GLT10_CAEEL
ID GLT10_CAEEL Reviewed; 684 AA.
AC O45947; Q2HQM0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 10;
DE Short=pp-GaNTase 10;
DE EC=2.4.1.41;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 10;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10;
GN Name=gly-10; ORFNames=Y45F10D.3;
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 [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).
RN [2]
RP IDENTIFICATION.
RX PubMed=15987734; DOI=10.1091/mbc.e05-05-0472;
RA Wang H., Spang A., Sullivan M.A., Hryhorenko J., Hagen F.K.;
RT "The terminal phase of cytokinesis in the Caenorhabditis elegans early
RT embryo requires protein glycosylation.";
RL Mol. Biol. Cell 16:4202-4213(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: May catalyze 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. {ECO:0000250}.
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=2;
CC Name=a;
CC IsoId=O45947-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O45947-2; Sequence=VSP_032724;
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; AL021492; CAA16378.1; -; Genomic_DNA.
DR EMBL; AL021492; CAJ76949.1; -; Genomic_DNA.
DR PIR; T26930; T26930.
DR RefSeq; NP_001041036.2; NM_001047571.3.
DR RefSeq; NP_001041037.1; NM_001047572.2. [O45947-2]
DR AlphaFoldDB; O45947; -.
DR SMR; O45947; -.
DR STRING; 6239.Y45F10D.3a; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; O45947; -.
DR EPD; O45947; -.
DR PaxDb; O45947; -.
DR PeptideAtlas; O45947; -.
DR PRIDE; O45947; -.
DR EnsemblMetazoa; Y45F10D.3a.1; Y45F10D.3a.1; WBGene00001635.
DR EnsemblMetazoa; Y45F10D.3b.1; Y45F10D.3b.1; WBGene00001635. [O45947-2]
DR GeneID; 178343; -.
DR KEGG; cel:CELE_Y45F10D.3; -.
DR UCSC; Y45F10D.3a; c. elegans. [O45947-1]
DR CTD; 178343; -.
DR WormBase; Y45F10D.3a; CE49749; WBGene00001635; gly-10.
DR WormBase; Y45F10D.3b; CE39841; WBGene00001635; gly-10. [O45947-2]
DR eggNOG; KOG3736; Eukaryota.
DR InParanoid; O45947; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; O45947; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:O45947; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001635; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O45947; 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; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 1: Evidence at protein 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..684
FT /note="Putative polypeptide N-
FT acetylgalactosaminyltransferase 10"
FT /id="PRO_0000059153"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..684
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 581..684
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 218..330
FT /note="Catalytic subdomain A"
FT REGION 386..448
FT /note="Catalytic subdomain B"
FT REGION 448..461
FT /note="Flexible loop"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 209..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 431..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 548..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 594..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 637..653
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_032724"
SQ SEQUENCE 684 AA; 78971 MW; 59B9B3F84C2B3445 CRC64;
MVAICIKIGE RERKRVHIML LAYTWKTRVS SHQCNKSPIF GLFAIQFSNI CSNLLLLQQK
LSMGLSRYLS RRHHWVIQYC GLLLFLYLIY SYVATSNDGP NLHEDIPVFQ GQGKDRANPN
PPAALGDEAL DPFEKYRGHE KIKWEDEAAY EKEKRREGPG EWGKPVKLPE DKEVEKEALS
LYKANGYNAY ISDMISLNRS IKDIRHKECK NMMYSAKLPT VSVIFPFHEE HNSTLLRSVY
SVINRSPPEL LKEIILVDDF SEKPALRQPL EDFLKKNKID HIVKVLRTKK REGLIRGRQL
GAQDATGEIL IFLDAHSEAN YNWLPPLLDP IAEDYRTVVC PFVDVIDCET YEVRPQDEGA
RGSFDWAFNY KRLPLTKKDR ESPTKPFNSP VMAGGYFAIS AKWFWELGGY DEGLDIWGGE
QYELSFKVWQ CHGRMVDAPC SRVAHIYRCK YAPFKNAGMG DFVSRNYKRV AEVWMDDYKE
TLYKHRPGVG NADAGDLKLM KGIREKLQCK SFDWFMKEIA FDQDKYYPAV EPKASAEGEI
RNVGTNFCID TQFKEQNQRF GLRKCTSDDK DGGGEQDLRL TRWHDIRPKG RKICFDCSTS
VDKAPVILFD CHSMKGNQLF KYRVAQKQIY HPISGQCLTA DENGKGFLHM KKCDSSSDLQ
KWAWQTVDNE LLETRQANEA KEQE
