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   27-MAR-2024, entry version 154.
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.
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   GlyCosmos; Q8I136; 1 site, No reported glycans.
DR   EPD; Q8I136; -.
DR   PaxDb; 6239-Y116F11B-12a-1; -.
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   AGR; WB:WBGene00001629; -.
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; 202750at2759; -.
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 cell types or 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: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; 2.80.10.50; -; 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   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF119; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 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
//