GALT4_CAEEL
ID GALT4_CAEEL Reviewed; 589 AA.
AC Q8I136; O61390;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 4;
DE Short=pp-GaNTase 4;
DE EC=2.4.1.41;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 4;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4;
GN Name=gly-4; ORFNames=Y116F11B.12;
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), 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], 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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q8I136-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q8I136-2; Sequence=VSP_011236, VSP_011237;
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; AF031834; AAC13670.1; -; mRNA.
DR EMBL; AL132943; CAB81985.3; -; Genomic_DNA.
DR EMBL; AL132943; CAC14394.1; -; Genomic_DNA.
DR PIR; T42244; T42244.
DR RefSeq; NP_001024216.1; NM_001029045.3. [Q8I136-1]
DR RefSeq; NP_507850.2; NM_075449.7. [Q8I136-2]
DR AlphaFoldDB; Q8I136; -.
DR SMR; Q8I136; -.
DR BioGRID; 45263; 3.
DR DIP; DIP-26941N; -.
DR IntAct; Q8I136; 1.
DR STRING; 6239.Y116F11B.12a.1; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR EPD; Q8I136; -.
DR PaxDb; Q8I136; -.
DR PeptideAtlas; Q8I136; -.
DR EnsemblMetazoa; Y116F11B.12a.1; Y116F11B.12a.1; WBGene00001629. [Q8I136-1]
DR EnsemblMetazoa; Y116F11B.12a.2; Y116F11B.12a.2; WBGene00001629. [Q8I136-1]
DR EnsemblMetazoa; Y116F11B.12b.1; Y116F11B.12b.1; WBGene00001629. [Q8I136-2]
DR GeneID; 180302; -.
DR KEGG; cel:CELE_Y116F11B.12; -.
DR UCSC; Y116F11B.12b.1; c. elegans. [Q8I136-1]
DR CTD; 180302; -.
DR WormBase; Y116F11B.12a; CE26046; WBGene00001629; gly-4. [Q8I136-1]
DR WormBase; Y116F11B.12b; CE32074; WBGene00001629; gly-4. [Q8I136-2]
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000156958; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8I136; -.
DR OMA; LVFRWEF; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8I136; -.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8I136; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001629; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q8I136; 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; 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; 2.
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..589
FT /note="Polypeptide N-acetylgalactosaminyltransferase 4"
FT /id="PRO_0000059147"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..589
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 458..589
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 33..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..255
FT /note="Catalytic subdomain A"
FT REGION 315..377
FT /note="Catalytic subdomain B"
FT COMPBIAS 37..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 360..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 471..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 514..531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 553..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 453
FT /note="E -> D (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011236"
FT VAR_SEQ 454..589
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011237"
SQ SEQUENCE 589 AA; 67031 MW; 108D621D91A329D2 CRC64;
MLPRMLKMKT VGTVLAVIWL FGLAFIYVQS TSSSLRPPGR HPPPLPQLDP LIPQNPPQND
EIRPKKSAPP IPTINLAEDT TIHERTEKDV TWKTFDVEKF LNKGKWHQGE DKYKANSFNQ
EASDALNPTR KIPDSREPQC RDVDYSKVGM QPTTVIITYH NEARSSLLRT VFSVFNQSPE
ELLLEIVLVD DNSQDVEIGK ELAQIQRITV LRNNQREGLI RSRVKGAQVA RAPVLTFLDS
HIECNQKWLE PLLARIAENP KAVVAPIIDV INVDNFNYVG ASADLRGGFD WTLVFRWEFM
NEQLRKERHA HPTAPIRSPT MAGGLFAISK EWFNELGTYD LDMEVWGGEN LEMSFRVWQC
GGSLEIMPCS RVGHVFRKKH PYTFPGGSGN VFQKNTRRAA EVWMDEYKAI YLKNVPSARF
VNFGDITDRL AIRDRLQCKS FKWYLENVYP QLEIPRKTPG KSFQMKIGNL CLDSMARKES
EAPGLFGCHG TGGNQEWVFD QLTKTFKNAI SQLCLDFSSN TENKTVTMVK CENLRPDTMV
VEKNGWLTQG GKCLTVNQGS GGDWLIYGAH CELNNGAQRW IFEKLDTYE
