GLT17_HUMAN
ID GLT17_HUMAN Reviewed; 598 AA.
AC Q6IS24; Q8NFV9; Q9NTA8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 17 {ECO:0000305};
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q9HCQ5};
DE AltName: Full=Polypeptide GalNAc transferase-like protein 3;
DE Short=GalNAc-T-like protein 3;
DE Short=pp-GaNTase-like protein 3;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 3;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 17 protein {ECO:0000303|PubMed:12073013, ECO:0000312|HGNC:HGNC:16347};
GN Name=GALNT17 {ECO:0000312|HGNC:HGNC:16347};
GN Synonyms=WBSCR17 {ECO:0000303|PubMed:12073013,
GN ECO:0000312|HGNC:HGNC:16347};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x;
RA Merla G., Ucla C., Guipponi M., Reymond A.;
RT "Identification of additional transcripts in the Williams-Beuren syndrome
RT critical region.";
RL Hum. Genet. 110:429-438(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-598.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(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.
CC {ECO:0000250|UniProtKB:Q9HCQ5}.
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:0000250|UniProtKB:Q9HCQ5};
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:0000250|UniProtKB:Q9HCQ5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9HCQ5};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9HCQ5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and heart. Weakly
CC expressed in kidney, liver, lung and spleen.
CC {ECO:0000269|PubMed:12073013}.
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 -!- DISEASE: Note=WBSCR17 is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC polypeptide N-acetylgalactosaminyltransferase-like protein 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_500";
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DR EMBL; AF410457; AAM62306.1; -; mRNA.
DR EMBL; BC067524; AAH67524.1; -; mRNA.
DR EMBL; BC067525; AAH67525.1; -; mRNA.
DR EMBL; BC069624; AAH69624.1; -; mRNA.
DR EMBL; BC069628; AAH69628.1; -; mRNA.
DR EMBL; BC069636; AAH69636.1; -; mRNA.
DR EMBL; BC069645; AAH69645.1; -; mRNA.
DR EMBL; BC069997; AAH69997.1; -; mRNA.
DR EMBL; AL137431; CAB70734.1; -; mRNA.
DR CCDS; CCDS5540.1; -.
DR PIR; T46260; T46260.
DR RefSeq; NP_071924.1; NM_022479.2.
DR AlphaFoldDB; Q6IS24; -.
DR SMR; Q6IS24; -.
DR BioGRID; 122161; 1.
DR STRING; 9606.ENSP00000329654; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q6IS24; 3 sites.
DR iPTMnet; Q6IS24; -.
DR PhosphoSitePlus; Q6IS24; -.
DR BioMuta; GALNT17; -.
DR DMDM; 51315852; -.
DR EPD; Q6IS24; -.
DR MassIVE; Q6IS24; -.
DR PaxDb; Q6IS24; -.
DR PeptideAtlas; Q6IS24; -.
DR PRIDE; Q6IS24; -.
DR ProteomicsDB; 66491; -.
DR Antibodypedia; 2698; 110 antibodies from 21 providers.
DR DNASU; 64409; -.
DR Ensembl; ENST00000333538.10; ENSP00000329654.5; ENSG00000185274.12.
DR GeneID; 64409; -.
DR KEGG; hsa:64409; -.
DR MANE-Select; ENST00000333538.10; ENSP00000329654.5; NM_022479.3; NP_071924.1.
DR UCSC; uc003tvy.5; human.
DR CTD; 64409; -.
DR DisGeNET; 64409; -.
DR GeneCards; GALNT17; -.
DR HGNC; HGNC:16347; GALNT17.
DR HPA; ENSG00000185274; Tissue enhanced (brain).
DR MIM; 615137; gene.
DR neXtProt; NX_Q6IS24; -.
DR OpenTargets; ENSG00000185274; -.
DR PharmGKB; PA38124; -.
DR VEuPathDB; HostDB:ENSG00000185274; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156014; -.
DR InParanoid; Q6IS24; -.
DR OMA; FMTFWAK; -.
DR OrthoDB; 273006at2759; -.
DR PhylomeDB; Q6IS24; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q6IS24; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 64409; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; GALNT17; human.
DR GeneWiki; WBSCR17; -.
DR GenomeRNAi; 64409; -.
DR Pharos; Q6IS24; Tbio.
DR PRO; PR:Q6IS24; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6IS24; protein.
DR Bgee; ENSG00000185274; Expressed in trigeminal ganglion and 139 other tissues.
DR ExpressionAtlas; Q6IS24; baseline and differential.
DR Genevisible; Q6IS24; HS.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix; Williams-Beuren syndrome.
FT CHAIN 1..598
FT /note="Polypeptide N-acetylgalactosaminyltransferase 17"
FT /id="PRO_0000059139"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..598
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 465..594
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 151..262
FT /note="Catalytic subdomain A"
FT REGION 319..381
FT /note="Catalytic subdomain B"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 364..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 478..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 526..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 568..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 596
FT /note="S -> P (in Ref. 2; AAH69997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 67751 MW; 9E2D52DBFBD907B1 CRC64;
MASLRRVKVL LVLNLIAVAG FVLFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ
DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPAEEEK AKGPHEKYGY
NSYLSEKISL DRSIPDYRPT KCKELKYSKD LPQISIIFIF VNEALSVILR SVHSAVNHTP
THLLKEIILV DDNSDEEELK VPLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKVATGQ
VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW
CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK
VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP
LENPGIDIGD VSERRALRKS LKCKNFQWYL DHVYPEMRRY NNTVAYGELR NNKAKDVCLD
QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD
CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WTIKNSIK
