GALT8_CAEEL
ID GALT8_CAEEL Reviewed; 421 AA.
AC O45293;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable N-acetylgalactosaminyltransferase 8;
DE EC=2.4.1.-;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 8;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8;
DE Short=pp-GaNTase 8;
GN Name=gly-8; ORFNames=Y66A7A.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9525933; DOI=10.1074/jbc.273.14.8268;
RA Hagen F.K., Nehrke K.;
RT "cDNA cloning and expression of a family of UDP-N-acetyl-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence
RT homologs from Caenorhabditis elegans.";
RL J. Biol. Chem. 273:8268-8277(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Potential glycopeptide transferase involved in O-linked
CC oligosaccharide biosynthesis (By similarity). In contrast to other
CC members of the family, it does not act as a peptide transferase that
CC transfers GalNAc onto serine or threonine residue on peptides that have
CC been tested. Some peptide transferase activity is however not excluded,
CC considering that its appropriate peptide substrate may remain
CC unidentified. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it lacks the C-
CC terminal ricin B-type lectin domain, which usually contributes to the
CC glycopeptide specificity. It instead contains a motif that may retain
CC its secretion form the endoplasmic reticulum. {ECO:0000305}.
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DR EMBL; AF031842; AAC13678.1; -; mRNA.
DR EMBL; AL590342; CAC35860.1; -; Genomic_DNA.
DR PIR; T42252; T42252.
DR RefSeq; NP_499504.1; NM_067103.4.
DR AlphaFoldDB; O45293; -.
DR SMR; O45293; -.
DR BioGRID; 41776; 8.
DR DIP; DIP-24790N; -.
DR STRING; 6239.Y66A7A.6.2; -.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; O45293; -.
DR EPD; O45293; -.
DR PaxDb; O45293; -.
DR PeptideAtlas; O45293; -.
DR PRIDE; O45293; -.
DR EnsemblMetazoa; Y66A7A.6.1; Y66A7A.6.1; WBGene00001633.
DR UCSC; Y66A7A.6.1; c. elegans.
DR WormBase; Y66A7A.6; CE15691; WBGene00001633; gly-8.
DR eggNOG; KOG3736; Eukaryota.
DR HOGENOM; CLU_013477_0_0_1; -.
DR InParanoid; O45293; -.
DR OMA; DMGMEIW; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O45293; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:O45293; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001633; Expressed in larva and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Probable N-acetylgalactosaminyltransferase 8"
FT /id="PRO_0000059151"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..421
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 106..219
FT /note="Catalytic subdomain A"
FT REGION 277..339
FT /note="Catalytic subdomain B"
FT MOTIF 418..421
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 98..331
FT /evidence="ECO:0000250"
FT DISULFID 322..399
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 48358 MW; 3FA38E18702D087D CRC64;
MRRHVVLSIF VFAGIVFAAE EAEKLPKCEH VDPYENLEGW LDLKPLTERK CNHTLKENLT
EAESKKSEWG IKSFAFDALS SEKLGPNRNV GKQAHKLCEE EKYDASYSTS VVVIHHNEAL
STILRMINGI IEFTPKSLLK EIVLYEDASE EDHVLTKHLE KFAKIKGLED KLIIKRSEYR
QGLIRAKVHA SRLATGEVIV FMDSHCEVAE RWLEPLLQPI KEDPKSIVLP VVDLINPVSF
DYSPSMVAKS GFDWGFTFKW IYLPWEYFET PENNVKPFNS PAMPGGLLAM RKEYFVELGE
YDMGMEIWGS ENIELSLKAW LCGGRVVVAP CSRVGHVFRM RRPYTSKPGM DTALYNAVRV
AKTWLGEYES KFFAVKPRGA KMVFGDLTEP MQVKDRLKCK DMKWFIENVY PELEPKVHDE
L
