BGAT1_RAT
ID BGAT1_RAT Reviewed; 348 AA.
AC Q9ET32; Q8CFC5; Q8CFC6; Q8R005; Q8R4Y3; Q8R552;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Histo-blood group ABO system transferase 1;
DE AltName: Full=Blood group A glycosyltransferase 1;
DE AltName: Full=Cis-AB transferase 1;
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=N-acetylgalactosaminyltransferase A blood group-like enzyme;
DE AltName: Full=NAGAT 1;
GN Name=Abo; Synonyms=Abo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BDIX; TISSUE=Stomach;
RX PubMed=12180981; DOI=10.1046/j.1432-1033.2002.03094.x;
RA Cailleau-Thomas A., Le Moullac-Vaidye B., Rocher J., Bouhours D.,
RA Szpirer C., Le Pendu J.;
RT "Cloning of a rat gene encoding the histo-blood group A enzyme. Tissue
RT expression of the gene and of the A and B antigens.";
RL Eur. J. Biochem. 269:4040-4047(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES A1 AND A2), AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11842091; DOI=10.1074/jbc.m112287200;
RA Olson F.J., Johansson M.E., Klinga-Levan K., Bouhours D., Enerbaeck L.,
RA Hansson G.C., Karlsson N.G.;
RT "Blood group A glycosyltransferase occurring as alleles with high sequence
RT difference is transiently induced during a Nippostrongylus brasiliensis
RT parasite infection.";
RL J. Biol. Chem. 277:15044-15052(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A2; A3 AND A4), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=12237302; DOI=10.1074/jbc.m206439200;
RA Iwamoto S., Kumada M., Kamesaki T., Okuda H., Kajii E., Inagaki T.,
RA Saikawa D., Takeuchi K., Ohgawara S., Takahashi R., Ueda S., Inoue S.,
RA Tahara K., Hakamata Y., Kobayashi E.;
RT "Rat encodes the paralogous gene equivalent of the human histo-blood group
RT ABO gene. Association with antigen expression by overexpression of human
RT ABO transferase.";
RL J. Biol. Chem. 277:46463-46469(2002).
CC -!- FUNCTION: Posseses strong A transferase activity and a weak B
CC transferase activity. {ECO:0000269|PubMed:12180981}.
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: Tongue, esophagus, large intestine, stomach,
CC caecum, pancreas, uterus, seminal vesicle, submaxillary gland, parotid
CC gland, thyroid gland, parathyroid gland, salivary gland and thymus (at
CC protein level). Esophagus, large intestine, stomach, kidney, urinary
CC bladder, uterus and thymus. {ECO:0000269|PubMed:12180981,
CC ECO:0000269|PubMed:12237302}.
CC -!- INDUCTION: During a Nippostrongylus brasiliensis parasite infection.
CC The expression is a transient event, with a maximum at day 6 of the 13-
CC day-long infection. {ECO:0000269|PubMed:11842091}.
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}.
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DR EMBL; AF264018; AAF74758.2; -; mRNA.
DR EMBL; AF296761; AAL98710.1; -; Genomic_DNA.
DR EMBL; AF296762; AAL98711.1; -; mRNA.
DR EMBL; AF469945; AAL82445.1; -; mRNA.
DR EMBL; AF469946; AAL82446.1; -; mRNA.
DR EMBL; AH011509; AAL82447.1; -; Genomic_DNA.
DR EMBL; AB081649; BAC16245.1; -; mRNA.
DR EMBL; AB081650; BAC16246.1; -; mRNA.
DR EMBL; AB081651; BAC16247.1; -; mRNA.
DR RefSeq; NP_075582.3; NM_023094.3.
DR AlphaFoldDB; Q9ET32; -.
DR SMR; Q9ET32; -.
DR STRING; 10116.ENSRNOP00000006553; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; Q9ET32; 1 site.
DR PaxDb; Q9ET32; -.
DR Ensembl; ENSRNOT00000006553; ENSRNOP00000006553; ENSRNOG00000039906.
DR Ensembl; ENSRNOT00000074271; ENSRNOP00000065701; ENSRNOG00000039906.
