UPAR_MOUSE
ID UPAR_MOUSE Reviewed; 327 AA.
AC P35456; P35457;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Macrophage;
RX PubMed=1661735; DOI=10.1083/jcb.115.6.1763;
RA Kristensen P., Eriksen J., Blasi F., Danoe K.;
RT "Two alternatively spliced mouse urokinase receptor mRNAs with different
RT histological localization in the gastrointestinal tract.";
RL J. Cell Biol. 115:1763-1771(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7929309; DOI=10.1016/s0021-9258(18)47149-9;
RA Suh T.T., Nerlov C., Dano K., Degen J.L.;
RT "The murine urokinase-type plasminogen activator receptor gene.";
RL J. Biol. Chem. 269:25992-25998(1994).
RN [3]
RP INTERACTION WITH SRPX2, AND TISSUE SPECIFICITY.
RX PubMed=19667118; DOI=10.1096/fj.09-135202;
RA Miljkovic-Licina M., Hammel P., Garrido-Urbani S., Bradfield P.F.,
RA Szepetowski P., Imhof B.A.;
RT "Sushi repeat protein X-linked 2, a novel mediator of angiogenesis.";
RL FASEB J. 23:4105-4116(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 24-300 IN COMPLEX WITH PLAU,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-75; ASN-193 AND ASN-282.
RX PubMed=20133942; DOI=10.1074/jbc.m109.093492;
RA Lin L., Gardsvoll H., Huai Q., Huang M., Ploug M.;
RT "Structure-based engineering of species selectivity in the interaction
RT between urokinase and its receptor: implication for preclinical cancer
RT therapy.";
RL J. Biol. Chem. 285:10982-10992(2010).
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 -!- SUBUNIT: Monomer (Probable). Interacts (via the UPAR/Ly6 domains) with
CC SRPX2. Interacts with MRC2 (By similarity). Interacts with SORL1 (via
CC N-terminal ectodomain); this interaction decreases PLAUR
CC internalization (By similarity). The ternary complex composed of PLAUR-
CC PLAU-SERPINE1 also interacts with SORL1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q03405, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P49616}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000250|UniProtKB:P49616}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GPI-anchored;
CC IsoId=P35456-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P35456-2, P35457-1;
CC Sequence=VSP_031837, VSP_031838;
CC -!- TISSUE SPECIFICITY: Expressed in angiogenic endothelial cells (at
CC protein level). {ECO:0000269|PubMed:19667118}.
CC -!- MISCELLANEOUS: [Isoform 1]: GPI-anchored form.
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DR EMBL; X62700; CAA44574.1; -; mRNA.
DR EMBL; X62701; CAA44575.1; -; mRNA.
DR EMBL; U12235; AAB60484.1; -; Genomic_DNA.
DR CCDS; CCDS20950.1; -. [P35456-1]
DR PIR; A55356; A55356.
DR PIR; B41643; B41643.
DR RefSeq; NP_035243.1; NM_011113.4. [P35456-1]
DR RefSeq; XP_006539702.1; XM_006539639.3. [P35456-1]
DR RefSeq; XP_006539703.1; XM_006539640.3. [P35456-1]
DR PDB; 3LAQ; X-ray; 3.20 A; U/V=24-300.
DR PDB; 6AEX; X-ray; 2.39 A; U=24-300.
DR PDBsum; 3LAQ; -.
DR PDBsum; 6AEX; -.
DR AlphaFoldDB; P35456; -.
DR SMR; P35456; -.
DR ComplexPortal; CPX-510; uPA-uPAR complex.
DR ComplexPortal; CPX-526; uPA-uPAR-vitronectin complex.
DR CORUM; P35456; -.
DR IntAct; P35456; 1.
DR STRING; 10090.ENSMUSP00000002284; -.
DR GlyGen; P35456; 7 sites.
DR iPTMnet; P35456; -.
DR PhosphoSitePlus; P35456; -.
DR SwissPalm; P35456; -.
DR MaxQB; P35456; -.
DR PaxDb; P35456; -.
