170
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 176..193
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 194..199
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 217..245
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 220..228
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 238..264
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 270..288
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 289..294
FT /evidence="ECO:0000250|UniProtKB:Q03405"
SQ SEQUENCE 336 AA; 36671 MW; 06E952B99EF8BDE5 CRC64;
MGHPLLLPLL LLLLHTGVPA SWGLRCMQCN GHGNCRVEEC ALGQNLCRTT SVRHWEEGEE
VEMVEKSCTH SEKTNRTMSF RTGVRITTLT EAVCGLDLCN QDSSGPAVTF PRSRFLECIS
CGSSDMSCER GRHQSLQCTS PKEQCLDMVT HRTSEAEEGR PKDDHHIRGC GHLPGCPGIA
GFHSEDTFHF LKCCNTTKCN GGPILSLANL PKNGHRCYSC QGNSTHGCSS ENTVLTDCRG
PMNQCLEATG IYEPLSESYM VRGCATSSMC QHDHVSDAFS MSHIDVACCT ENDCNNPAED
IQHRSEAAPQ PGPAHLSLTI TGLMTARLWG GTLLWT
