BGAT_HUMAN
ID BGAT_HUMAN Reviewed; 354 AA.
AC P16442; B0JDB9; O14758; Q14490; Q53I57; Q6ISD4; Q6KFZ2; Q70V27; Q99484;
AC Q99485; Q9NY01; Q9UQ68; Q9UQ69;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Histo-blood group ABO system 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:0000269|PubMed:12198488, ECO:0000269|PubMed:17259183};
DE AltName: Full=Glycoprotein-fucosylgalactoside alpha-galactosyltransferase;
DE EC=2.4.1.37 {ECO:0000269|PubMed:12198488, ECO:0000269|PubMed:17259183};
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;
DE Contains:
DE RecName: Full=Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form;
GN Name=ABO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2104828; DOI=10.1016/s0021-9258(19)40170-1;
RA Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.;
RT "Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc
RT alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-blood group A
RT transferase) mRNA.";
RL J. Biol. Chem. 265:1146-1151(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2333095; DOI=10.1038/345229a0;
RA Yamamoto F., Clausen H., White T., Marken J., Hakomori S.;
RT "Molecular genetic basis of the histo-blood group ABO system.";
RL Nature 345:229-233(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANT LEU-156.
RX PubMed=7598760; DOI=10.1006/bbrc.1995.1044;
RA Bennett E.P., Steffensen R., Clausen H., Weghuis D.O.,
RA Geurts van Kessel A.;
RT "Genomic cloning of the human histo-blood group ABO locus.";
RL Biochem. Biophys. Res. Commun. 206:318-325(1995).
RN [4]
RP ERRATUM OF PUBMED:7598760.
RX PubMed=7779106; DOI=10.1006/bbrc.1995.1817;
RA Bennett E.P., Steffensen R., Clausen H., Weghuis D.O.,
RA Geurts van Kessel A.;
RL Biochem. Biophys. Res. Commun. 211:347-347(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], POLYMORPHISM, AND VARIANTS
RP LEU-156; GLY-176; SER-235 AND MET-266.
RA Yamamoto F.;
RT "Human histo-blood group ABO gene locus alleles.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood;
RX PubMed=16533287; DOI=10.1111/j.1537-2995.2006.00740.x;
RA Seltsam A., Das Gupta C., Bade-Doeding C., Blasczyk R.;
RT "A weak blood group A phenotype caused by a translation-initiator mutation
RT in the ABO gene.";
RL Transfusion 46:434-440(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood;
RX PubMed=17764507; DOI=10.1111/j.1537-2995.2007.01475.x;
RA Seltsam A., Wagner F.F., Gruger D., Gupta C.D., Bade-Doeding C.,
RA Blasczyk R.;
RT "Weak blood group B phenotypes may be caused by variations in the CCAAT-
RT binding factor/NF-Y enhancer region of the ABO gene.";
RL Transfusion 47:2330-2335(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS ARG-230;
RP SER-235; MET-266 AND ALA-268.
RC TISSUE=Peripheral blood;
RX PubMed=18513251; DOI=10.1111/j.1537-2995.2008.01782.x;
RA Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D., Deluca D.S.,
RA Blasczyk R.;
RT "Aberrant intracellular trafficking of a variant B glycosyltransferase.";
RL Transfusion 48:1898-1905(2008).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS ARG-35;
RP PHE-36; HIS-63; SER-74; LEU-156; HIS-161; GLY-176; CYS-199; ILE-216;
RP SER-235; MET-266; ALA-268 AND MET-277.
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], POLYMORPHISM, AND VARIANTS GLY-176;
RP SER-235; MET-266 AND ALA-268.
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, AND VARIANTS
RP SER-74; LEU-156; MET-163; GLY-176; TRP-198; SER-235; MET-266; ALA-268;
RP ARG-268; ARG-288 AND MET-346.
RX PubMed=12829588; DOI=10.1182/blood-2003-03-0955;
RA Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.;
RT "The nature of diversity and diversification at the ABO locus.";
RL Blood 102:3035-3042(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, POLYMORPHISM, AND VARIANTS
RP LEU-156; GLY-176; ARG-214; ILE-216; ASP-223; SER-235; MET-266; ALA-268;
RP MET-277; ASN-291; GLY-352 AND TRP-352.
RX PubMed=8839869;
RA Ogasawara K., Yabe R., Uchikawa M., Saitou N., Bannai M., Nakata K.,
RA Takenaka M., Fujisawa K., Ishikawa Y., Juji T., Tokunaga K.;
RT "Molecular genetic analysis of variant phenotypes of the ABO blood group
RT system.";
RL Blood 88:2732-2737(1996).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354.
RX PubMed=9800297; DOI=10.1046/j.1365-3148.1998.00161.x;
RA Olsson M.L., Chester M.A.;
RT "Heterogeneity of the blood group Ax allele: genetic recombination of
RT common alleles can result in the Ax phenotype.";
RL Transfus. Med. 8:231-238(1998).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, AND VARIANTS
RP GLY-176; SER-235; MET-266 AND ALA-268.
RX PubMed=15104652; DOI=10.1111/j.1537-2995.2004.03346.x;
RA Roubinet F., Despiau S., Calafell F., Jin F., Bertanpetit J., Saitou N.,
RA Blancher A.;
RT "Evolution of the O alleles of the human ABO blood group gene.";
RL Transfusion 44:707-715(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, POLYMORPHISM, AND VARIANTS
RP GLY-176; SER-235 AND MET-346.
RA Seltsam A., Hallensleben M., Salama A., Blasczyk R.;
RT "A novel B Transferase.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, POLYMORPHISM, AND VARIANTS
RP MET-266 AND ALA-268.
RX PubMed=1449469; DOI=10.1016/0006-291x(92)91538-2;
RA Kominato Y., McNeill P.D., Yamamoto M., Russell M., Hakomori S.,
RA Yamamoto F.;
RT "Animal histo-blood group ABO genes.";
RL Biochem. Biophys. Res. Commun. 189:154-164(1992).
RN [17]
RP CHARACTERIZATION, AND POLYMORPHISM.
RX PubMed=2121736; DOI=10.1016/s0021-9258(17)30652-x;
RA Yamamoto F., Hakomori S.;
RT "Sugar-nucleotide donor specificity of histo-blood group A and B
RT transferases is based on amino acid substitutions.";
RL J. Biol. Chem. 265:19257-19262(1990).
RN [18]
RP POLYMORPHISM, AND VARIANT ALA-234.
RX PubMed=10462501; DOI=10.1006/bbrc.1999.1246;
RA Yu L.C., Lee H.L., Chan Y.S., Lin M.;
RT "The molecular basis for the B(A) allele: an amino acid alteration in the
RT human histoblood group B alpha-(1,3)-galactosyltransferase increases its
RT intrinsic alpha-(1,3)-N-acetylgalactosaminyltransferase activity.";
RL Biochem. Biophys. Res. Commun. 262:487-493(1999).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 64-354 IN COMPLEX WITH MANGANESE
RP AND UDP-N-ACETYL-D-GALACTOSAMINE, METAL-BINDING, MUTAGENESIS OF GLU-303,
RP AND CATALYTIC ACTIVITY.
RX PubMed=12198488; DOI=10.1038/nsb832;
RA Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L.,
RA Palcic M.M., Evans S.V.;
RT "The structural basis for specificity in human ABO(H) blood group
RT biosynthesis.";
RL Nat. Struct. Biol. 9:685-690(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 OF MUTANT SER-234 IN
RP COMPLEX WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG.
RX PubMed=12529355; DOI=10.1074/jbc.m212002200;
RA Marcus S.L., Polakowski R., Seto N.O.L., Leinala E., Borisova S.,
RA Blancher A., Roubinet F., Evans S.V., Palcic M.M.;
RT "A single point mutation reverses the donor specificity of human blood
RT group B-synthesizing galactosyltransferase.";
RL J. Biol. Chem. 278:12403-12405(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 IN COMPLEXES WITH
RP MANGANESE; UDP; UDP-N-ACETYL-GALACTOSAMINE; UDP-GALACTOSE AND GLYCOPROTEIN
RP FUCOSYL-GALACTOSE ANALOGS.
RX PubMed=12972418; DOI=10.1074/jbc.m308770200;
RA Nguyen H.P., Seto N.O.L., Cai Y., Leinala E.K., Borisova S.N., Palcic M.M.,
RA Evans S.V.;
RT "The influence of an intramolecular hydrogen bond in differential
RT recognition of inhibitory acceptor analogs by human ABO(H) blood group A
RT and B glycosyltransferases.";
RL J. Biol. Chem. 278:49191-49195(2003).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF MUTANTS SER-74 AND
RP ARG-268 IN COMPLEXES WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG AND
RP UDP-N-ACETYL-GALACTOSAMINE.
