Tmprss2
entrez
50528
canonical
uniprot
Q9JIQ8
canonical
ensembl
ENSMUSG00000000385
resolver
ensp
ENSMUSP00000000395
resolver
enst
ENSMUST00000000395
resolver
genesymbol
Tmprss2
resolver
uniprot
Q7TN04
resolver
uniprot
Q9JKC4
resolver
uniprot
Q9QY82
resolver
uniprot_entry
TMPS2_MOUSE
resolver
uniprot_sec
Q7TN04
resolver
uniprot_sec
Q9JKC4
resolver
uniprot_sec
Q9QY82
resolver
amino_acid_sequence
MALNSGSPPGIGPCYENHGYQSEHICPPRPPVAPNGYNLYPAQYYPSPVPQYAPRITTQASTSVIHTHPKSSGALCTSKSKKSLCLALALGTVLTGAAVAAVLLWRFWDSNCSTSEMECGSSGTCISSSLWCDGVAHCPNGEDENRCVRLYGQSFILQVYSSQRKAWYPVCQDDWSESYGRAACKDMGYKNNFYSSQGIPDQSGATSFMKLNVSSGNVDLYKKLYHSDSCSSRMVVSLRCIECGVRSVKRQSRIVGGLNASPGDWPWQVSLHVQGVHVCGGSIITPEWIVTAAHCVEEPLSSPRYWTAFAGILRQSLMFYGSRHQVEKVISHPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGKTSDVLNAAMVPLIEPSKCNSKYIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQMRANS
uniprot
proteins
ec_number
3.4.21.122
uniprot
proteins
function
FUNCTION: Plasma membrane-anchored serine protease that cleaves at arginine residues (By similarity). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption (By similarity). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (PubMed:25734995). {ECO:0000250|UniProtKB:O15393, ECO:0000269|PubMed:25734995}.; FUNCTION: (Microbial infection) Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9) and is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. {ECO:0000269|PubMed:24348248, ECO:0000269|PubMed:24522916, ECO:0000269|PubMed:24600012}.
uniprot
proteins
mass_dalton
53526
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed; by an autocatalytic mechanism. Autocleavage induces active conformation. {ECO:0000250|UniProtKB:O15393}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10683448
uniprot
proteins
pubmed
11169526
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16428450
uniprot
proteins
pubmed
24348248
uniprot
proteins
pubmed
24522916
uniprot
proteins
pubmed
24600012
uniprot
proteins
pubmed
25734995
uniprot
proteins
sequence_length
490
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15393}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15393}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 2 catalytic chain]: Secreted {ECO:0000250|UniProtKB:O15393}. Note=Activated by cleavage and secreted. {ECO:0000250|UniProtKB:O15393}.
uniprot
proteins
transmembrane_region
TRANSMEM 84..104; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins