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   27-MAR-2024, entry version 142.
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   GlyCosmos; P38649; 1 site, No reported glycans.
DR   GlyGen; P38649; 1 site.
DR   iPTMnet; P38649; -.
DR   PhosphoSitePlus; P38649; -.
DR   PaxDb; 10090-ENSMUSP00000099964; -.
DR   ProteomicsDB; 273673; -.
DR   Antibodypedia; 80247; 847 antibodies from 24 providers.
DR   DNASU; 80908; -.
DR   Ensembl; ENSMUST00000102900.2; ENSMUSP00000099964.2; ENSMUSG00000015787.16.
DR   GeneID; 80908; -.
DR   KEGG; mmu:80908; -.
DR   UCSC; uc008iwb.2; mouse.
DR   AGR; MGI:2135738; -.
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   OMA; TGKPKCY; -.
DR   OrthoDB; 4223357at2759; -.
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; 1 hit in 78 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 23 other cell types or tissues.
DR   ExpressionAtlas; P38649; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:0030259; P:lipid glycosylation; IBA:GO_Central.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02515; Glyco_transf_6; 1.
DR   InterPro; IPR005076; Glyco_trans_6.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10462; GLYCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10462:SF29; HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE; 1.
DR   Pfam; PF03414; Glyco_transf_6; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; P38649; MM.
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
//