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Protein

Probable N-acetylgalactosaminyltransferase 8

Gene

gly-8

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potential glycopeptide transferase involved in O-linked oligosaccharide biosynthesis (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.By similarity

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei147SubstrateBy similarity1
Binding sitei180SubstrateBy similarity1
Metal bindingi203ManganeseBy similarity1
Binding sitei204SubstrateBy similarity1
Metal bindingi205ManganeseBy similarity1
Binding sitei308SubstrateBy similarity1
Metal bindingi336ManganeseBy similarity1
Binding sitei339SubstrateBy similarity1
Binding sitei344SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable N-acetylgalactosaminyltransferase 8 (EC:2.4.1.-)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 8
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Short name:
pp-GaNTase 8
Gene namesi
Name:gly-8
ORF Names:Y66A7A.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiY66A7A.6; CE15691; WBGene00001633; gly-8.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 3CytoplasmicSequence analysis3
Transmembranei4 – 24Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini25 – 421LumenalSequence analysisAdd BLAST397

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591511 – 421Probable N-acetylgalactosaminyltransferase 8Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)1 Publication1
Glycosylationi58N-linked (GlcNAc...)1 Publication1
Disulfide bondi98 ↔ 331By similarity
Disulfide bondi322 ↔ 399By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO45293.
PaxDbiO45293.
PeptideAtlasiO45293.
PRIDEiO45293.

Expressioni

Gene expression databases

BgeeiWBGene00001633.

Interactioni

Protein-protein interaction databases

BioGridi41776. 2 interactors.
DIPiDIP-24790N.
MINTiMINT-1070872.
STRINGi6239.Y66A7A.6.3.

Structurei

3D structure databases

ProteinModelPortaliO45293.
SMRiO45293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 219Catalytic subdomain AAdd BLAST114
Regioni277 – 339Catalytic subdomain BAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi418 – 421Prevents secretion from ERPROSITE-ProRule annotation4

Domaini

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.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00670000097647.
HOGENOMiHOG000038227.
InParanoidiO45293.
OMAiLCEEEKY.
OrthoDBiEOG091G085O.
PhylomeDBiO45293.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O45293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRHVVLSIF VFAGIVFAAE EAEKLPKCEH VDPYENLEGW LDLKPLTERK
60 70 80 90 100
CNHTLKENLT EAESKKSEWG IKSFAFDALS SEKLGPNRNV GKQAHKLCEE
110 120 130 140 150
EKYDASYSTS VVVIHHNEAL STILRMINGI IEFTPKSLLK EIVLYEDASE
160 170 180 190 200
EDHVLTKHLE KFAKIKGLED KLIIKRSEYR QGLIRAKVHA SRLATGEVIV
210 220 230 240 250
FMDSHCEVAE RWLEPLLQPI KEDPKSIVLP VVDLINPVSF DYSPSMVAKS
260 270 280 290 300
GFDWGFTFKW IYLPWEYFET PENNVKPFNS PAMPGGLLAM RKEYFVELGE
310 320 330 340 350
YDMGMEIWGS ENIELSLKAW LCGGRVVVAP CSRVGHVFRM RRPYTSKPGM
360 370 380 390 400
DTALYNAVRV AKTWLGEYES KFFAVKPRGA KMVFGDLTEP MQVKDRLKCK
410 420
DMKWFIENVY PELEPKVHDE L
Length:421
Mass (Da):48,358
Last modified:June 1, 1998 - v1
Checksum:i3FA38E18702D087D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031842 mRNA. Translation: AAC13678.1.
AL590342 Genomic DNA. Translation: CAC35860.1.
PIRiT42252.
RefSeqiNP_499504.1. NM_067103.4.
UniGeneiCel.19663.

Genome annotation databases

EnsemblMetazoaiY66A7A.6.1; Y66A7A.6.1; WBGene00001633.
Y66A7A.6.2; Y66A7A.6.2; WBGene00001633.
GeneIDi176595.
KEGGicel:CELE_Y66A7A.6.
UCSCiY66A7A.6.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031842 mRNA. Translation: AAC13678.1.
AL590342 Genomic DNA. Translation: CAC35860.1.
PIRiT42252.
RefSeqiNP_499504.1. NM_067103.4.
UniGeneiCel.19663.

3D structure databases

ProteinModelPortaliO45293.
SMRiO45293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41776. 2 interactors.
DIPiDIP-24790N.
MINTiMINT-1070872.
STRINGi6239.Y66A7A.6.3.

Protein family/group databases

CAZyiGT27. Glycosyltransferase Family 27.

Proteomic databases

EPDiO45293.
PaxDbiO45293.
PeptideAtlasiO45293.
PRIDEiO45293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY66A7A.6.1; Y66A7A.6.1; WBGene00001633.
Y66A7A.6.2; Y66A7A.6.2; WBGene00001633.
GeneIDi176595.
KEGGicel:CELE_Y66A7A.6.
UCSCiY66A7A.6.1. c. elegans.

Organism-specific databases

CTDi176595.
WormBaseiY66A7A.6; CE15691; WBGene00001633; gly-8.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00670000097647.
HOGENOMiHOG000038227.
InParanoidiO45293.
OMAiLCEEEKY.
OrthoDBiEOG091G085O.
PhylomeDBiO45293.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

PROiO45293.

Gene expression databases

BgeeiWBGene00001633.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGALT8_CAEEL
AccessioniPrimary (citable) accession number: O45293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Caution

In contrast to other members of the family, it lacks the C-terminal ricin B-type lectin domain, which usually contributes to the glycopeptide specificity. It instead contains a motif that may retain its secretion form the endoplasmic reticulum.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.