BGAT_MOUSE
ID BGAT_MOUSE Reviewed; 332 AA.
AC P38649; A2AL98; Q8BZH3; Q8BZQ6; Q9EQW2; Q9EQW3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histo-blood group ABO system transferase;
DE AltName: Full=Cis-AB transferase;
DE AltName: Full=Fucosylglycoprotein 3-alpha-galactosyltransferase;
DE AltName: Full=Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase;
DE AltName: Full=Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase;
DE EC=2.4.1.40 {ECO:0000250|UniProtKB:P16442};
DE AltName: Full=Glycoprotein-fucosylgalactoside alpha-galactosyltransferase;
DE EC=2.4.1.37 {ECO:0000250|UniProtKB:P16442};
DE AltName: Full=Histo-blood group A transferase;
DE Short=A transferase;
DE AltName: Full=Histo-blood group B transferase;
DE Short=B transferase;
DE AltName: Full=NAGAT;
GN Name=Abo;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11278752; DOI=10.1074/jbc.m010805200;
RA Yamamoto M., Lin X.-H., Kominato Y., Hata Y., Noda R., Saitou N.,
RA Yamamoto F.;
RT "Murine equivalent of the human histo-blood group ABO gene is a cis-AB gene
RT and encodes a glycosyltransferase with both A and B transferase activity.";
RL J. Biol. Chem. 276:13701-13708(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis, and Urinary bladder;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=7523108; DOI=10.1002/elps.11501501101;
RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT "Separation and sequencing of familiar and novel murine proteins using
RT preparative two-dimensional gel electrophoresis.";
RL Electrophoresis 15:735-745(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-
CC N-acetyl-alpha-D-galactosamine = an N-acetyl-alpha-D-galactosaminyl-
CC (1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) +
CC UDP; Xref=Rhea:RHEA:19021, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:140327, ChEBI:CHEBI:140559;
CC EC=2.4.1.40; Evidence={ECO:0000250|UniProtKB:P16442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-
CC alpha-D-galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-
CC (1->2)]-beta-D-galactosyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:14349, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:140327, ChEBI:CHEBI:140328;
CC EC=2.4.1.37; Evidence={ECO:0000250|UniProtKB:P16442};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P16442};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P16442};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P16442}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Secreted. Note=Membrane-bound form in
CC trans cisternae of Golgi. Secreted into the body fluid (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Submaxillary glands (at protein level).
CC {ECO:0000269|PubMed:11278752}.
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM23695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB041038; BAB20559.1; -; Genomic_DNA.
DR EMBL; AB041039; BAB20560.1; -; mRNA.
DR EMBL; AK033786; BAC28473.1; -; mRNA.
DR EMBL; AK035261; BAC29005.1; -; mRNA.
DR EMBL; AL773563; CAM23695.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL773563; CAM23696.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08332.1; -; Genomic_DNA.
DR EMBL; BC116759; AAI16760.1; -; mRNA.
DR EMBL; BC116761; AAI16762.1; -; mRNA.
DR CCDS; CCDS15811.1; -.
DR RefSeq; NP_001277373.1; NM_001290444.1.
DR RefSeq; NP_109643.3; NM_030718.5.
DR AlphaFoldDB; P38649; -.
DR SMR; P38649; -.
DR STRING; 10090.ENSMUSP00000099964; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; P38649; 1 site.
DR iPTMnet; P38649; -.
DR PhosphoSitePlus; P38649; -.
DR PaxDb; P38649; -.
DR PRIDE; P38649; -.
DR ProteomicsDB; 273673; -.
DR Antibodypedia; 80247; 795 antibodies from 23 providers.
DR DNASU; 80908; -.
DR Ensembl; ENSMUST00000102900; ENSMUSP00000099964; ENSMUSG00000015787.
DR GeneID; 80908; -.
DR KEGG; mmu:80908; -.
DR UCSC; uc008iwb.2; mouse.
DR CTD; 28; -.
DR MGI; MGI:2135738; Abo.
DR VEuPathDB; HostDB:ENSMUSG00000015787; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_0_1_1; -.
DR InParanoid; P38649; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; P38649; -.
DR TreeFam; TF330991; -.
DR BRENDA; 2.4.1.37; 3474.
DR BRENDA; 2.4.1.40; 3474.
DR BRENDA; 2.4.1.88; 3474.
DR Reactome; R-MMU-9033807; ABO blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 80908; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Abo; mouse.
DR PRO; PR:P38649; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P38649; protein.
DR Bgee; ENSMUSG00000015787; Expressed in prostate gland ventral lobe and 22 other tissues.
DR ExpressionAtlas; P38649; baseline and differential.
DR Genevisible; P38649; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0001962; F:alpha-1,3-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; ISO:MGI.
DR GO; GO:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; IDA:MGI.
DR GO; GO:0004380; F:glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="Histo-blood group ABO system transferase"
FT /id="PRO_0000157293"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..332
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 100..102
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 105
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 190..192
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 212
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 224
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 282
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 305
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 77
FT /note="G -> R (in Ref. 2; BAC29005)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="L -> I (in Ref. 2; BAC29005)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="W -> C (in Ref. 2; BAC28473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38777 MW; C48DB1090EA0D3E4 CRC64;
MNLRGRPKCN FLHLGILPFA VFVLVFFGYL FLSFRSQNLG HPGAVTRNAY LQPRVLKPTR
KDVLVLTPWL APIIWEGTFN IDILNEQFRI RNTTIGLTVF AIKKYVVFLK LFLETAEQHF
MVGHKVIYYV FTDRPADVPQ VILGAGRQLV VLTVRNYTRW QDVSMHRMEM ISHFSERRFL
REVDYLVCAD ADMKFSDHVG VEILSTFFGT LHPGFYSSSR EAFTYERRPQ SQAYIPWDRG
DFYYGGAFFG GSVLEVYHLT KACHEAMMED KANGIEPVWH DESYLNKYLL YHKPTKVLSP
EYLWDQQLLG WPSIMKKLRY VAVPKDHQAI RN
