GALT6_MOUSE
ID GALT6_MOUSE Reviewed; 622 AA.
AC Q8C7U7; Q0VE84; Q3TWF0; Q8CED2; Q9QZ16;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 6;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 6;
DE Short=GalNAc-T6;
DE Short=pp-GaNTase 6;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
GN Name=Galnt6;
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].
RC TISSUE=Gastric carcinoma;
RX PubMed=10464263; DOI=10.1074/jbc.274.36.25362;
RA Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N.,
RA Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.;
RT "Cloning and characterization of a close homologue of human UDP-N-acetyl--
RT D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3,
RT designated GalNAc-T6. Evidence for genetic but not functional redundancy.";
RL J. Biol. Chem. 274:25362-25370(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
CC -!- FUNCTION: Catalyzes 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. May participate in
CC synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2,
CC EA2 and fibronectin peptides (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAB55352.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 6;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_515";
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DR EMBL; AJ133523; CAB55352.1; ALT_FRAME; mRNA.
DR EMBL; AK028506; BAC25984.1; -; mRNA.
DR EMBL; AK049222; BAC33618.1; -; mRNA.
DR EMBL; AK155008; BAE32989.1; -; mRNA.
DR EMBL; AK159721; BAE35316.1; -; mRNA.
DR EMBL; BC119324; AAI19325.1; -; mRNA.
DR EMBL; BC119326; AAI19327.1; -; mRNA.
DR CCDS; CCDS27843.1; -.
DR RefSeq; NP_001155239.1; NM_001161767.1.
DR RefSeq; NP_001155240.1; NM_001161768.1.
DR RefSeq; NP_766039.2; NM_172451.3.
DR AlphaFoldDB; Q8C7U7; -.
DR SMR; Q8C7U7; -.
DR STRING; 10090.ENSMUSP00000056705; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8C7U7; 2 sites.
DR PhosphoSitePlus; Q8C7U7; -.
DR EPD; Q8C7U7; -.
DR MaxQB; Q8C7U7; -.
DR PaxDb; Q8C7U7; -.
DR PeptideAtlas; Q8C7U7; -.
DR PRIDE; Q8C7U7; -.
DR ProteomicsDB; 267554; -.
DR Antibodypedia; 14380; 201 antibodies from 22 providers.
DR DNASU; 207839; -.
DR Ensembl; ENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
DR Ensembl; ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
DR Ensembl; ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
DR GeneID; 207839; -.
DR KEGG; mmu:207839; -.
DR UCSC; uc007xrz.2; mouse.
DR CTD; 11226; -.
DR MGI; MGI:1891640; Galnt6.
DR VEuPathDB; HostDB:ENSMUSG00000037280; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160845; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; Q8C7U7; -.
DR OMA; QRELRHN; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8C7U7; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 207839; 7 hits in 75 CRISPR screens.
DR PRO; PR:Q8C7U7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C7U7; protein.
DR Bgee; ENSMUSG00000037280; Expressed in molar tooth and 112 other tissues.
DR Genevisible; Q8C7U7; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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; IDA:MGI.
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.
FT CHAIN 1..622
FT /note="Polypeptide N-acetylgalactosaminyltransferase 6"
FT /id="PRO_0000059115"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..622
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 496..622
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 176..285
FT /note="Catalytic subdomain A"
FT REGION 348..410
FT /note="Catalytic subdomain B"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 393..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 509..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 597..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 14
FT /note="A -> T (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="K -> R (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="K -> N (in Ref. 2; BAC25984)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="V -> M (in Ref. 2; BAC25984)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="K -> G (in Ref. 2; BAC25984)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..275
FT /note="EVLTFLDAHCECF -> KGAHVSWTPTVSVS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> P (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> Q (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> G (in Ref. 2; BAC25984)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="R -> Q (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="G -> S (in Ref. 1; CAB55352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 71537 MW; 6DBCA3A2CCFDBDAA CRC64;
MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK DQVLDFMLGA
VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK PFWDRPPQDP NSPGADGKAF
QKKEWTNLET KEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLPTTS
VIIVFHNEAW STLLRTVYSV LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV
VRQRERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT
IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK SPTFAGGLFS
ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
TSVIARNQVR LAEVWMDDYK KIFYRRNLQA AKMVQENNFG DISERLRLRE QLRCHNFSWY
LHNVYPEMFV PDLNPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS
QRDLRHNIGK QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS
QDKKPAMAPC NPRDPYQLWL FV
