ID   GALT5_CAEEL             Reviewed;         626 AA.
AC   Q95ZJ1; O61391; O61392; O61393; Q95ZJ2; Q9U2J8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
DE            Short=pp-GaNTase 5;
DE            EC=2.4.1.41;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
GN   Name=gly-5; ORFNames=Y39E4B.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] (ISOFORMS A; B AND C).
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=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   -!- 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=3;
CC       Name=a; Synonyms=GLY5b, GLY-5b;
CC         IsoId=Q95ZJ1-1; Sequence=Displayed;
CC       Name=b; Synonyms=GLY5a, GLY-5a;
CC         IsoId=Q95ZJ1-2; Sequence=VSP_011238;
CC       Name=c; Synonyms=GLY5c, GLY-5c;
CC         IsoId=Q95ZJ1-3; Sequence=VSP_011239;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF031835; AAC13671.1; -; mRNA.
DR   EMBL; AF031836; AAC13672.1; -; mRNA.
DR   EMBL; AF031837; AAC13673.1; -; mRNA.
DR   EMBL; AL110487; CAB54435.1; -; Genomic_DNA.
DR   EMBL; AL110487; CAC42369.1; -; Genomic_DNA.
DR   EMBL; AL110487; CAC42368.1; -; Genomic_DNA.
DR   PIR; T42245; T42245.
DR   PIR; T42246; T42246.
DR   PIR; T42247; T42247.
DR   RefSeq; NP_001022850.1; NM_001027679.4.
DR   RefSeq; NP_001022851.1; NM_001027680.4.
DR   RefSeq; NP_001022852.1; NM_001027681.5. [Q95ZJ1-3]
DR   AlphaFoldDB; Q95ZJ1; -.
DR   SMR; Q95ZJ1; -.
DR   BioGRID; 41908; 18.
DR   DIP; DIP-26207N; -.
DR   IntAct; Q95ZJ1; 3.
DR   STRING; 6239.Y39E4B.12a.1; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q95ZJ1; 2 sites, No reported glycans.
DR   EPD; Q95ZJ1; -.
DR   PaxDb; 6239-Y39E4B-12a-1; -.
DR   PeptideAtlas; Q95ZJ1; -.
DR   EnsemblMetazoa; Y39E4B.12a.1; Y39E4B.12a.1; WBGene00001630. [Q95ZJ1-1]
DR   EnsemblMetazoa; Y39E4B.12a.2; Y39E4B.12a.2; WBGene00001630. [Q95ZJ1-1]
DR   EnsemblMetazoa; Y39E4B.12b.1; Y39E4B.12b.1; WBGene00001630. [Q95ZJ1-2]
DR   EnsemblMetazoa; Y39E4B.12b.2; Y39E4B.12b.2; WBGene00001630. [Q95ZJ1-2]
DR   EnsemblMetazoa; Y39E4B.12c.1; Y39E4B.12c.1; WBGene00001630. [Q95ZJ1-3]
DR   EnsemblMetazoa; Y39E4B.12c.2; Y39E4B.12c.2; WBGene00001630. [Q95ZJ1-3]
DR   GeneID; 176736; -.
DR   UCSC; Y39E4B.12c; c. elegans. [Q95ZJ1-1]
DR   AGR; WB:WBGene00001630; -.
DR   WormBase; Y39E4B.12a; CE24240; WBGene00001630; gly-5. [Q95ZJ1-1]
DR   WormBase; Y39E4B.12b; CE28119; WBGene00001630; gly-5. [Q95ZJ1-2]
DR   WormBase; Y39E4B.12c; CE28120; WBGene00001630; gly-5. [Q95ZJ1-3]
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000170662; -.
DR   InParanoid; Q95ZJ1; -.
DR   OMA; FSIDRAF; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q95ZJ1; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q95ZJ1; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00001630; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
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:SF131; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9-RELATED; 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; 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..626
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 5"
FT                   /id="PRO_0000059148"
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..626
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          488..610
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          174..284
FT                   /note="Catalytic subdomain A"
FT   REGION          345..407
FT                   /note="Catalytic subdomain B"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        165..399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        390..466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        502..521
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        544..557
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        583..598
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   VAR_SEQ         492..523
FT                   /note="VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG -> MRNAGGKNRQCIDYKP
FT                   SGGKTVGMYQCHN (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9525933"
FT                   /id="VSP_011238"
FT   VAR_SEQ         492..523
FT                   /note="VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG -> LRNAQTSQCLDSAVGE
FT                   EVENKAITPYPCHE (in isoform c)"
FT                   /evidence="ECO:0000303|PubMed:9525933"
FT                   /id="VSP_011239"
FT   CONFLICT        361
FT                   /note="K -> E (in Ref. 1; AAC13671/AAC13672/AAC13673)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   626 AA;  71382 MW;  561BD0576514B983 CRC64;
     MIIFKKKAIL KVLLLVPVFW ICSLIFFAAT SNDSSQIGSN NDLANKIAEA NFHPKAAKQD
     VIQGFGPPIE PEPVVENNKV EEEEQPGGNL AKPKFMVDPN DPIYKKGDAA QAGELGKAVV
     VDKTKLSTEE KAKYDKGMLN NAFNQYASDM ISVHRTLPTN IDAECKTEKY NENLPRTSVI
     ICFHNEAWSV LLRTVHSVLE RTPDHLLEEV VLVDDFSDMD HTKRPLEEYM SQFGGKVKIL
     RMEKREGLIR ARLRGAAVAT GEVLTYLDSH CECMEGWMEP LLDRIKRDPT TVVCPVIDVI
     DDNTFEYHHS KAYFTSVGGF DWGLQFNWHS IPERDRKNRT RPIDPVRSPT MAGGLFSIDK
     KYFEKLGTYD PGFDIWGGEN LELSFKIWMC GGTLEIVPCS HVGHVFRKRS PYKWRTGVNV
     LKRNSIRLAE VWLDDYKTYY YERINNQLGD FGDISSRKKL REDLGCKSFK WYLDNIYPEL
     FVPGESVAKG EVRNSAVQPA RCLDCMVGRH EKNRPVGTYQ CHGQGGNQYW MLSKDGEIRR
     DESCVDYAGS DVMVFPCHGM KGNQEWRYNH DTGRLQHAVS QKCLGMTKDG AKLEMVACQY
     DDPYQHWKFK EYNEAKAIEH GAKPPS
//