PLAUR
entrez
5329
canonical
uniprot
Q03405
canonical
ensembl
ENSG00000011422
resolver
ensp
ENSP00000221264
resolver
ensp
ENSP00000339328
resolver
ensp
ENSP00000342049
resolver
ensp
ENSP00000471881
resolver
ensp
ENSP00000617510
resolver
ensp
ENSP00000709445
resolver
ensp
ENSP00000709446
resolver
enst
ENST00000601723
resolver
genesymbol
PLAUR
resolver
genesymbol_syn
MO3
resolver
genesymbol_syn
UPAR
resolver
hgnc
HGNC:9053
resolver
uniprot
A8K409
resolver
uniprot
M0R1I2
resolver
uniprot
Q12876
resolver
uniprot
Q15845
resolver
uniprot
Q16887
resolver
uniprot
Q6IB52
resolver
uniprot
Q9BWT0
resolver
uniprot
Q9NYC8
resolver
uniprot
Q9UD69
resolver
uniprot
Q9UEA6
resolver
uniprot
Q9UM92
resolver
uniprot
Q9UMV0
resolver
uniprot_entry
M0R1I2_HUMAN
resolver
uniprot_entry
UPAR_HUMAN
resolver
uniprot_sec
A8K409
resolver
uniprot_sec
Q12876
resolver
uniprot_sec
Q15845
resolver
uniprot_sec
Q16887
resolver
uniprot_sec
Q6IB52
resolver
uniprot_sec
Q9BWT0
resolver
uniprot_sec
Q9NYC8
resolver
uniprot_sec
Q9UD69
resolver
uniprot_sec
Q9UEA6
resolver
uniprot_sec
Q9UM92
resolver
uniprot_sec
Q9UMV0
resolver
activity_regulation
ACTIVITY REGULATION: Cleavage of the GPI anchor by GDPD2 inactivates receptor functions in vitronectin-mediated cell-matrix adhesion and plasmin-dependent extracellular matrix remodeling (PubMed:28849762). The receptor is also cleaved and inactivated by its ligand PLAU/uPA as part of a negative feedback loop regulating its activity (PubMed:9030717). {ECO:0000269|PubMed:28849762, ECO:0000269|PubMed:9030717}.
uniprot
proteins
amino_acid_sequence
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
uniprot
proteins
function
FUNCTION: GPI-anchored receptor that recruits and activates the urokinase-type plasminogen activator (uPA) at the cell surface. Activated uPA converts plasminogen into plasmin, initiating extracellular matrix degradation and remodeling (PubMed:1689240, PubMed:15677461). Also binds the extracellular matrix protein vitronectin, promoting cell-matrix adhesion and indirectly integrin signaling (PubMed:17548516, PubMed:25168639, PubMed:28849762). This dual interaction coordinates dynamic changes in cell migration, proliferation, and tissue remodeling (PubMed:28849762). {ECO:0000269|PubMed:15677461, ECO:0000269|PubMed:1689240, ECO:0000269|PubMed:17548516, ECO:0000269|PubMed:25168639, ECO:0000269|PubMed:28849762}.
uniprot
proteins
mass_dalton
36978
uniprot
proteins
post_translational_modification
PTM: Attached to the external leaflet of the plasma membrane via a GPI anchor. The GPI anchor can be cleaved by the phospholipase C GDPD2, releasing the protein from membranes. {ECO:0000269|PubMed:28849762}.
uniprot
proteins
pubmed
10636902
uniprot
proteins
pubmed
11051819
uniprot
proteins
pubmed
12376466
uniprot
proteins
pubmed
1316922
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14764453
uniprot
proteins
pubmed
15053742
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15677461
uniprot
proteins
pubmed
15861141
uniprot
proteins
pubmed
16456079
uniprot
proteins
pubmed
1689240
uniprot
proteins
pubmed
17548516
uniprot
proteins
pubmed
18718938
uniprot
proteins
pubmed
2156852
uniprot
proteins
pubmed
22285761
uniprot
proteins
pubmed
23486467
uniprot
proteins
pubmed
25168639
uniprot
proteins
pubmed
28849762
uniprot
proteins
pubmed
7539799
uniprot
proteins
pubmed
7605992
uniprot
proteins
pubmed
8049431
uniprot
proteins
pubmed
8131971
uniprot
proteins
pubmed
8392005
uniprot
proteins
pubmed
8394346
uniprot
proteins
pubmed
9030717
uniprot
proteins
sequence_length
335
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:12376466}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:28849762}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:28849762}. Note=Colocalized with FAP (seprase) preferentially at the cell surface of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin-dependent manner. {ECO:0000269|PubMed:12376466}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000250|UniProtKB:P49616}.
uniprot
proteins