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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Metal bindingi203 – 2031ManganeseBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Metal bindingi205 – 2051ManganeseBy similarity
Binding sitei308 – 3081SubstrateBy similarity
Metal bindingi336 – 3361ManganeseBy similarity
Binding sitei339 – 3391SubstrateBy similarity
Binding sitei344 – 3441SubstrateBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
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
ProteomesiUP000001940: Chromosome III

Organism-specific databases

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

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicSequence Analysis
Transmembranei4 – 2421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 421397LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Probable N-acetylgalactosaminyltransferase 8PRO_0000059151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)1 Publication
Glycosylationi58 – 581N-linked (GlcNAc...)1 Publication
Disulfide bondi98 ↔ 331By similarity
Disulfide bondi322 ↔ 399By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO45293.

Interactioni

Protein-protein interaction databases

BioGridi41776. 2 interactions.
DIPiDIP-24790N.
MINTiMINT-1070872.
STRINGi6239.Y66A7A.6.1.

Structurei

3D structure databases

ProteinModelPortaliO45293.
SMRiO45293. Positions 76-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 219114Catalytic subdomain AAdd
BLAST
Regioni277 – 33963Catalytic subdomain BAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi418 – 4214Prevents secretion from ERPROSITE-ProRule annotation

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

eggNOGiNOG295988.
GeneTreeiENSGT00670000097647.
HOGENOMiHOG000038227.
InParanoidiO45293.
OMAiPENNVKP.
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. Positions 76-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41776. 2 interactions.
DIPiDIP-24790N.
MINTiMINT-1070872.
STRINGi6239.Y66A7A.6.1.

Protein family/group databases

CAZyiGT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbiO45293.

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

eggNOGiNOG295988.
GeneTreeiENSGT00670000097647.
HOGENOMiHOG000038227.
InParanoidiO45293.
OMAiPENNVKP.
PhylomeDBiO45293.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi893222.
PROiO45293.

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans."
    Hagen F.K., Nehrke K.
    J. Biol. Chem. 273:8268-8277(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-58, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

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: January 7, 2015
This is version 102 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

External Data

Dasty 3

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 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.