DR PeptideAtlas; P35456; -.
DR PRIDE; P35456; -.
DR ProteomicsDB; 300097; -. [P35456-1]
DR ProteomicsDB; 300098; -. [P35456-2]
DR Antibodypedia; 31096; 620 antibodies from 42 providers.
DR DNASU; 18793; -.
DR Ensembl; ENSMUST00000002284; ENSMUSP00000002284; ENSMUSG00000046223. [P35456-1]
DR GeneID; 18793; -.
DR KEGG; mmu:18793; -.
DR UCSC; uc009fpr.1; mouse. [P35456-1]
DR CTD; 5329; -.
DR MGI; MGI:97612; Plaur.
DR VEuPathDB; HostDB:ENSMUSG00000046223; -.
DR eggNOG; ENOG502S36D; Eukaryota.
DR GeneTree; ENSGT00940000153599; -.
DR HOGENOM; CLU_072612_0_0_1; -.
DR InParanoid; P35456; -.
DR OMA; ECASCAS; -.
DR PhylomeDB; P35456; -.
DR TreeFam; TF338662; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR BioGRID-ORCS; 18793; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; P35456; -.
DR PRO; PR:P35456; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35456; protein.
DR Bgee; ENSMUSG00000046223; Expressed in granulocyte and 132 other tissues.
DR ExpressionAtlas; P35456; baseline and differential.
DR Genevisible; P35456; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0030377; F:urokinase plasminogen activator receptor activity; IEA:InterPro.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; ISO:MGI.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0051917; P:regulation of fibrinolysis; IC:ComplexPortal.
DR GO; GO:0010755; P:regulation of plasminogen activation; IC:ComplexPortal.
DR GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..?298
FT /note="Urokinase plasminogen activator surface receptor"
FT /id="PRO_0000036096"
FT PROPEP ?299..327
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036097"
FT DOMAIN 24..117
FT /note="UPAR/Ly6 1"
FT DOMAIN 117..212
FT /note="UPAR/Ly6 2"
FT DOMAIN 213..298
FT /note="UPAR/Ly6 3"
FT LIPID 298
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133942"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133942"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 26..47
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 29..35
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 40..68
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 94..99
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 119..146
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 122..129
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 139..168
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 174..191
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 192..197
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 215..243
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 218..226
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 236..262
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 268..287
FT /evidence="ECO:0000269|PubMed:20133942"
FT DISULFID 288..293
FT /evidence="ECO:0000269|PubMed:20133942"
FT VAR_SEQ 157..222
FT /note="RSLKDEDYTRGCGSLPGCPGTAGFHSNQTFHFLKCCNYTHCNGGPVLDLQSF
FT PPNGFQCYSCEGNN -> SKLPSAGQLLVEIFKSWEQSASKRQLNPHTVTGPTFSVTGS
FT SGSLDQLGSDQEPSYLVMSRILLSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1661735"
FT /id="VSP_031837"
FT VAR_SEQ 223..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1661735"
FT /id="VSP_031838"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3LAQ"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3LAQ"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:6AEX"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6AEX"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:6AEX"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:6AEX"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:6AEX"
SQ SEQUENCE 327 AA; 35428 MW; A117441D738B6343 CRC64;
MGLPRRLLLL LLLATTCVPA SQGLQCMQCE SNQSCLVEEC ALGQDLCRTT VLREWQDDRE
LEVVTRGCAH SEKTNRTMSY RMGSMIISLT ETVCATNLCN RPRPGARGRA FPQGRYLECA
SCTSLDQSCE RGREQSLQCR YPTEHCIEVV TLQSTERSLK DEDYTRGCGS LPGCPGTAGF
HSNQTFHFLK CCNYTHCNGG PVLDLQSFPP NGFQCYSCEG NNTLGCSSEE ASLINCRGPM
NQCLVATGLD VLGNRSYTVR GCATASWCQG SHVADSFPTH LNVSVSCCHG SGCNSPTGGA
PRPGPAQLSL IASLLLTLGL WGVLLWT
