GenomeNet

Database: UniProt/SWISS-PROT
Entry: GLT17_HUMAN
LinkDB: GLT17_HUMAN
Original site: 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   22-APR-2020, entry version 136.
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";
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   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   iPTMnet; Q6IS24; -.
DR   PhosphoSitePlus; Q6IS24; -.
DR   BioMuta; GALNT17; -.
DR   DMDM; 51315852; -.
DR   EPD; Q6IS24; -.
DR   jPOST; Q6IS24; -.
DR   MassIVE; Q6IS24; -.
DR   PaxDb; Q6IS24; -.
DR   PeptideAtlas; Q6IS24; -.
DR   PRIDE; Q6IS24; -.
DR   ProteomicsDB; 66491; -.
DR   Antibodypedia; 2698; 100 antibodies.
DR   DNASU; 64409; -.
DR   Ensembl; ENST00000333538; ENSP00000329654; ENSG00000185274.
DR   GeneID; 64409; -.
DR   KEGG; hsa:64409; -.
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   eggNOG; KOG3736; Eukaryota.
DR   eggNOG; ENOG410XPMK; LUCA.
DR   GeneTree; ENSGT00940000156014; -.
DR   InParanoid; Q6IS24; -.
DR   KO; K00710; -.
DR   OMA; AFVFRRW; -.
DR   OrthoDB; 273006at2759; -.
DR   PhylomeDB; Q6IS24; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
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 cerebellum and 157 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; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 3.90.550.10; -; 1.
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   METAL           246
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           248
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           378
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /note="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
//
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