GLT11_CAEEL
ID GLT11_CAEEL Reviewed; 605 AA.
AC Q7K755; Q9XW72;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 11;
DE Short=pp-GaNTase 11;
DE EC=2.4.1.41;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 11;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11;
GN Name=gly-11; ORFNames=Y75B8A.9;
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 [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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: May catalyze the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
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=2;
CC Name=a;
CC IsoId=Q7K755-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q7K755-2; Sequence=VSP_011242, VSP_011243;
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; AL033514; CAA22098.1; -; Genomic_DNA.
DR EMBL; AL033514; CAE47472.1; -; Genomic_DNA.
DR PIR; T27397; T27397.
DR RefSeq; NP_001022948.1; NM_001027777.3. [Q7K755-1]
DR RefSeq; NP_001022949.1; NM_001027778.3. [Q7K755-2]
DR AlphaFoldDB; Q7K755; -.
DR SMR; Q7K755; -.
DR BioGRID; 41826; 3.
DR STRING; 6239.Y75B8A.9a; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; Q7K755; -.
DR EPD; Q7K755; -.
DR PaxDb; Q7K755; -.
DR PeptideAtlas; Q7K755; -.
DR PRIDE; Q7K755; -.
DR EnsemblMetazoa; Y75B8A.9a.1; Y75B8A.9a.1; WBGene00001636. [Q7K755-1]
DR EnsemblMetazoa; Y75B8A.9b.1; Y75B8A.9b.1; WBGene00001636. [Q7K755-2]
DR GeneID; 176647; -.
DR KEGG; cel:CELE_Y75B8A.9; -.
DR UCSC; Y75B8A.9a; c. elegans. [Q7K755-1]
DR CTD; 176647; -.
DR WormBase; Y75B8A.9a; CE23021; WBGene00001636; gly-11. [Q7K755-1]
DR WormBase; Y75B8A.9b; CE35810; WBGene00001636; gly-11. [Q7K755-2]
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000165841; -.
DR InParanoid; Q7K755; -.
DR OMA; CHNQGAH; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q7K755; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q7K755; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001636; Expressed in pharyngeal muscle cell (C elegans) and 3 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:0030246; F:carbohydrate binding; 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 CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR027791; Galactosyl_T_C.
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; PF02709; Glyco_transf_7C; 1.
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 3: Inferred from homology;
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..605
FT /note="Putative polypeptide N-
FT acetylgalactosaminyltransferase 11"
FT /id="PRO_0000059154"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..605
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 481..605
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 49..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..271
FT /note="Catalytic subdomain A"
FT REGION 329..391
FT /note="Catalytic subdomain B"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 374..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 494..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 541..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 578..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 436
FT /note="G -> V (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011242"
FT VAR_SEQ 437..605
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011243"
SQ SEQUENCE 605 AA; 69597 MW; F84C132FA794C661 CRC64;
MLLLWRRKTV GLICLFSILL TIYLYVSMYP EDNERVWNSG NADIQRKHEK LNNGGQGRHD
FDDDEGAEKD EEDAVEKQNI AAPPLPKSFT TFPDRSKEIE IDTDLLGKIN GKAEDDLQVE
GYKKYQFNGL LSDRIGSRRK IKDSRNARCS SLTYSDSLPA ASIVVCYFNE SPSVLIRMVN
SIFDRTKPEH LHEILLVDDS SEWSNATDEA IKYREKHIIQ WEKVKFLKTD KNEGLIRAKI
FGARRANGEV LVFLDSHCEV NEEWLPPLLD QIKQNRRRVV CPIIDIIDAI TMKYVESPVC
TGGVNWAMTF KWDYPHRSYF EDPMNYVNPL KSPTMAGGLF AIDKEYFFEI GSYDEGMDVW
GAENVEISVR IWTCGGELLI MPCSRVGHIF RRQRPYGIKT DSMGKNSVRL ARVWLDEYLE
NFFEARPNYR TFTDYGDLTS RISLRRNLQC KPFKWYLENI YPELLPDNTP NQLNNQILVA
GKKYLIKMAN GTHCLSAENS QGRIANGNRV EMRKCNHMER MQQWKYSSTN ELRPMGSSRM
CLDSLRGISV ILCHNQGAHQ MWQVSNAGKL YSRSVNKCAT GSNDVSALST LKFCSLANSF
QFVEL
