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transmembrane protease serine 2; serine protease 10; contains: transmembrane protease serine 2 non-catalytic chain; transmembrane protease serine 2 catalytic chain (TMPRSS2, PRSS10)
Structure:
- belongs to the peptidase S1 family
- contains 1 LDL-receptor class A domain
- contains 1 peptidase S1 domain
- contains 1 SRCR domain
Compartment:
- cell membrane
- single-pass type 2 membrane protein
- transmembrane protease serine 2 catalytic chain: secreted
- activated by cleavage & secreted
Expression:
- expressed strongly in small intestine
- also expressed in prostate, colon, stomach & salivary gland
- Expressed in type II pneumocytes in the lung [1]
Pathology:
- facilitates SARS CoV2 virus entry into cells after attachment of viral spike glycoprotein to ACE2 on the surface of human cells
- proteolytically cleaves & activates the viral spike glycoproteins which facilitate virus-cell membrane fusions
- fusion glycoproteins F0 of Sendai virus, metapneumovirus, parainfluenza 1, 2, 3, 4a & 4b viruses
- essential for spread & pathogenesis of influenza A virus (strains H1N1, H3N2, H7N9)
- role in proteolytic cleavage & activation of hemagglutinin (HA) protein
General
glycoprotein
transmembrane serine protease
Properties
SIZE: entity length = 492 aa
MW = 54 kD
COMPARTMENT: cellular membrane
MOTIF: transmembrane domain {85-105}
LDL-receptor class A {112-149}
MOTIF: cysteine residue {C113}
MODIFICATION: cysteine residue {C126}
cysteine residue {C120}
MODIFICATION: cysteine residue {C139}
cysteine residue {C126}
MODIFICATION: cysteine residue {C113}
cysteine residue {C133}
MODIFICATION: cysteine residue {C148}
cysteine residue {C139}
MODIFICATION: cysteine residue {C120}
cysteine residue {C148}
MODIFICATION: cysteine residue {C133}
SRCR {150-242}
MOTIF: cysteine residue {C172}
MODIFICATION: cysteine residue {C231}
cysteine residue {C185}
MODIFICATION: cysteine residue {C241}
N-glycosylation site {N213}
cysteine residue {C231}
MODIFICATION: cysteine residue {C172}
cysteine residue {C241}
MODIFICATION: cysteine residue {C185}
cysteine residue {C244}
MODIFICATION: cysteine residue {C-INTERCHAIN}
N-glycosylation site {N249}
proteolytic site {255-256}
S1 domain {256-489}
MOTIF: cysteine residue {C281}
MODIFICATION: cysteine residue {C297}
histidine residue {H296}
cysteine residue {C297}
MODIFICATION: cysteine residue {C281}
aspartate residue {D345}
cysteine residue {C410}
MODIFICATION: cysteine residue {C426}
cysteine residue {C426}
MODIFICATION: cysteine residue {C410}
cysteine residue {C437}
MODIFICATION: cysteine residue {C465}
serine residue {S441}
cysteine residue {C465}
MODIFICATION: cysteine residue {C437}
Database Correlations
OMIM 602060
UniProt O15393
PFAM correlations
Entrez Gene 7113
Kegg hsa:7113
References
- UniProt :accession O15393
- Hoffmann M, Kleine-Weber H, Schroeder S
SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked
by a Clinically Proven Protease Inhibitor.
Cell. 2020 Mar 4. pii: S0092-8674(20)30229-4.
PMID: 32142651