A0A8K0P4Y3 · A0A8K0P4Y3_LADFU

Function

function

Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins. Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties. Is specific for alpha linked terminal mannose.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: The manganese ion interacts primarily with the substrate UDP-N-acetylglucosamine.

Pathway

Protein modification; protein glycosylation.

GO annotations

AspectTerm
Cellular ComponentGolgi membrane
Molecular Functionbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity
Molecular Functioncarbohydrate binding
Molecular Functionmanganese ion binding
Biological ProcessO-glycan processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
  • EC number
  • Short names
    POMGnT1

Gene names

    • ORF names
      J437_LFUL016141

Organism names

Accessions

  • Primary accession
    A0A8K0P4Y3

Proteomes

Subcellular Location

Golgi apparatus membrane
; Single-pass type II membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane44-65Helical

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Interacts with DAG1 (via O-linked mannose moiety). Interacts (via transmembrane domain) with FKTN; the interaction is direct and is required for normal location in Golgi membranes.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-22Disordered
Domain136-225ILEI/PANDER

Domain

The stem domain mediates specific interaction with beta-linked N-acetylglucosamine moieties of O-glycosylated proteins. It also interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O-alpha-D-mannosylprotein.

Sequence similarities

Belongs to the glycosyltransferase 13 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    572
  • Mass (Da)
    65,830
  • Last updated
    2022-08-03 v1
  • Checksum
    5B6B0537D12E2CF3
MKMDPRRGVLRPQQSRSSRRSLFPYTSHTLVTRPMARPRILTKLFQSLLVIVLLVTIGINIMFIMDTSRRLQEEVQHSDIGDNNDHVRAESRRNTLRLQESIPKSLAIEVLSSQLKVSVSVDGTTILEDGEDHKGRGIHVLVLNQASGSVMAQRTFDTYSPHEDEAMALFLNMVSDGRIIVFAIKDEGTFQMKQPARDLLKRLGSKRAQIIGWRDMWAMVIHKGGKMFGESYSKSSEFNTWGAPVILRVEVPLVPFEDSECDWPYTEENRRRRDFCNHIEGYGSVCSCTDPAPLIFNPESILNNQVHDVPVAIIASNRPHYLYRMLRSLLSANGANPEMITVFIDGYFEEPLEVTKLFGLRGIQHTPIGAKNARISQHYKASLTATFNIFPNAQYAIIVEEDLDASPDFFRRLLEEDESIYCISAWNDQGYEHTSEDSSLLYRVETMPGLGWLLKRSLYKDELEAKWPTPEKMWDWDMWMRLPEVRRGRECVIPDVSRTYHFGASGLNMNSYFQDVYFKKHSFNTQPHVELKNIDNVKKENYEELIRTLIKKGTILDHSKSPCDESFIPDRK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ308989
EMBL· GenBank· DDBJ
KAG8236090.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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