PLAU
entrez
5328
canonical
uniprot
P00749
canonical
ensembl
ENSG00000122861
resolver
ensp
ENSP00000361850
resolver
ensp
ENSP00000388474
resolver
ensp
ENSP00000564782
resolver
ensp
ENSP00000605850
resolver
ensp
ENSP00000605851
resolver
ensp
ENSP00000792606
resolver
enst
ENST00000446342
resolver
genesymbol
PLAU
resolver
hgnc
HGNC:9052
resolver
uniprot
B4DNJ4
resolver
uniprot
B4DPZ2
resolver
uniprot
E7ET40
resolver
uniprot
Q15844
resolver
uniprot
Q16618
resolver
uniprot
Q53XS3
resolver
uniprot
Q59GZ8
resolver
uniprot
Q5SWW9
resolver
uniprot
Q969W6
resolver
uniprot_entry
B4DNJ4_HUMAN
resolver
uniprot_entry
E7ET40_HUMAN
resolver
uniprot_entry
Q59GZ8_HUMAN
resolver
uniprot_entry
UROK_HUMAN
resolver
uniprot_sec
B4DPZ2
resolver
uniprot_sec
Q15844
resolver
uniprot_sec
Q16618
resolver
uniprot_sec
Q53XS3
resolver
uniprot_sec
Q5SWW9
resolver
uniprot_sec
Q969W6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by SERPINA5 (PubMed:14696115, PubMed:3501295). Inhibited by SERPINE1 (PubMed:21925150). {ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:21925150, ECO:0000269|PubMed:3501295}.
uniprot
proteins
amino_acid_sequence
MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL
uniprot
proteins
disease_involvement
DISEASE: Quebec platelet disorder (QPD) [MIM:601709]: An autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins. {ECO:0000269|PubMed:20007542}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.73
uniprot
proteins
function
FUNCTION: Serine protease that cleaves the inactive precursor plasminogen at a specific Arg-Val peptide bond, converting it into active plasmin (PubMed:1969415, PubMed:2521625, PubMed:4270330). Secreted as an inactive zymogen, it is recruited and activated at the cell surface through interaction with the urokinase plasminogen activator receptor (uPAR). Cell-surface activation enables localized, plasmin-dependent pericellular proteolysis, regulating extracellular matrix degradation in cell migration and tissue remodeling (PubMed:1829461, PubMed:2521625, PubMed:28849762). Also contributes to fibrinolysis and blood clot clearance by promoting plasmin generation (By similarity). {ECO:0000250|UniProtKB:P06869, ECO:0000269|PubMed:1829461, ECO:0000269|PubMed:1969415, ECO:0000269|PubMed:2521625, ECO:0000269|PubMed:28849762, ECO:0000269|PubMed:4270330}.
uniprot
proteins
mass_dalton
48523
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="S->E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323."; /evidence="ECO:0000269|PubMed:9151681"; MUTAGEN 178; /note="K->E: Loss of cleavage by PLG."; /evidence="ECO:0000269|PubMed:1969415"; MUTAGEN 323; /note="S->E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158."; /evidence="ECO:0000269|PubMed:9151681
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding. {ECO:0000269|PubMed:9151681}.; PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4. {ECO:0000269|PubMed:24434139}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10340997
uniprot
proteins
pubmed
10636902
uniprot
proteins
pubmed
10805774
uniprot
proteins
pubmed
11384978
uniprot
proteins
pubmed
1327118
uniprot
proteins
pubmed
14696115
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15053742
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15988036
uniprot
proteins
pubmed
16456079
uniprot
proteins
pubmed
1829461
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
1969415
uniprot
proteins
pubmed
20007542
uniprot
proteins
pubmed
2023947
uniprot
proteins
pubmed
21925150
uniprot
proteins
pubmed
2415429
uniprot
proteins
pubmed
24434139
uniprot
proteins
pubmed
2521625
uniprot
proteins
pubmed
2536903
uniprot
proteins
pubmed
28849762
uniprot
proteins
pubmed
2987867
uniprot
proteins
pubmed
3501295
uniprot
proteins
pubmed
3888571
uniprot
proteins
pubmed
4270330
uniprot
proteins
pubmed
6589620
uniprot
proteins
pubmed
6749491
uniprot
proteins
pubmed
6754569
uniprot
proteins
pubmed
6754572
uniprot
proteins
pubmed
8107091
uniprot
proteins
pubmed
8161544
uniprot
proteins
pubmed
8591045
uniprot
proteins
pubmed
8652631
uniprot
proteins
pubmed
9065988
uniprot
proteins
pubmed
9151681
uniprot
proteins
pubmed
9194591
uniprot
proteins
sequence_length
431
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24434139}. Note=Secreted as an inactive zymogen, it is activated through specific proteolytic cleavage. {ECO:0000269|PubMed:24434139}.
uniprot
proteins