O01705 · EXT2_CAEEL
- ProteinExostosin-2 homolog
- Generib-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids814 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP + H+
- 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP + H+
- 3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP + H+
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 570 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 595 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 620 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 625 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 641 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 642 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 643 | Mn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 643 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 727 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 728 | |||||
Sequence: D | ||||||
Binding site | 728 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 771 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | acetylglucosaminyltransferase activity | |
Molecular Function | enzyme binding | |
Molecular Function | glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity | |
Molecular Function | glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | heparan sulfate N-acetylglucosaminyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity | |
Biological Process | embryonic morphogenesis | |
Biological Process | heparan sulfate proteoglycan biosynthetic process | |
Biological Process | nematode pharynx development | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameExostosin-2 homolog
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionO01705
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-14 | Cytoplasmic | ||||
Sequence: MAIKLNGSSRSFVP | ||||||
Transmembrane | 15-35 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: SLRVSAFLIFIFFVITYIIIY | ||||||
Topological domain | 36-814 | Lumenal | ||||
Sequence: NVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQENCSLERRRQLIGSSTFCFLLPSEMFFQDFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSFEISDIIEMRRVGRLFYETYLADRHLLARSLLAALRYKLQIPTREVRRNQAIPLFNSSFTAPKGSVVNVQANFDDEYLLGPLESRVESTSYAYNFTEFQLYSYDFWNIIMSPHYTKEFLVNAAELPTEAEFFEDTKIGFRPIEPGSGAEFSKALGGNRQREQFTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAVLSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHARYGDSMFYNSNHTCQMSMILTGAAFIHKNYLTAYTYEMPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHECMRLFTKIYGYNPLKFSQFRADSILFKTRLPQNHQKCFKYV |
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149663 | 1-814 | Exostosin-2 homolog | |||
Sequence: MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQENCSLERRRQLIGSSTFCFLLPSEMFFQDFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSFEISDIIEMRRVGRLFYETYLADRHLLARSLLAALRYKLQIPTREVRRNQAIPLFNSSFTAPKGSVVNVQANFDDEYLLGPLESRVESTSYAYNFTEFQLYSYDFWNIIMSPHYTKEFLVNAAELPTEAEFFEDTKIGFRPIEPGSGAEFSKALGGNRQREQFTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAVLSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHARYGDSMFYNSNHTCQMSMILTGAAFIHKNYLTAYTYEMPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHECMRLFTKIYGYNPLKFSQFRADSILFKTRLPQNHQKCFKYV | ||||||
Glycosylation | 36 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 227 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 322 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 454 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 492 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 685 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 726↔774 | |||||
Sequence: CEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHEC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length814
- Mass (Da)94,197
- Last updated2002-03-27 v2
- Checksum38FA58C5EB17DB16
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 604 | in Ref. 1; AAC47510 | ||||
Sequence: T → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |