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   24-JAN-2024, entry version 121.
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   GlyCosmos; Q8CFC4; 1 site, No reported glycans.
DR   GlyGen; Q8CFC4; 1 site.
DR   PhosphoSitePlus; Q8CFC4; -.
DR   PaxDb; 10116-ENSRNOP00000039997; -.
DR   Ensembl; ENSRNOT00000044775.5; ENSRNOP00000039997.3; ENSRNOG00000046958.3.
DR   GeneID; 100301568; -.
DR   KEGG; rno:100301568; -.
DR   UCSC; RGD:2307241; rat.
DR   AGR; RGD:2307241; -.
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   OrthoDB; 4223357at2759; -.
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 cell types or tissues.
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: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:0030259; P:lipid glycosylation; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO: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   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; Q8CFC4; RN.
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
//