RX PubMed=15475562; DOI=10.1074/jbc.m500897200;
RA Lee H.J., Barry C.H., Borisova S.N., Seto N.O.L., Zheng R.B., Blancher A.,
RA Evans S.V., Palcic M.M.;
RT "Structural basis for the inactivity of human blood group O2
RT glycosyltransferase.";
RL J. Biol. Chem. 280:525-529(2005).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF HISTO-BLOOD GROUP A
RP TRANSFERASE AND HISTO-BLOOD GROUP B TRANSFERASE IN COMPLEX WITH MANGANESE
RP AND GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
RX PubMed=16326711; DOI=10.1074/jbc.m507620200;
RA Letts J.A., Rose N.L., Fang Y.R., Barry C.H., Borisova S.N., Seto N.O.L.,
RA Palcic M.M., Evans S.V.;
RT "Differential recognition of the type I and II H antigen acceptors by the
RT human ABO(H) blood group A and B glycosyltransferases.";
RL J. Biol. Chem. 281:3625-3632(2006).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND
RP THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF
RP MET-214, AND CATALYTIC ACTIVITY.
RX PubMed=17259183; DOI=10.1074/jbc.m610998200;
RA Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M.,
RA Evans S.V., Olsson M.L.;
RT "Structural effects of naturally occurring human blood group B
RT galactosyltransferase mutations adjacent to the DXD motif.";
RL J. Biol. Chem. 282:9564-9570(2007).
CC -!- FUNCTION: This protein is the basis of the ABO blood group system. The
CC histo-blood group ABO involves three carbohydrate antigens: A, B, and
CC H. A, B, and AB individuals express a glycosyltransferase activity that
CC converts the H antigen to the A antigen (by addition of UDP-GalNAc) or
CC to the B antigen (by addition of UDP-Gal), whereas O individuals lack
CC such activity.
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:0000269|PubMed:12198488,
CC ECO:0000269|PubMed:17259183};
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:0000269|PubMed:12198488,
CC ECO:0000269|PubMed:17259183};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17259183};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:17259183};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
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.
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 -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- POLYMORPHISM: Genetic variations in ABO define the ABO blood group
CC system [MIM:616093]. The ABO blood group system is the most important
CC blood group system in blood transfusion. The sequence shown here is
CC that of the A transferase. The B form differs by a few residues
CC substitution. Residues 266 and 268 are important for specificity. The
CC reference genome assembly (GRCh38/hg38) describes a non-functional O-
CC type ABO allele. The O-type ABO allele results in a guanine deletion
CC (NM_020469.2: c.286delG). This deletion induces a frameshift and
CC creates a premature stop codon resulting in a truncated (117 amino
CC acids) protein deprived of any glycosyltransferase activity
CC (PubMed:2333095). {ECO:0000269|PubMed:10462501,
CC ECO:0000269|PubMed:12829588, ECO:0000269|PubMed:1449469,
CC ECO:0000269|PubMed:15104652, ECO:0000269|PubMed:15489334,
CC ECO:0000269|PubMed:18513251, ECO:0000269|PubMed:2121736,
CC ECO:0000269|PubMed:2333095, ECO:0000269|PubMed:7598760,
CC ECO:0000269|PubMed:8839869, ECO:0000269|Ref.15, ECO:0000269|Ref.5,
CC ECO:0000269|Ref.9}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/abo/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Histo-
CC blood group ABO system transferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_450";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Histo-
CC blood group ABO system transferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_502";
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DR EMBL; J05175; AAA36792.1; -; mRNA.
DR EMBL; X84746; CAA59233.1; -; Genomic_DNA.
DR EMBL; X84747; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; X84748; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; X84749; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; X84750; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; X84751; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; X84752; CAA59233.1; JOINED; Genomic_DNA.
DR EMBL; AF134412; AAD26572.1; -; mRNA.
DR EMBL; AF134413; AAD26573.1; -; mRNA.
DR EMBL; AF134414; AAD26574.1; -; mRNA.
DR EMBL; AH007586; AAD26575.1; -; Genomic_DNA.
DR EMBL; AH007587; AAD26576.1; -; Genomic_DNA.
DR EMBL; AH007592; AAD26581.1; -; Genomic_DNA.
DR EMBL; AJ920329; CAI79116.1; -; Genomic_DNA.
DR EMBL; AM423110; CAM28424.1; -; Genomic_DNA.
DR EMBL; AM492698; CAM34526.1; -; Genomic_DNA.
DR EMBL; AM492699; CAM34527.1; -; Genomic_DNA.