DR GeneID; 65270; -.
DR KEGG; rno:65270; -.
DR UCSC; RGD:628609; rat.
DR CTD; 65270; -.
DR RGD; 628609; Abo.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_0_1_1; -.
DR InParanoid; Q9ET32; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; Q9ET32; -.
DR TreeFam; TF330991; -.
DR BRENDA; 2.4.1.40; 5301.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9ET32; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Genevisible; Q9ET32; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004380; F:glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEP:RGD.
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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..348
FT /note="Histo-blood group ABO system transferase 1"
FT /id="PRO_0000356179"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..348
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 116..118
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 121
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 206..208
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228
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 240
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 298
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 321
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 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 22
FT /note="L -> I (in allele A4)"
FT VARIANT 24
FT /note="L -> S (in allele A3)"
FT VARIANT 35
FT /note="K -> R (in allele A2 and allele A3)"
FT VARIANT 36
FT /note="I -> F (in allele A2 and allele A4)"
FT VARIANT 37
FT /note="Q -> H (in allele A2)"
FT VARIANT 43..44
FT /note="GG -> AV (in allele A2)"
FT VARIANT 46
FT /note="T -> S (in allele A4)"
FT VARIANT 53
FT /note="T -> M (in allele A2, allele A3 and allele A4)"
FT VARIANT 56..57
FT /note="QK -> HE (in allele A2, allele A3 and allele A4)"
FT VARIANT 65
FT /note="A -> T (in allele A3 and allele A4)"
FT VARIANT 70
FT /note="N -> K (in allele A3 and allele A4)"
FT VARIANT 71..73
FT /note="VLT -> MLK (in allele A4)"
FT VARIANT 75
FT /note="I -> T (in allele A2 and allele A3)"
FT VARIANT 106
FT /note="L -> T (in allele A4)"
FT VARIANT 107
FT /note="Q -> R (in allele A2 and allele A4)"
FT VARIANT 146
FT /note="V -> I (in allele A3)"
FT VARIANT 152
FT /note="S -> A (in allele A2, allele A3 and allele A4)"
FT VARIANT 164
FT /note="K -> R (in allele A2, allele A3 and allele A4)"
FT VARIANT 197
FT /note="H -> Y (in allele A2)"
FT VARIANT 205
FT /note="G -> A (in allele A4)"
FT VARIANT 222
FT /note="A -> S (in allele A4)"
FT VARIANT 233
FT /note="R -> S (in allele A4)"
FT VARIANT 235
FT /note="R -> Q (in allele A4)"
FT VARIANT 245
FT /note="P -> S (in allele A4)"
FT VARIANT 253
FT /note="R -> G (in allele A4)"
FT VARIANT 270
FT /note="V -> L (in allele A2, allele A3 and allele A4)"
FT VARIANT 281
FT /note="Q -> K (in allele A2, allele A3 and allele A4)"
FT VARIANT 284
FT /note="V -> L (in allele A4)"
FT VARIANT 287
FT /note="Q -> K (in allele A2 and allele A3)"
FT VARIANT 300
FT /note="H -> Y (in allele A2 and allele A3)"
SQ SEQUENCE 348 AA; 40375 MW; FC5E572B100ED7B3 CRC64;
MDLRGRPKCY SLHLGILPFI VLVLVFFGYG FLSHKIQEFR NPGGETCMAT RQTDVQKVVS
VPRMAYPQPN VLTPIRNDVL VFTPWLAPII WEGTFNIDIL NEQFKLQNTT IGLTVFAIKK
YVVFLKLFLE TAEQHFMVGH KVIYYVFTDR PSDVPQVPLG AGRKLVVLTV RNYTRWQDVS
MHRMEMISHF SEQRFQHEVD YLVCGDVDMK FSDHVGVEIL SALFGTLHPG FYRSRRESFT
YERRPKSQAY IPRDEGDFYY AGGFFGGSVV EVHHLTKACH QAMVEDQANG IEAVWHDESH
LNKYLLYHKP TKVLSPEYVW DQKLLGWPSI MKKLRYVAVP KNHQAIRN
