Q7TT15 · GLT17_MOUSE

  • Protein
    Polypeptide N-acetylgalactosaminyltransferase 17
  • Gene
    Galnt17
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Pathway

Protein modification; protein glycosylation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site192substrate
Binding site223substrate
Binding site246Mn2+ (UniProtKB | ChEBI)
Binding site248Mn2+ (UniProtKB | ChEBI)
Binding site378Mn2+ (UniProtKB | ChEBI)
Binding site381substrate
Binding site386substrate

GO annotations

AspectTerm
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Molecular Functioncarbohydrate binding
Molecular Functionmetal ion binding
Molecular Functionpolypeptide N-acetylgalactosaminyltransferase activity
Biological Processprotein O-linked glycosylation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM13Carbohydrate-Binding Module Family 13
    • GT27Glycosyltransferase Family 27

Names & Taxonomy

Protein names

  • Recommended name
    Polypeptide N-acetylgalactosaminyltransferase 17
  • EC number
  • Alternative names
    • Polypeptide GalNAc transferase-like protein 3 (GalNAc-T-like protein 3; pp-GaNTase-like protein 3)
    • Protein-UDP acetylgalactosaminyltransferase-like protein 3
    • UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
    • Williams-Beuren syndrome chromosomal region 17 protein homolog

Gene names

    • Name
      Galnt17
    • Synonyms
      Wbscr17

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q7TT15
  • Secondary accessions
    • Q8BKN7
    • Q8BUY1
    • Q8BX73
    • Q8BZC8
    • Q8K483

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-6Cytoplasmic
Transmembrane7-27Helical; Signal-anchor for type II membrane protein
Topological domain28-598Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000591401-598Polypeptide N-acetylgalactosaminyltransferase 17
Glycosylation50N-linked (GlcNAc...) asparagine
Disulfide bond142↔373
Disulfide bond364↔443
Glycosylation461N-linked (GlcNAc...) asparagine
Disulfide bond478↔494
Glycosylation486N-linked (GlcNAc...) asparagine
Disulfide bond526↔541
Disulfide bond568↔586

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region151-262Catalytic subdomain A
Region319-381Catalytic subdomain B
Domain465-594Ricin B-type lectin

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q7TT15-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    598
  • Mass (Da)
    67,691
  • Last updated
    2003-10-01 v1
  • Checksum
    66F91B355EF571F5
MASLRRVKVLLVLNLIAVAGFVIFLAKCRPIAVRSGDAFHEIRPRAEVANLSAHSASPIQDAVLKRLSLLEDIVYRQLNGLSKSLGLIEGYGGRGKGGLPATLSPSEEEKAKGPHEKYGYNSYLSEKISLDRSIPDYRPTKCKELKYSKELPQISIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKAPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKAATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELWCMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLPLENPGIDIGDVSERKALRKSLKCKNFQWYLDHVYPEMRRYNNTIAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLDCDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWAIKNPIK

Q7TT15-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E9Q714E9Q714_MOUSEGalnt17371

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict74in Ref. 3; BAC33446
Alternative sequenceVSP_011232194-196in isoform 2
Sequence conflict224in Ref. 3; BAC33446
Sequence conflict264in Ref. 3; BAC33446

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF467979
EMBL· GenBank· DDBJ
AAM62404.1
EMBL· GenBank· DDBJ
mRNA
AK035817
EMBL· GenBank· DDBJ
BAC29197.1
EMBL· GenBank· DDBJ
mRNA
AK048758
EMBL· GenBank· DDBJ
BAC33446.2
EMBL· GenBank· DDBJ
mRNA
AK051281
EMBL· GenBank· DDBJ
BAC34591.2
EMBL· GenBank· DDBJ
mRNA
BC052469
EMBL· GenBank· DDBJ
AAH52469.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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