UPAR_BOVIN
ID UPAR_BOVIN Reviewed; 330 AA.
AC Q05588; A5PJ83;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RX PubMed=8385052; DOI=10.1016/0378-1119(93)90325-w;
RA Kraetzschmar J., Haendler B., Kojima S., Rifkin D.B., Schleuning W.-D.;
RT "Bovine urokinase-type plasminogen activator and its receptor: cloning and
RT induction by retinoic acid.";
RL Gene 125:177-183(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RX PubMed=8122188; DOI=10.1016/0049-3848(93)90173-l;
RA Reuning U., Little S.P., Dixon E.P., Johnstone E.M., Bang N.U.;
RT "Molecular cloning of cDNA for the bovine urokinase-type plasminogen
RT activator receptor.";
RL Thromb. Res. 72:59-70(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 -!- 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: Cell membrane {ECO:0000250|UniProtKB:P49616};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P49616}.
CC -!- INDUCTION: By retinoic acid.
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DR EMBL; L03545; AAA30802.1; -; mRNA.
DR EMBL; S70635; AAB30120.1; -; mRNA.
DR EMBL; BC134754; AAI34755.1; -; mRNA.
DR EMBL; BC142002; AAI42003.1; -; mRNA.
DR PIR; JN0561; JN0561.
DR RefSeq; NP_776848.1; NM_174423.3.
DR AlphaFoldDB; Q05588; -.
DR SMR; Q05588; -.
DR STRING; 9913.ENSBTAP00000017446; -.
DR PaxDb; Q05588; -.
DR PRIDE; Q05588; -.
DR Ensembl; ENSBTAT00000017446; ENSBTAP00000017446; ENSBTAG00000013125.
DR GeneID; 281983; -.
DR KEGG; bta:281983; -.
DR CTD; 5329; -.
DR VEuPathDB; HostDB:ENSBTAG00000013125; -.
DR VGNC; VGNC:32976; PLAUR.
DR eggNOG; ENOG502S36D; Eukaryota.
DR GeneTree; ENSGT00940000153599; -.
DR HOGENOM; CLU_072612_0_0_1; -.
DR InParanoid; Q05588; -.
DR OMA; ECASCAS; -.
DR OrthoDB; 1102918at2759; -.
DR TreeFam; TF338662; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013125; Expressed in milk and 98 other tissues.
DR ExpressionAtlas; Q05588; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IDA:AgBase.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0030377; F:urokinase plasminogen activator receptor activity; IEA:InterPro.
DR GO; GO:0035375; F:zymogen binding; IPI:AgBase.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
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 membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..?300
FT /note="Urokinase plasminogen activator surface receptor"
FT /id="PRO_0000036086"
FT PROPEP ?301..330
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036087"
FT DOMAIN 21..112
FT /note="UPAR/Ly6 1"
FT DOMAIN 113..208
FT /note="UPAR/Ly6 2"
FT DOMAIN 209..300
FT /note="UPAR/Ly6 3"
FT LIPID 300
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..44
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 26..32
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 37..65
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 91..96
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 115..142
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 118..125
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 135..164
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 170..187
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 188..193
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 211..239
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 214..222
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 232..258
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 264..282
FT /evidence="ECO:0000250|UniProtKB:Q03405"
FT DISULFID 283..288
FT /evidence="ECO:0000250|UniProtKB:Q03405"
SQ SEQUENCE 330 AA; 35989 MW; 75E8BFAD1CE39C5C CRC64;
MGQPLLLLLL VYTYIPGSWG LRCLQCENTT SCSVEECTPG QDLCRTTVLS VWEGGNEMNV
VRKGCTHPDK TNRSMSYRAA DQIITLSETV CRSDLCNKPN PGRDATVSRN RYLECASCSS
TDLSCERGWD QTMQCLKSRD QCVDVITHRS LKENPGDERH IRGCGILPGC PGPTGFHNNH
TFHFLRCCNT TKCNAGSVLE LQNLPPNGLQ CYSCEGNGAH RCSSEETFLI DCRGPMNQCL
EATGTKGLRN PSYTIRGCAA PSWCQSLHVA EAFDLTHVNV SCCTGSGCNH PARDDQPGKG
GAPKTSPAHL SFFVSLLLTA RLWGATLLCT
