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   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 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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 syndrome
RT   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 project:
RT   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 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   -!- 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), 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}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC       polypeptide N-acetylgalactosaminyltransferase-like 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   SMR; Q7TT15; -.
DR   STRING; 10090.ENSMUSP00000083187; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyConnect; 2662; -.
DR   iPTMnet; Q7TT15; -.
DR   PhosphoSitePlus; Q7TT15; -.
DR   jPOST; Q7TT15; -.
DR   PaxDb; Q7TT15; -.
DR   PRIDE; Q7TT15; -.
DR   Antibodypedia; 2698; 100 antibodies.
DR   Ensembl; ENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040. [Q7TT15-1]
DR   GeneID; 212996; -.
DR   KEGG; mmu:212996; -.
DR   UCSC; uc008zuq.1; mouse. [Q7TT15-1]
DR   CTD; 64409; -.
DR   MGI; MGI:2137594; Galnt17.
DR   eggNOG; KOG3736; Eukaryota.
DR   eggNOG; ENOG410XPMK; LUCA.
DR   GeneTree; ENSGT00940000156014; -.
DR   HOGENOM; CLU_013477_4_0_1; -.
DR   InParanoid; Q7TT15; -.
DR   KO; K00710; -.
DR   OMA; AFVFRRW; -.
DR   PhylomeDB; Q7TT15; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; Galntl6; mouse.
DR   PRO; PR:Q7TT15; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q7TT15; protein.
DR   Bgee; ENSMUSG00000034040; Expressed in embryo and 93 other tissues.
DR   ExpressionAtlas; Q7TT15; 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; 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; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin; Manganese;
KW   Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..598
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 17"
FT                   /id="PRO_0000059140"
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   VAR_SEQ         194..196
FT                   /note="SDE -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12073013"
FT                   /id="VSP_011232"
FT   CONFLICT        74
FT                   /note="V -> D (in Ref. 3; BAC33446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="E -> D (in Ref. 3; BAC33446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="Q -> K (in Ref. 3; BAC33446)"
FT                   /evidence="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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