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   24-JAN-2024, entry version 148.
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; 9.
DR   DIP; DIP-24790N; -.
DR   STRING; 6239.Y66A7A.6.2; -.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; O45293; 2 sites, No reported glycans.
DR   iPTMnet; O45293; -.
DR   EPD; O45293; -.
DR   PaxDb; 6239-Y66A7A-6-2; -.
DR   PeptideAtlas; O45293; -.
DR   EnsemblMetazoa; Y66A7A.6.1; Y66A7A.6.1; WBGene00001633.
DR   UCSC; Y66A7A.6.1; c. elegans.
DR   AGR; WB:WBGene00001633; -.
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; 202750at2759; -.
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 cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR045885; GalNAc-T.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF116; N-ACETYLGALACTOSAMINYLTRANSFERASE 8-RELATED; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//