Sequence Browser (O15393-1)

Available Structures (Graph-View Mode)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
492

Isoforms (From UniProt)

Isoform
Remark
Ref
O15393-1  
O15393-2
No experimental confirmation available.
VSP_045083
Click on Isoform of interest to be redirected to the corresponding page

Variants (From UniProt)

Type
Variation
Position
sequence variant
V → M
160
sequence variant
E → Q
329
sequence variant
D → N
491
mutagenesis site
S → A
441
sequence conflict
N → S
62
sequence conflict
I → L
242
splice variant
M → MPPAPPGGESGCEERGAAGHIEHSRYLSLLDAVDNSKM
1
sequence variant
S → C
254
sequence variant
K → N
449
mutagenesis site
R → Q
255
sequence conflict
Y → H
26
sequence conflict
S → P
163
sequence conflict
RAD → KAN
489 - 491

3D Structure Viewer - JSMol  

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Protein Information (From UniProt)

Protein:
Transmembrane protease serine 2
Other Names:
Serine protease 10
Primary Accession:
O15393
Other Accessions:
A8K6Z8, B2R8E5, B7Z459, D3DSJ2, F8WES1, Q6GTK7, Q9BXX1
Gene :
TMPRSS2*, synonyms (PRSS10)
Organism :
Human
Entry Name :
TMPS2_HUMAN
Length :
492
Mass (Da) :
53,859
Last modified :
03-Jan-2006
Version :
v3
Isoforms :
2 
Variants :
13 
Interactions :
1 
Structures :
Experimental 0 | Phyre prediction 4
Function : Show Hide

Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Interactions (From UniProt)

With
Entry
IntAct
Exp
TMEM128
Q5BJH2-2
EBI-12345267, EBI-10694905
4