DR EMBL; AY268591; AAP03430.1; -; Genomic_DNA.
DR EMBL; BC069595; AAH69595.1; -; mRNA.
DR EMBL; BC111575; AAI11576.1; -; mRNA.
DR EMBL; AJ536135; CAD60222.1; -; Genomic_DNA.
DR EMBL; AJ536136; CAD60223.1; -; Genomic_DNA.
DR EMBL; D82842; BAA11591.2; -; Genomic_DNA.
DR EMBL; D82843; BAA11592.2; -; Genomic_DNA.
DR EMBL; AF016622; AAB86462.1; -; Genomic_DNA.
DR EMBL; AF448199; AAQ04662.1; -; Genomic_DNA.
DR EMBL; AF448200; AAQ04663.1; -; Genomic_DNA.
DR EMBL; AJ276689; CAB81779.1; -; Genomic_DNA.
DR PIR; PC1165; PC1165.
DR RefSeq; NP_065202.2; NM_020469.2.
DR PDB; 1LZ0; X-ray; 1.80 A; A=64-354.
DR PDB; 1LZ7; X-ray; 1.65 A; A=64-354.
DR PDB; 1LZI; X-ray; 1.35 A; A=64-354.
DR PDB; 1LZJ; X-ray; 1.32 A; A=64-354.
DR PDB; 1R7T; X-ray; 2.09 A; A=64-345.
DR PDB; 1R7U; X-ray; 1.61 A; A=64-345.
DR PDB; 1R7V; X-ray; 2.09 A; A=64-345.
DR PDB; 1R7X; X-ray; 1.97 A; A=64-345.
DR PDB; 1R7Y; X-ray; 1.75 A; A=64-345.
DR PDB; 1R80; X-ray; 1.65 A; A=64-345.
DR PDB; 1R81; X-ray; 1.75 A; A=64-345.
DR PDB; 1R82; X-ray; 1.55 A; A=64-345.
DR PDB; 1WSZ; X-ray; 1.59 A; A=64-354.
DR PDB; 1WT0; X-ray; 1.80 A; A=64-354.
DR PDB; 1WT1; X-ray; 1.55 A; A=64-354.
DR PDB; 1WT2; X-ray; 1.90 A; A=64-354.
DR PDB; 1WT3; X-ray; 1.80 A; A=64-354.
DR PDB; 1XZ6; X-ray; 1.55 A; A=64-354.
DR PDB; 1ZHJ; X-ray; 1.59 A; A=64-354.
DR PDB; 1ZI1; X-ray; 1.57 A; A=64-354.
DR PDB; 1ZI3; X-ray; 1.69 A; A=64-354.
DR PDB; 1ZI4; X-ray; 1.85 A; A=64-354.
DR PDB; 1ZI5; X-ray; 1.55 A; A=64-354.
DR PDB; 1ZIZ; X-ray; 1.49 A; A=64-354.
DR PDB; 1ZJ0; X-ray; 1.67 A; A=64-354.
DR PDB; 1ZJ1; X-ray; 1.65 A; A=64-354.
DR PDB; 1ZJ2; X-ray; 1.69 A; A=64-354.
DR PDB; 1ZJ3; X-ray; 1.69 A; A=64-354.
DR PDB; 1ZJO; X-ray; 1.64 A; A=64-354.
DR PDB; 1ZJP; X-ray; 1.59 A; A=64-354.
DR PDB; 2A8U; X-ray; 1.69 A; A=64-354.
DR PDB; 2A8W; X-ray; 1.59 A; A=64-354.
DR PDB; 2I7B; X-ray; 1.99 A; A=64-354.
DR PDB; 2O1F; X-ray; 1.99 A; A=64-354.
DR PDB; 2O1G; X-ray; 1.71 A; A=64-354.
DR PDB; 2O1H; X-ray; 1.67 A; A=64-354.
DR PDB; 2PGV; X-ray; 1.79 A; A=64-354.
DR PDB; 2PGY; X-ray; 2.39 A; A=64-354.
DR PDB; 2RIT; X-ray; 1.43 A; A=64-354.
DR PDB; 2RIX; X-ray; 1.75 A; A=64-354.
DR PDB; 2RIY; X-ray; 1.55 A; A=64-354.
DR PDB; 2RIZ; X-ray; 1.45 A; A=64-354.
DR PDB; 2RJ0; X-ray; 1.52 A; A=64-354.
DR PDB; 2RJ1; X-ray; 1.55 A; A=64-354.
DR PDB; 2RJ4; X-ray; 1.47 A; A=64-354.
