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   07-NOV-2018, entry version 127.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   syndrome 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
RT   project: 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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
CC       oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
CC       galactosamine residue to a serine or threonine residue on the
CC       protein receptor. {ECO:0000250|UniProtKB:Q9HCQ5}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
CC       polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
CC       {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};
CC       Single-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),
CC       which is probably involved in manganese coordination and substrate
CC       binding and the C-terminal domain (domain B, also called
CC       Gal/GalNAc-T motif), which is probably involved in catalytic
CC       reaction and UDP-Gal binding. {ECO:0000250}.
CC   -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
CC       contributes to the glycopeptide specificity. {ECO:0000250}.
CC   -!- DISEASE: Note=WBSCR17 is located in the Williams-Beuren syndrome
CC       (WBS) critical region. WBS results from a hemizygous deletion of
CC       several genes on chromosome 7q11.23, thought to arise as a
CC       consequence of unequal crossing over between highly homologous
CC       low-copy repeat 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;
CC       Note=Putative polypeptide N-acetylgalactosaminyltransferase-like
CC       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   UniGene; Hs.488591; -.
DR   ProteinModelPortal; Q6IS24; -.
DR   SMR; Q6IS24; -.
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   DMDM; 51315852; -.
DR   EPD; Q6IS24; -.
DR   PaxDb; Q6IS24; -.
DR   PeptideAtlas; Q6IS24; -.
DR   PRIDE; Q6IS24; -.
DR   ProteomicsDB; 66491; -.
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   EuPathDB; HostDB:ENSG00000185274.11; -.
DR   GeneCards; GALNT17; -.
DR   HGNC; HGNC:16347; GALNT17.
DR   HPA; HPA013624; -.
DR   HPA; HPA047986; -.
DR   MIM; 615137; gene.
DR   neXtProt; NX_Q6IS24; -.
DR   OpenTargets; ENSG00000185274; -.
DR   PharmGKB; PA38124; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   eggNOG; ENOG410XPMK; LUCA.
DR   GeneTree; ENSGT00900000140827; -.
DR   HOGENOM; HOG000038228; -.
DR   HOVERGEN; HBG051699; -.
DR   InParanoid; Q6IS24; -.
DR   KO; K00710; -.
DR   OMA; KGPLEEY; -.
DR   OrthoDB; EOG091G03F2; -.
DR   PhylomeDB; Q6IS24; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; GALNTL6; human.
DR   GeneWiki; WBSCR17; -.
DR   GenomeRNAi; 64409; -.
DR   PRO; PR:Q6IS24; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000185274; Expressed in 158 organ(s), highest expression level in cerebellum.
DR   CleanEx; HS_WBSCR17; -.
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   Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix; Williams-Beuren syndrome.
FT   CHAIN         1    598       Polypeptide N-
FT                                acetylgalactosaminyltransferase 17.
FT                                /FTId=PRO_0000059139.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     27       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     28    598       Lumenal. {ECO:0000255}.
FT   DOMAIN      465    594       Ricin B-type lectin.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   REGION      151    262       Catalytic subdomain A.
FT   REGION      319    381       Catalytic subdomain B.
FT   METAL       246    246       Manganese. {ECO:0000250}.
FT   METAL       248    248       Manganese. {ECO:0000250}.
FT   METAL       378    378       Manganese. {ECO:0000250}.
FT   BINDING     192    192       Substrate. {ECO:0000250}.
FT   BINDING     223    223       Substrate. {ECO:0000250}.
FT   BINDING     381    381       Substrate. {ECO:0000250}.
FT   BINDING     386    386       Substrate. {ECO:0000250}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    142    373       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    364    443       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    478    494       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    526    541       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    568    586       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   CONFLICT    596    596       S -> P (in Ref. 2; AAH69997).
FT                                {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
//
DBGET integrated database retrieval system