GALT9_CAEEL
ID GALT9_CAEEL Reviewed; 579 AA.
AC Q9U2C4; O61398; Q5GMH7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable N-acetylgalactosaminyltransferase 9;
DE EC=2.4.1.-;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
DE Short=pp-GaNTase 9;
GN Name=gly-9; ORFNames=Y47D3A.23;
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] (ISOFORM A).
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], 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: 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=2;
CC Name=a;
CC IsoId=Q9U2C4-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9U2C4-2; Sequence=VSP_020151;
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; AF031843; AAC13679.1; -; mRNA.
DR EMBL; AL117202; CAB57897.1; -; Genomic_DNA.
DR EMBL; AL117202; CAI46621.1; -; Genomic_DNA.
DR PIR; T31549; T31549.
DR RefSeq; NP_001022876.1; NM_001027705.2. [Q9U2C4-1]
DR RefSeq; NP_001022877.1; NM_001027706.2.
DR AlphaFoldDB; Q9U2C4; -.
DR SMR; Q9U2C4; -.
DR STRING; 6239.Y47D3A.23a; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR EPD; Q9U2C4; -.
DR PaxDb; Q9U2C4; -.
DR PeptideAtlas; Q9U2C4; -.
DR EnsemblMetazoa; Y47D3A.23a.1; Y47D3A.23a.1; WBGene00012934. [Q9U2C4-1]
DR EnsemblMetazoa; Y47D3A.23b.1; Y47D3A.23b.1; WBGene00012934. [Q9U2C4-2]
DR GeneID; 176557; -.
DR KEGG; cel:CELE_Y47D3A.23; -.
DR UCSC; Y47D3A.23a; c. elegans. [Q9U2C4-1]
DR CTD; 176557; -.
DR WormBase; Y47D3A.23a; CE24334; WBGene00012934; gly-9. [Q9U2C4-1]
DR WormBase; Y47D3A.23b; CE37859; WBGene00012934; gly-9. [Q9U2C4-2]
DR eggNOG; KOG3736; Eukaryota.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q9U2C4; -.
DR OMA; IIFFNEP; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q9U2C4; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9U2C4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012934; Expressed in adult organism 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: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..579
FT /note="Probable N-acetylgalactosaminyltransferase 9"
FT /id="PRO_0000059152"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..579
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 450..574
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 133..243
FT /note="Catalytic subdomain A"
FT REGION 302..364
FT /note="Catalytic subdomain B"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 347..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 464..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 507..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 545..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..254
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020151"
FT CONFLICT 203
FT /note="V -> D (in Ref. 1; AAC13679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 66430 MW; 2F50B222CFB13597 CRC64;
MLRYIIPRKK GTFVIAAFLT VAFFCIVAYH RNDRRRTKFQ FPDIEKYAEE LVRLPETWNG
ELHQIPNYTA PREGPGEKGK PVVLTGKDAE LGQADMKKWF MNVHASDKIS LDRDVPDPRI
QACKDIKYDY AALPKTSVII IFTDEAWTPL LRTVHSVINR SPPELLQEVI LLDDNSKRQE
LQEPLDEHIK RFGGKVRLIR KHVRHGLIRA KLAGAREAVG DIIVFLDSHC EANHGWLEPI
VQRISDERTA IVCPMIDSIS DNTLAYHGDW SLSTGGFSWA LHFTWEGLSE EEQKRRTKPT
DYIRSPTMAG GLLAANREYF FEVGGYDEEM DIWGGENLEI SFRAWMCGGS IEFIPCSHVG
HIFRAGHPYN MTGRNNNKDV HGTNSKRLAE VWMDDYKRLY YMHREDLRTK DVGDLTARHE
LRKRLNCKPF KWFLDNIAKG KFIMDEDVVA YGALHTVVSG TRMCTDTLQR DEKMSQLLGV
FHCQGKGSSP QLMSLSKEGN LRRENTCASE ENGNIRMKTC SKKAQFNERW AYENKMIRNL
KSGKCMSTAN LKPGDNAIVV ECDEKDEHQK WNFIDPAKA