DR PDB; 2RJ5; X-ray; 1.45 A; A=64-354.
DR PDB; 2RJ6; X-ray; 1.41 A; A=64-354.
DR PDB; 2RJ7; X-ray; 1.70 A; A=64-354.
DR PDB; 2RJ8; X-ray; 1.69 A; A=64-354.
DR PDB; 2RJ9; X-ray; 1.69 A; A=64-354.
DR PDB; 2Y7A; X-ray; 2.06 A; A/B/C/D=64-354.
DR PDB; 3I0C; X-ray; 1.55 A; A=69-354.
DR PDB; 3I0D; X-ray; 1.90 A; A=69-354.
DR PDB; 3I0E; X-ray; 1.81 A; A=69-354.
DR PDB; 3I0F; X-ray; 1.56 A; A=69-354.
DR PDB; 3I0G; X-ray; 1.40 A; A=69-354.
DR PDB; 3I0H; X-ray; 2.00 A; A=69-354.
DR PDB; 3I0I; X-ray; 1.90 A; X=69-354.
DR PDB; 3I0J; X-ray; 1.48 A; A=69-354.
DR PDB; 3I0K; X-ray; 2.20 A; A=69-354.
DR PDB; 3I0L; X-ray; 1.60 A; A=69-354.
DR PDB; 3IOH; X-ray; 1.25 A; A=64-354.
DR PDB; 3IOI; X-ray; 1.45 A; A=64-354.
DR PDB; 3IOJ; X-ray; 1.65 A; A/B=64-354.
DR PDB; 3SX3; X-ray; 1.45 A; A=64-354.
DR PDB; 3SX5; X-ray; 1.43 A; A=64-354.
DR PDB; 3SX7; X-ray; 1.42 A; A=64-354.
DR PDB; 3SX8; X-ray; 1.47 A; A=64-354.
DR PDB; 3SXA; X-ray; 1.50 A; A=64-354.
DR PDB; 3SXB; X-ray; 1.49 A; A=64-354.
DR PDB; 3SXC; X-ray; 1.90 A; A=64-354.
DR PDB; 3SXD; X-ray; 1.55 A; A=64-354.
DR PDB; 3SXE; X-ray; 1.49 A; A=64-354.
DR PDB; 3SXG; X-ray; 1.86 A; A=64-354.
DR PDB; 3U0X; X-ray; 1.85 A; A/B=64-354.
DR PDB; 3U0Y; X-ray; 1.60 A; A/B=64-354.
DR PDB; 3V0L; X-ray; 1.75 A; A=64-354.
DR PDB; 3V0M; X-ray; 1.68 A; A/B=64-354.
DR PDB; 3V0N; X-ray; 1.75 A; A/B=64-354.
DR PDB; 3V0O; X-ray; 1.65 A; A/B=64-354.
DR PDB; 3V0P; X-ray; 1.90 A; A/B=64-354.
DR PDB; 3V0Q; X-ray; 1.80 A; A/B=64-354.
DR PDB; 3ZGF; X-ray; 1.70 A; A/B=64-354.
DR PDB; 3ZGG; X-ray; 1.90 A; A=64-354.
DR PDB; 4C2S; X-ray; 2.48 A; A/B=64-354.
DR PDB; 4FQW; X-ray; 2.02 A; A=64-354.
DR PDB; 4FRA; X-ray; 1.43 A; A=64-354.
DR PDB; 4FRB; X-ray; 1.54 A; A=64-354.
DR PDB; 4FRD; X-ray; 1.55 A; A=64-354.
DR PDB; 4FRE; X-ray; 1.85 A; A=64-354.
DR PDB; 4FRH; X-ray; 1.80 A; A=64-354.
DR PDB; 4FRL; X-ray; 1.90 A; A=64-354.
DR PDB; 4FRM; X-ray; 1.90 A; A=64-354.
DR PDB; 4FRO; X-ray; 1.75 A; A=64-354.
DR PDB; 4FRP; X-ray; 2.00 A; A=64-354.
DR PDB; 4FRQ; X-ray; 2.35 A; A=64-354.
DR PDB; 4GBP; X-ray; 2.15 A; A=64-354.
DR PDB; 4KC1; X-ray; 1.50 A; A=64-346.
DR PDB; 4KC2; X-ray; 1.70 A; A=64-346.
DR PDB; 4KC4; X-ray; 1.60 A; A=64-346.
DR PDB; 4KXO; X-ray; 2.00 A; A=64-354.
