O01705 · EXT2_CAEEL

  • Protein
    Exostosin-2 homolog
  • Gene
    rib-2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Glycosyltransferase required for the biosynthesis of heparan sulfate (PubMed:11121397, PubMed:16828468, PubMed:17237233).
Initiates heparan sulfate synthesis by transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core linker (GlcNAcT-I activity) (PubMed:11121397).
In association with rib-1, is also responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains (GlcNAcT-II and GlcAT-II activities) (PubMed:11121397, PubMed:17237233).
Required for normal ventral epidermal enclosure during the early stages of embryonic development (PubMed:17237233).
In addition, involved in the elongation of the pharyngeal isthmus during the later stages of embryonic development (PubMed:16828468).
Involved in the directed migration of hermaphrodite-specific neurons (PubMed:17237233, PubMed:24052309).

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Activity regulation

Binding to rib-1 is required for GlcAT-II activity and for increasing GlcNAc-II activity in vitro.

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site570UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site595UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site620UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site625UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site641UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site642UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site643Mn2+ (UniProtKB | ChEBI); catalytic
Binding site643UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site727UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site728
Binding site728UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site771UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentprotein-containing complex
Molecular Functionacetylglucosaminyltransferase activity
Molecular Functionenzyme binding
Molecular Functionglucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity
Molecular Functionglucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity
Molecular Functionglycosyltransferase activity
Molecular Functionheparan sulfate N-acetylglucosaminyltransferase activity
Molecular Functionmetal ion binding
Molecular FunctionN-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity
Biological Processembryonic morphogenesis
Biological Processheparan sulfate proteoglycan biosynthetic process
Biological Processnematode pharynx development
Biological Processprotein glycosylation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GT47Glycosyltransferase Family 47
    • GT64Glycosyltransferase Family 64

Names & Taxonomy

Protein names

  • Recommended name
    Exostosin-2 homolog
  • EC number
  • Alternative names
    • Glucuronyl-galactosyl-proteoglycan 4-alpha-N- acetylglucosaminyltransferase
      (GlcNAc transferase I
      ; GlcNAcT-I
      )
    • Glucuronyl-galactosyl-proteoglycan/Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase (GlcAT-II
      ; GlcNAc transferase II
      ; GlcNAcT-II
      ; Glucuronyl transferase II
      )
    • Multiple exostoses homolog 2

Gene names

    • Name
      rib-2
    • ORF names
      K01G5.6

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    O01705
  • Secondary accessions
    • O17920

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type II membrane protein
Golgi apparatus membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-14Cytoplasmic
Transmembrane15-35Helical; Signal-anchor for type II membrane protein
Topological domain36-814Lumenal

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant embryos are arrested at the 1-fold stage due to a failure in epidermal enclosure (PubMed:17237233).
RNAi-mediated knockdown results in the failure of hermaphrodite-specific neurons to migrate to their correct position and in a defect in axonal guidance (PubMed:24052309).

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001496631-814Exostosin-2 homolog
Glycosylation36N-linked (GlcNAc...) asparagine
Glycosylation227N-linked (GlcNAc...) asparagine
Glycosylation297N-linked (GlcNAc...) asparagine
Glycosylation322N-linked (GlcNAc...) asparagine
Glycosylation454N-linked (GlcNAc...) asparagine
Glycosylation492N-linked (GlcNAc...) asparagine
Glycosylation685N-linked (GlcNAc...) asparagine
Disulfide bond726↔774

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with rib-1.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    814
  • Mass (Da)
    94,197
  • Last updated
    2002-03-27 v2
  • Checksum
    38FA58C5EB17DB16
MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQENCSLERRRQLIGSSTFCFLLPSEMFFQDFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSFEISDIIEMRRVGRLFYETYLADRHLLARSLLAALRYKLQIPTREVRRNQAIPLFNSSFTAPKGSVVNVQANFDDEYLLGPLESRVESTSYAYNFTEFQLYSYDFWNIIMSPHYTKEFLVNAAELPTEAEFFEDTKIGFRPIEPGSGAEFSKALGGNRQREQFTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAVLSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHARYGDSMFYNSNHTCQMSMILTGAAFIHKNYLTAYTYEMPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHECMRLFTKIYGYNPLKFSQFRADSILFKTRLPQNHQKCFKYV

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict604in Ref. 1; AAC47510

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U94835
EMBL· GenBank· DDBJ
AAC47510.1
EMBL· GenBank· DDBJ
mRNA
AB077851
EMBL· GenBank· DDBJ
BAB83878.1
EMBL· GenBank· DDBJ
mRNA
Z92803
EMBL· GenBank· DDBJ
CAB07245.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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