BGAT2_RAT
ID BGAT2_RAT Reviewed; 334 AA.
AC Q8CFC4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histo-blood group ABO system transferase 2;
DE AltName: Full=B blood group galactosyltransferase;
DE AltName: Full=Blood group A glycosyltransferase 2;
DE AltName: Full=Cis-AB transferase 2;
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 2;
DE AltName: Full=Putative blood group A transferase T2;
GN Name=Abo2;
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], 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12799344; DOI=10.1093/glycob/cwg087;
RA Turcot A.-L., Blancher A., Le Moullac-Vaidye B., Despiau S., Rocher J.,
RA Roubinet F., Szpirer C., Le Pendu J.;
RT "Cloning of a rat gene encoding the histo-blood group B enzyme: rats have
RT more than one Abo gene.";
RL Glycobiology 13:919-928(2003).
RN [3]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Posseses strong B transferase activity and a weak A
CC transferase activity. {ECO:0000269|PubMed:12799344}.
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: Large intestine, caecum, stomach, pancreas,
CC submaxillary gland and kidney (at protein level). Ubiquitous.
CC {ECO:0000269|PubMed:12180981, ECO:0000269|PubMed:12237302,
CC ECO:0000269|PubMed:12799344}.
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; AY228143; AAO72725.1; -; mRNA.
DR EMBL; AB081652; BAC16248.1; -; mRNA.
DR RefSeq; NP_001153735.1; NM_001160263.1.
DR AlphaFoldDB; Q8CFC4; -.
DR SMR; Q8CFC4; -.
DR STRING; 10116.ENSRNOP00000039997; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; Q8CFC4; 1 site.
DR PaxDb; Q8CFC4; -.
DR PRIDE; Q8CFC4; -.
DR Ensembl; ENSRNOT00000044775; ENSRNOP00000039997; ENSRNOG00000046958.
DR GeneID; 100301568; -.
DR KEGG; rno:100301568; -.
DR UCSC; RGD:2307241; rat.
DR CTD; 28; -.
DR RGD; 2307241; Abo2.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_0_1_1; -.
DR InParanoid; Q8CFC4; -.
DR OMA; MADHANG; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; Q8CFC4; -.
DR TreeFam; TF330991; -.
DR BRENDA; 2.4.1.37; 5301.
DR Reactome; R-RNO-9033807; ABO blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8CFC4; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000046958; Expressed in stomach and 19 other tissues.
DR Genevisible; Q8CFC4; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0003823; F:antigen binding; ISO:RGD.
DR GO; GO:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0004380; F:glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity; IDA:RGD.
DR GO; GO:0030145; F:manganese ion binding; ISO:RGD.
DR GO; GO:0000166; F:nucleotide binding; ISO:RGD.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:RGD.
DR GO; GO:0051691; P:cellular oligosaccharide metabolic process; IMP:RGD.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009624; P:response to nematode; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
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..334
FT /note="Histo-blood group ABO system transferase 2"
FT /id="PRO_0000356180"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 102..104
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 107
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 192..194
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:P16442"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 214
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 226
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 284
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 307
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 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 39079 MW; 4EFF83B51393C506 CRC64;
MKDLRFGRLK CYSLHLGILP LTVLVLVFFC FVCLSLRSQE WGHPGAVNRK AYPQPRVLTP
TRTDVLVLTP WLAPIIWEGT FDIDTLNEQF RLRNTTIGLT VFAVKKYVVF LKLFLETAEQ
HFMVGHKVIY YVFTDRPADV PQVPLGAGRR LVVLTVRNYT RWQDVSMHRM EVISHFSEQR
FRHEVDYLVC ADVDMKFRDH VGVEILSALF GTLHPGFYRS RRESFTYERR PQSQAYIPWD
QGDFYYMGAF FGGSVVEVHH LTKACHQAMV EDQANGIEAV WHDESHLNKY LLYHKPTKVL
SPEYMWDQQL LGWPSIMKKL RYVAVPKNHQ AIRN
