GALT7_CAEEL
ID GALT7_CAEEL Reviewed; 601 AA.
AC O61397;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable N-acetylgalactosaminyltransferase 7;
DE EC=2.4.1.-;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
DE Short=pp-GaNTase 7;
GN Name=gly-7; ORFNames=Y46H3A.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).
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 -!- 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}.
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DR EMBL; AF031841; AAC13677.1; -; mRNA.
DR EMBL; FO081307; CCD70652.1; -; Genomic_DNA.
DR PIR; T42251; T42251.
DR RefSeq; NP_503512.1; NM_071111.3.
DR AlphaFoldDB; O61397; -.
DR SMR; O61397; -.
DR STRING; 6239.Y46H3A.6; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR EPD; O61397; -.
DR PaxDb; O61397; -.
DR PeptideAtlas; O61397; -.
DR EnsemblMetazoa; Y46H3A.6a.1; Y46H3A.6a.1; WBGene00001632.
DR GeneID; 178661; -.
DR KEGG; cel:CELE_Y46H3A.6; -.
DR UCSC; Y46H3A.6; c. elegans.
DR CTD; 178661; -.
DR WormBase; Y46H3A.6a; CE24309; WBGene00001632; gly-7.
DR eggNOG; KOG3737; Eukaryota.
DR GeneTree; ENSGT00940000167329; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; O61397; -.
DR OMA; FDDTHKE; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O61397; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:O61397; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001632; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O61397; 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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..601
FT /note="Probable N-acetylgalactosaminyltransferase 7"
FT /id="PRO_0000059150"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..601
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 477..595
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 61..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..265
FT /note="Catalytic subdomain A"
FT REGION 328..390
FT /note="Catalytic subdomain B"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 146..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 373..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 490..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 529..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 568..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 601 AA; 68108 MW; 1A7E744C93BDCDE7 CRC64;
MIIARKKLQL QRLWRQRGCR VATYICLGVL VLFGFVYNSK GNSMSSIKSD SAAQQFDDLD
DLTNKELPGG PDPNTIFRGS ELGNYEPKEP EIPSNQPGEH GKPVPVTDEE GMAAGRAAEK
EFGFNTYVSD MISMNRTIPD IRPEECKHWD YPEKLPTVSV VVVFHNEGWT PLLRTVHSVL
LRSPPELIEQ VVMVDDDSDK PHLKEKLDKY VTRFNGKVIV VRTEQREGLI NARSIGAKHS
TGEVVLFLDA HCEVNTNWLP PLLAPIKRNR KVMTVPVIDG IDSNSWEYRS VYGSPNAHHS
GIFEWGLLYK ETQITERETA HRKHNSQPFR SPTHAGGLFA INRLWFKELG YYDEGLQIWG
GEQYELSFKI WQCGGGIVFV PCSHVGHVYR SHMPYSFGKF SGKPVISINM MRVVKTWMDD
YSKYYLTREP QATNVNPGDI SAQLALRDKL QCKSFKWYME NVAYDVLKSY PMLPPNDVWG
EARNPATGKC LDRMGGIPGP MGATGCHGYG GNQLIRLNVQ GQMAQGEWCL TANGIRIQAN
HCVKGTVNGF WSYDRKTKQI IHSQKRQCIT VSESGSEVTL QTCTEDNERQ KFVWKEFYQS
S
