UPAR_RAT
ID UPAR_RAT Reviewed; 328 AA.
AC P49616; O35771; P51573; Q7TN35;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 137.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Osteoblast;
RX PubMed=8307160; DOI=10.1016/0014-5793(94)80118-5;
RA Rabbani S.A., Rajwans N., Achbarou A., Murthy K.K., Goltzman D.;
RT "Isolation and characterization of multiple isoforms of the rat urokinase
RT receptor in osteoblasts.";
RL FEBS Lett. 338:69-74(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Aortic smooth muscle;
RA DeYoung M.B., Wohlgemuth J., Dichek D.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=1321734; DOI=10.1016/0014-5793(92)80998-v;
RA Ragno P., Cassano S., Degen J., Kessler C., Blasi F., Rossi G.;
RT "The receptor for the plasminogen activator of urokinase type is up-
RT regulated in transformed rat thyroid cells.";
RL FEBS Lett. 306:193-198(1992).
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:0000269|PubMed:1321734}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:1321734}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000305|PubMed:8307160}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GPI-anchored;
CC IsoId=P49616-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P49616-3, P51573-1;
CC Sequence=VSP_031840, VSP_031841;
CC -!- INDUCTION: Up-regulated in transformed thyroid cell lines.
CC {ECO:0000269|PubMed:1321734}.
CC -!- MISCELLANEOUS: [Isoform 1]: GPI-anchored form.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50717.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA50718.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X71898; CAA50717.1; ALT_FRAME; mRNA.
DR EMBL; X71899; CAA50718.1; ALT_FRAME; mRNA.
DR EMBL; X76129; CAA53732.1; -; Genomic_DNA.
DR EMBL; AF007789; AAB62974.1; -; mRNA.
DR EMBL; BC127499; AAI27500.1; -; mRNA.
DR PIR; S42152; S42152.
DR PIR; S42429; S42429.
DR RefSeq; NP_059046.1; NM_017350.1.
DR RefSeq; NP_599179.1; NM_134352.1. [P49616-1]
DR AlphaFoldDB; P49616; -.
DR SMR; P49616; -.
DR IntAct; P49616; 1.
DR STRING; 10116.ENSRNOP00000063960; -.
DR BindingDB; P49616; -.
DR ChEMBL; CHEMBL3638329; -.
DR GlyGen; P49616; 7 sites.
DR PhosphoSitePlus; P49616; -.
DR PaxDb; P49616; -.
DR PRIDE; P49616; -.
DR GeneID; 50692; -.
DR KEGG; rno:50692; -.
DR CTD; 5329; -.
DR RGD; 620597; Plaur.
DR eggNOG; ENOG502S36D; Eukaryota.
DR InParanoid; P49616; -.
DR OrthoDB; 1102918at2759; -.
DR PhylomeDB; P49616; -.
DR Reactome; R-RNO-162791; Attachment of GPI anchor to uPAR.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR PRO; PR:P49616; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; ISO:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0030377; F:urokinase plasminogen activator receptor activity; TAS:RGD.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:RGD.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..299
FT /note="Urokinase plasminogen activator surface receptor"
FT /id="PRO_0000036099"
FT PROPEP 300..328
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036100"
FT DOMAIN 25..118
FT /note="UPAR/Ly6 1"
FT DOMAIN 118..213
FT /note="UPAR/Ly6 2"
FT DOMAIN 214..299
FT /note="UPAR/Ly6 3"
FT LIPID 299
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
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 CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..48
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 30..36
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 41..69
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 95..100
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 120..147
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 123..130
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 140..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..288
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 289..294
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT VAR_SEQ 159..220
FT /note="SVKDEPYTKGCGSLPGCPGTAGFHSNQTFHFLKCCNFTQCNGGPVLDLQSLP
FT PNGFQCYSCE -> KLPAAGSPLGCPKEISKFQACKQNSHSHATAHSVPGSSESLDQLE
FT SDQELSYLVVSHILLSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8307160"
FT /id="VSP_031840"
FT VAR_SEQ 221..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8307160"
FT /id="VSP_031841"
FT VARIANT 95
FT /note="C -> S"
FT CONFLICT 232..234
FT /note="TSL -> SSF (in Ref. 1; CAA50718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 35753 MW; 9CF24A90B07B2E0A CRC64;
MGLLRRRLLL LVVVVTTCVP ASQGLRCIQC ESNQDCLVEE CALGQDLCRT TVLREWEDAE
ELEVVTRGCA HKEKTNRTMS YRMGSVIVSL TETVCATNLC NRPRPGARGR PFPRGRYLEC
ASCTSLDQSC ERGREQSLQC RYPTEHCIEV VTLQSTERSV KDEPYTKGCG SLPGCPGTAG
FHSNQTFHFL KCCNFTQCNG GPVLDLQSLP PNGFQCYSCE GNSTFGCSYE ETSLIDCRGP
MNQCLEATGL DVLGNRSYTV RGCATASWCQ GSHVADSFQT HVNLSISCCN GSGCNRPTGG
APGPGPAHLI LIASLLLTLR LWGIPLWT
