GenomeNet

Database: UniProt/SWISS-PROT
Entry: GLT17_MOUSE
LinkDB: GLT17_MOUSE
Original site: GLT17_MOUSE 
ID   GLT17_MOUSE             Reviewed;         598 AA.
AC   Q7TT15; Q8BKN7; Q8BUY1; Q8BX73; Q8BZC8; Q8K483;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   12-SEP-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 homolog {ECO:0000312|MGI:MGI:2137594};
GN   Name=Galnt17 {ECO:0000250|UniProtKB:Q6IS24};
GN   Synonyms=Wbscr17 {ECO:0000303|PubMed:12073013,
GN   ECO:0000312|MGI:MGI:2137594};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 1-455 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 128-143, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TT15-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TT15-2; Sequence=VSP_011232;
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   -!- 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/search/jsp/landing.jsp?query=gt_mou_528";
DR   EMBL; AF467979; AAM62404.1; -; mRNA.
DR   EMBL; AK035817; BAC29197.1; -; mRNA.
DR   EMBL; AK048758; BAC33446.2; -; mRNA.
DR   EMBL; AK051281; BAC34591.2; -; mRNA.
DR   EMBL; BC052469; AAH52469.1; -; mRNA.
DR   CCDS; CCDS39296.1; -. [Q7TT15-1]
DR   RefSeq; NP_660253.2; NM_145218.3. [Q7TT15-1]
DR   UniGene; Mm.299204; -.
DR   ProteinModelPortal; Q7TT15; -.
DR   SMR; Q7TT15; -.
DR   STRING; 10090.ENSMUSP00000083187; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   iPTMnet; Q7TT15; -.
DR   PhosphoSitePlus; Q7TT15; -.
DR   PaxDb; Q7TT15; -.
DR   PRIDE; Q7TT15; -.
DR   Ensembl; ENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040. [Q7TT15-1]
DR   GeneID; 212996; -.
DR   KEGG; mmu:212996; -.
DR   UCSC; uc008zuq.1; mouse. [Q7TT15-1]
DR   CTD; 212996; -.
DR   MGI; MGI:2137594; Galnt17.
DR   eggNOG; KOG3736; Eukaryota.
DR   eggNOG; ENOG410XPMK; LUCA.
DR   GeneTree; ENSGT00900000140827; -.
DR   HOGENOM; HOG000038228; -.
DR   HOVERGEN; HBG051699; -.
DR   InParanoid; Q7TT15; -.
DR   KO; K00710; -.
DR   OMA; NWELWCM; -.
DR   OrthoDB; EOG091G03F2; -.
DR   PhylomeDB; Q7TT15; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; Wbscr17; mouse.
DR   PRO; PR:Q7TT15; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000034040; Expressed in 94 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q7TT15; baseline and differential.
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   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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Lectin; Manganese; Membrane; Metal-binding; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    598       Polypeptide N-
FT                                acetylgalactosaminyltransferase 17.
FT                                /FTId=PRO_0000059140.
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   VAR_SEQ     194    196       SDE -> R (in isoform 2).
FT                                {ECO:0000303|PubMed:12073013}.
FT                                /FTId=VSP_011232.
FT   CONFLICT     74     74       V -> D (in Ref. 3; BAC33446).
FT                                {ECO:0000305}.
FT   CONFLICT    224    224       E -> D (in Ref. 3; BAC33446).
FT                                {ECO:0000305}.
FT   CONFLICT    264    264       Q -> K (in Ref. 3; BAC33446).
FT                                {ECO:0000305}.
SQ   SEQUENCE   598 AA;  67691 MW;  66F91B355EF571F5 CRC64;
     MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ
     DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPSEEEK AKGPHEKYGY
     NSYLSEKISL DRSIPDYRPT KCKELKYSKE LPQISIIFIF VNEALSVILR SVHSAVNHTP
     THLLKEIILV DDNSDEEELK APLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKAATGQ
     VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW
     CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK
     VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP
     LENPGIDIGD VSERKALRKS LKCKNFQWYL DHVYPEMRRY NNTIAYGELR NNKAKDVCLD
     QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD
     CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WAIKNPIK
//
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