GALT3_CAEEL
ID GALT3_CAEEL Reviewed; 612 AA.
AC P34678; Q9U003;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3;
DE EC=2.4.1.41;
DE AltName: Full=GalNAc-T1;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3;
DE Short=pp-GaNTase 3;
GN Name=gly-3; ORFNames=ZK688.8;
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], AND ENZYME ACTIVITY.
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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: Catalyzes 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.
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 Evidence={ECO:0000269|PubMed:9525933};
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 Evidence={ECO:0000269|PubMed:9525933};
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; AF031833; AAC13669.1; -; mRNA.
DR EMBL; FO080277; CCD62541.1; -; Genomic_DNA.
DR PIR; A88515; A88515.
DR PIR; T42243; T42243.
DR RefSeq; NP_498722.1; NM_066321.5.
DR AlphaFoldDB; P34678; -.
DR SMR; P34678; -.
DR BioGRID; 41319; 13.
DR STRING; 6239.ZK688.8; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR EPD; P34678; -.
DR PaxDb; P34678; -.
DR PeptideAtlas; P34678; -.
DR EnsemblMetazoa; ZK688.8.1; ZK688.8.1; WBGene00001628.
DR GeneID; 176112; -.
DR KEGG; cel:CELE_ZK688.8; -.
DR UCSC; ZK688.8.1; c. elegans.
DR CTD; 176112; -.
DR WormBase; ZK688.8; CE29649; WBGene00001628; gly-3.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000169874; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; P34678; -.
DR OMA; FYKMVPA; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; P34678; -.
DR Reactome; R-CEL-190372; FGFR3c ligand binding and activation.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:P34678; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001628; Expressed in germ line (C elegans) and 4 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; IDA:WormBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:WormBase.
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..612
FT /note="Polypeptide N-acetylgalactosaminyltransferase 3"
FT /id="PRO_0000059146"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..612
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 478..607
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 61..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..279
FT /note="Catalytic subdomain A"
FT REGION 339..401
FT /note="Catalytic subdomain B"
FT COMPBIAS 71..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 384..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 496..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 536..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 582..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 612 AA; 68912 MW; 3031C2FE933F9858 CRC64;
MLSVGGGRSA VCRAVIATSI VWLLIDVVIL FYYLDPSTSQ QQPFPEDNRI LNRARRIEPL
PPAAQHDSDP DAHPIQPEKQ EKQVYPVDKE TANQLRKLME TQAFGPGYHG QGGTGVTVPE
DKKTIKEKRF LENQFNVVAS EMISVNRTLP DYRSDACRTS GNNLKTAGMP KTSIIIVFHN
EAWTTLLRTL HSVINRSPRH LLEEIILVDD KSDRDYLVKP LDSYIKMFPI PIHLVHLENR
SGLIRARLTG SEMAKGKILL FLDAHVEVTD GWLEPLVSRV AEDRKRVVAP IIDVISDDTF
EYVTASETTW GGFNWHLNFR WYAVPKRELN RRGSDRSMPI QTPTIAGGLF AIDKQFFYDI
GSYDEGMQVW GGENLEISFR VWMCGGSLEI HPCSRVGHVF RKQTPYTFPG GTAKVIHHNA
ARTAEVWMDE YKAFFYKMVP AARNVEAGDV SERKKLRETL QCKSFKWYLE NIYPEAPLPA
DFRSLGAIVN RFTEKCVDTN GKKDGQAPGI QACHGAGGNQ AWSLTGKGEI RSDDLCLSSG
HVYQIGSELK LERCSVSKIN VKHVFVFDDQ AGTLLHKKTG KCVTGADQRV TLDECGLGRK
DQMWQLEGYQ SP
