Sequence Browser (O00219-1)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
553
Isoform
Remark
Ref
O00219-1  
No experimental confirmation available.
VSP_042022
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Type
Variation
Position
splice variant
ILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV → PPGKGMAVEDDQVQAAQVRATEAWSVHQRHVSREQ
247 - 553
sequence conflict
G → E
493
sequence variant
R → H
173

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Protein:
Other Names:
Hyaluronate synthase 3, Hyaluronic acid synthase 3
Primary Accession:
Other Accessions:
A8K5T5, Q8WTZ0, Q9NYP0
Gene :
HAS3*
Organism :
Human
Entry Name :
Length :
553
Mass (Da) :
62,998
Last modified :
23-Jan-2008
Version :
v3
Isoforms :
2 
Variants :
3 
Interactions :
0 
Structures :
Experimental 0 | Phyre prediction 2

Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction (By similarity).

No interactions reported for this protein.