GALT6_CAEEL
ID GALT6_CAEEL Reviewed; 618 AA.
AC O61394; O61395; O61396;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable N-acetylgalactosaminyltransferase 6;
DE EC=2.4.1.-;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
DE Short=pp-GaNTase 6;
GN Name=gly-6; ORFNames=H38K22.5;
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] (ISOFORMS A; B AND C).
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).
CC -!- FUNCTION: Probable glycopeptide transferase involved in O-linked
CC oligosaccharide biosynthesis. Glycopeptide transferases catalyze the
CC transfer of an N-acetyl-D-galactosamine residue to an already
CC glycosylated peptide (By similarity). In contrast to other members of
CC the family, it does not act as a peptide transferase that transfers
CC GalNAc onto serine or threonine residue on peptides that have been
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a; Synonyms=GLY6a, GLY-6a;
CC IsoId=O61394-1; Sequence=Displayed;
CC Name=b; Synonyms=GLY6b, GLY-6b;
CC IsoId=O61394-2; Sequence=VSP_011240;
CC Name=c; Synonyms=GLY6c, GLY-6c;
CC IsoId=O61394-3; Sequence=VSP_011241;
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 -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF031838; AAC13674.1; -; mRNA.
DR EMBL; AF031839; AAC13675.1; -; mRNA.
DR EMBL; AF031840; AAC13676.1; -; mRNA.
DR EMBL; AL024499; CAA19707.1; -; Genomic_DNA.
DR EMBL; AL024499; CAC42317.1; -; Genomic_DNA.
DR EMBL; AL024499; CAC42318.1; -; Genomic_DNA.
DR PIR; T42248; T42248.
DR PIR; T42249; T42249.
DR PIR; T42250; T42250.
DR RefSeq; NP_001022644.1; NM_001027473.2. [O61394-1]
DR RefSeq; NP_001022645.1; NM_001027474.2.
DR RefSeq; NP_001022646.1; NM_001027475.2. [O61394-3]
DR AlphaFoldDB; O61394; -.
DR SMR; O61394; -.
DR STRING; 6239.H38K22.5a.1; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR EPD; O61394; -.
DR PaxDb; O61394; -.
DR EnsemblMetazoa; H38K22.5a.1; H38K22.5a.1; WBGene00001631. [O61394-1]
DR EnsemblMetazoa; H38K22.5a.2; H38K22.5a.2; WBGene00001631. [O61394-1]
DR EnsemblMetazoa; H38K22.5b.1; H38K22.5b.1; WBGene00001631. [O61394-2]
DR EnsemblMetazoa; H38K22.5b.2; H38K22.5b.2; WBGene00001631. [O61394-2]
DR EnsemblMetazoa; H38K22.5c.1; H38K22.5c.1; WBGene00001631. [O61394-3]
DR GeneID; 175558; -.
DR UCSC; H38K22.5c.1; c. elegans. [O61394-1]
DR CTD; 175558; -.
DR WormBase; H38K22.5a; CE18833; WBGene00001631; gly-6. [O61394-1]
DR WormBase; H38K22.5b; CE28040; WBGene00001631; gly-6. [O61394-2]
DR WormBase; H38K22.5c; CE28041; WBGene00001631; gly-6. [O61394-3]
DR eggNOG; KOG3736; Eukaryota.
DR InParanoid; O61394; -.
DR OMA; VWMDEWA; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O61394; -.
DR Reactome; R-CEL-190372; FGFR3c ligand binding and activation.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:O61394; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001631; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O61394; baseline and differential.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..618
FT /note="Probable N-acetylgalactosaminyltransferase 6"
FT /id="PRO_0000059149"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..618
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 474..609
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 156..267
FT /note="Catalytic subdomain A"
FT REGION 327..389
FT /note="Catalytic subdomain B"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 372..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 487..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 530..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 575..597
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 479..512
FT /note="TSSSNSSVCLAWTLRSSGIKTASTADCLKIFHKT -> SNSNYCTAFRPGDT
FT GPKNHRLLGSPCTMGFDLW (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9525933"
FT /id="VSP_011240"
FT VAR_SEQ 495..618
FT /note="SGIKTASTADCLKIFHKTQLWLYTGDRRIRTDEHLCLSVVQLLHTTSDWKIQ
FT LKECAGFDTEYWDFKPKIGRFQNRKTGLCLASPDIFDPTKDEFNPPIVQKCRSSNDRQN
FT WTITEMSWLPEHP -> CPTQTTAQPSGQVTRVPKITDCSDHPVLWDSTCGSCGSTLAT
FT VEYVQMSIYAYQLFNFFTQLPIGKFN (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9525933"
FT /id="VSP_011241"
SQ SEQUENCE 618 AA; 71115 MW; 738A01F7BB445E22 CRC64;
MIASLIRSRR RSRRCVVYSV FLFGFLALWG SFALALVFLS DMYIGEDQIS TQKAIKPIAR
SNYHVVVGHY NGNLPEDKKR NLTSEELNAN LYAPHDDWGE GGAGVSHLTP EQQKLADSTF
AVNQFNLLVS DGISVRRSLP EIRKPSCRNM TYPDNLPTTS VIIVYHNEAY STLLRTVWSV
IDRSPKELLK EIILVDDFSD REFLRYPTLD TTLKPLPTDI KIIRSKERVG LIRARMMGAQ
EAQGDVLTFL DSHCECTKGW LEPLLTRIKL NRKAVPCPVI DIINDNTFQY QKGIEMFRGG
FNWNLQFRWY GMPTAMAKQH LLDPTGPIES PTMAGGLFSI NRNYFEELGE YDPGMDIWGG
ENLEMSFRIW QCGGRVEILP CSHVGHVFRK SSPHDFPGKS SGKVLNTNLL RVAEVWMDDW
KHYFYKIAPQ AHRMRSSIDV SERVELRKKL NCKSFKWYLQ NVFQDHFLPT PLDRFGRMTS
SSNSSVCLAW TLRSSGIKTA STADCLKIFH KTQLWLYTGD RRIRTDEHLC LSVVQLLHTT
SDWKIQLKEC AGFDTEYWDF KPKIGRFQNR KTGLCLASPD IFDPTKDEFN PPIVQKCRSS
NDRQNWTITE MSWLPEHP
