Sequence Browser (O15393-1)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
If the whole structure is coloured grey in '3D Structure Viewer' panel, please click the icon - on the top left corner of the viewer.
(If nothing changes then 'Sequence ↔ Structure' mapping may be unavailable).
1
492
Isoform
Remark
Ref
O15393-1  
No experimental confirmation available.
VSP_045083
Click on Isoform of interest to be redirected to the corresponding page
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

To analyse the structural impact of your missense variant:

  • Select the corresponding experimental/modelled structure from the "Available Structures" Panel.
  • Right-click on the target structure and download it.
  • Go to our web server Missense3D to analyse structural impact.

  • Go to Missense3D
Protein:
Other Names:
Serine protease 10
Primary Accession:
Other Accessions:
A8K6Z8, B2R8E5, B7Z459, D3DSJ2, F8WES1, Q6GTK7, Q9BXX1
Gene :
TMPRSS2*, synonyms (PRSS10)
Organism :
Human
Entry Name :
Length :
492
Mass (Da) :
53,859
Last modified :
Jan 3, 2006
Version :
v3
Isoforms :
2 
Variants :
13 
Interactions :
1 
Structures :
Experimental 0 | Phyre prediction 4

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.

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