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   24-JAN-2024, entry version 172.
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; 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.
DR   RefSeq; XP_006539703.1; XM_006539640.3.
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   GlyCosmos; P35456; 7 sites, No reported glycans.
DR   GlyGen; P35456; 7 sites.
DR   iPTMnet; P35456; -.
DR   PhosphoSitePlus; P35456; -.
DR   SwissPalm; P35456; -.
DR   MaxQB; P35456; -.
DR   PaxDb; 10090-ENSMUSP00000002284; -.
DR   PeptideAtlas; P35456; -.
DR   ProteomicsDB; 300097; -. [P35456-1]
DR   ProteomicsDB; 300098; -. [P35456-2]
DR   Antibodypedia; 31096; 733 antibodies from 42 providers.
DR   DNASU; 18793; -.
DR   Ensembl; ENSMUST00000002284.11; ENSMUSP00000002284.10; ENSMUSG00000046223.11. [P35456-1]
DR   GeneID; 18793; -.
DR   KEGG; mmu:18793; -.
DR   UCSC; uc009fpr.1; mouse. [P35456-1]
DR   AGR; MGI:97612; -.
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; TGNGCNH; -.
DR   OrthoDB; 4599852at2759; -.
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 79 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 135 other cell types or tissues.
DR   ExpressionAtlas; P35456; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA: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: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:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; 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; NAS:ComplexPortal.
DR   GO; GO:0010755; P:regulation of plasminogen activation; NAS:ComplexPortal.
DR   GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; NAS:ComplexPortal.
DR   CDD; cd00117; LU; 3.
DR   Gene3D; 2.10.60.10; CD59; 3.
DR   InterPro; IPR018363; CD59_antigen_CS.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   PANTHER; PTHR10624:SF6; UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR; 1.
DR   PANTHER; PTHR10624; UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR-RELATED; 1.
DR   Pfam; PF00021; UPAR_LY6; 3.
DR   SMART; SM00134; LU; 3.
DR   SUPFAM; SSF57302; Snake toxin-like; 3.
DR   PROSITE; PS00983; LY6_UPAR; 3.
DR   Genevisible; P35456; MM.
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
//