GALT5_CAEEL
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 03-AUG-2022, entry version 152.
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}.
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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 EPD; Q95ZJ1; -.
DR PaxDb; Q95ZJ1; -.
DR PeptideAtlas; Q95ZJ1; -.
DR PRIDE; 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 CTD; 176736; -.
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; QFNWHAV; -.
DR OrthoDB; 606683at2759; -.
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 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 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
