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Probable N-acetylgalactosaminyltransferase 6 (EC 2.4.1.-) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6) (pp-GaNTase 6)

 GALT6_CAEEL             Reviewed;         618 AA.
O61394; O61395; O61396;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=Probable N-acetylgalactosaminyltransferase 6;
EC=2.4.1.-;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
Short=pp-GaNTase 6;
Name=gly-6; ORFNames=H38K22.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
STRAIN=Bristol N2;
PubMed=9525933; DOI=10.1074/jbc.273.14.8268;
Hagen F.K., Nehrke K.;
"cDNA cloning and expression of a family of UDP-N-acetyl-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence
homologs from Caenorhabditis elegans.";
J. Biol. Chem. 273:8268-8277(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
-!- FUNCTION: Probable glycopeptide transferase involved in O-linked
oligosaccharide biosynthesis. Glycopeptide transferases catalyze
the transfer of an N-acetyl-D-galactosamine residue to an already
glycosylated peptide (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. {ECO:0000250}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a; Synonyms=GLY6a, GLY-6a;
IsoId=O61394-1; Sequence=Displayed;
Name=b; Synonyms=GLY6b, GLY-6b;
IsoId=O61394-2; Sequence=VSP_011240;
Name=c; Synonyms=GLY6c, GLY-6c;
IsoId=O61394-3; Sequence=VSP_011241;
-!- DOMAIN: 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. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
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EMBL; AF031838; AAC13674.1; -; mRNA.
EMBL; AF031839; AAC13675.1; -; mRNA.
EMBL; AF031840; AAC13676.1; -; mRNA.
EMBL; AL024499; CAA19707.1; -; Genomic_DNA.
EMBL; AL024499; CAC42317.1; -; Genomic_DNA.
EMBL; AL024499; CAC42318.1; -; Genomic_DNA.
PIR; T42248; T42248.
PIR; T42249; T42249.
PIR; T42250; T42250.
RefSeq; NP_001022644.1; NM_001027473.2. [O61394-1]
RefSeq; NP_001022645.1; NM_001027474.2.
RefSeq; NP_001022646.1; NM_001027475.2.
UniGene; Cel.8088; -.
ProteinModelPortal; O61394; -.
SMR; O61394; -.
STRING; 6239.H38K22.5a.1; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
EPD; O61394; -.
PaxDb; O61394; -.
PRIDE; O61394; -.
EnsemblMetazoa; H38K22.5a.1; H38K22.5a.1; WBGene00001631. [O61394-1]
EnsemblMetazoa; H38K22.5a.2; H38K22.5a.2; WBGene00001631. [O61394-1]
GeneID; 175558; -.
KEGG; cel:CELE_H38K22.5; -.
UCSC; H38K22.5c.1; c. elegans. [O61394-1]
CTD; 175558; -.
WormBase; H38K22.5a; CE18833; WBGene00001631; gly-6. [O61394-1]
WormBase; H38K22.5b; CE28040; WBGene00001631; gly-6. [O61394-2]
WormBase; H38K22.5c; CE28041; WBGene00001631; gly-6. [O61394-3]
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
InParanoid; O61394; -.
KO; K00710; -.
OMA; IIVYHNE; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; O61394; -.
UniPathway; UPA00378; -.
PRO; PR:O61394; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00001631; -.
ExpressionAtlas; O61394; baseline and differential.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 618 Probable N-
acetylgalactosaminyltransferase 6.
/FTId=PRO_0000059149.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 39 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 40 618 Lumenal. {ECO:0000255}.
DOMAIN 474 609 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 156 267 Catalytic subdomain A.
REGION 327 389 Catalytic subdomain B.
METAL 251 251 Manganese. {ECO:0000250}.
METAL 253 253 Manganese. {ECO:0000250}.
METAL 386 386 Manganese. {ECO:0000250}.
BINDING 197 197 Substrate. {ECO:0000250}.
BINDING 228 228 Substrate. {ECO:0000250}.
BINDING 252 252 Substrate. {ECO:0000250}.
BINDING 358 358 Substrate. {ECO:0000250}.
BINDING 389 389 Substrate. {ECO:0000250}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 147 381 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 372 452 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 487 505 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 530 550 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 575 597 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 479 512 TSSSNSSVCLAWTLRSSGIKTASTADCLKIFHKT -> SNS
NYCTAFRPGDTGPKNHRLLGSPCTMGFDLW (in
isoform b). {ECO:0000303|PubMed:9525933}.
/FTId=VSP_011240.
VAR_SEQ 495 618 SGIKTASTADCLKIFHKTQLWLYTGDRRIRTDEHLCLSVVQ
LLHTTSDWKIQLKECAGFDTEYWDFKPKIGRFQNRKTGLCL
ASPDIFDPTKDEFNPPIVQKCRSSNDRQNWTITEMSWLPEH
P -> CPTQTTAQPSGQVTRVPKITDCSDHPVLWDSTCGSC
GSTLATVEYVQMSIYAYQLFNFFTQLPIGKFN (in
isoform c). {ECO:0000303|PubMed:9525933}.
/FTId=VSP_011241.
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


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