DR PDB; 4Y62; X-ray; 1.60 A; A=1-354.
DR PDB; 4Y63; X-ray; 1.30 A; A=1-354.
DR PDB; 4Y64; X-ray; 1.60 A; A=1-354.
DR PDB; 5BXC; X-ray; 1.40 A; A=64-354.
DR PDB; 5C1G; X-ray; 1.46 A; A=64-354.
DR PDB; 5C1H; X-ray; 1.55 A; A=64-354.
DR PDB; 5C1L; X-ray; 1.40 A; A=64-354.
DR PDB; 5C36; X-ray; 1.55 A; A=64-354.
DR PDB; 5C38; X-ray; 1.45 A; A=64-354.
DR PDB; 5C3A; X-ray; 1.33 A; A=64-354.
DR PDB; 5C3B; X-ray; 1.40 A; A=64-354.
DR PDB; 5C3D; X-ray; 1.39 A; A=64-354.
DR PDB; 5C47; X-ray; 1.39 A; A=64-354.
DR PDB; 5C48; X-ray; 1.46 A; A=64-354.
DR PDB; 5C49; X-ray; 1.49 A; A=64-354.
DR PDB; 5C4B; X-ray; 1.54 A; A=64-354.
DR PDB; 5C4C; X-ray; 1.43 A; A=64-354.
DR PDB; 5C4D; X-ray; 1.40 A; A=64-354.
DR PDB; 5C4E; X-ray; 1.55 A; A=64-354.
DR PDB; 5C4F; X-ray; 1.41 A; A=64-354.
DR PDB; 5C8R; X-ray; 1.45 A; A=64-354.
DR PDB; 5CMF; X-ray; 1.95 A; X=64-345.
DR PDB; 5CMG; X-ray; 1.83 A; X=64-354.
DR PDB; 5CMH; X-ray; 1.61 A; A=64-354.
DR PDB; 5CMI; X-ray; 1.85 A; A=64-354.
DR PDB; 5CMJ; X-ray; 1.73 A; A=64-354.
DR PDB; 5CQL; X-ray; 1.69 A; X=64-354.
DR PDB; 5CQM; X-ray; 1.65 A; X=64-354.
DR PDB; 5CQN; X-ray; 1.61 A; X=64-354.
DR PDB; 5CQO; X-ray; 1.69 A; A=64-354.
DR PDB; 5CQP; X-ray; 1.83 A; A=64-354.
DR PDB; 5M79; X-ray; 1.30 A; A=64-354.
DR PDB; 5M7A; X-ray; 1.30 A; A=64-354.
DR PDB; 5M7B; X-ray; 1.50 A; A=64-354.
DR PDB; 5M7C; X-ray; 1.60 A; A/B=64-354.
DR PDB; 5M7D; X-ray; 1.20 A; A=64-354.
DR PDB; 5TJK; X-ray; 1.45 A; A=64-354.
DR PDB; 5TJL; X-ray; 1.89 A; A=64-354.
DR PDB; 5TJN; X-ray; 1.47 A; A=64-354.
DR PDB; 5TJO; X-ray; 1.57 A; A=64-354.
DR PDB; 6BJI; X-ray; 1.54 A; A=64-354.
DR PDB; 6BJJ; X-ray; 1.45 A; A=64-354.
DR PDB; 6BJK; X-ray; 2.12 A; A=64-354.
DR PDB; 6BJL; X-ray; 1.69 A; A=64-345.
DR PDB; 6BJM; X-ray; 1.45 A; A=64-345.
DR PDB; 6GWY; X-ray; 1.40 A; A=64-354.
DR PDB; 6GWZ; X-ray; 1.65 A; A=64-354.
DR PDB; 6GX0; X-ray; 1.25 A; A=64-354.
DR PDB; 6GX1; X-ray; 1.60 A; A=64-354.
DR PDB; 6GX2; X-ray; 1.07 A; A=64-354.
DR PDBsum; 1LZ0; -.
DR PDBsum; 1LZ7; -.
DR PDBsum; 1LZI; -.
DR PDBsum; 1LZJ; -.
DR PDBsum; 1R7T; -.
DR PDBsum; 1R7U; -.
DR PDBsum; 1R7V; -.
DR PDBsum; 1R7X; -.
DR PDBsum; 1R7Y; -.
DR PDBsum; 1R80; -.
DR PDBsum; 1R81; -.
DR PDBsum; 1R82; -.
DR PDBsum; 1WSZ; -.
DR PDBsum; 1WT0; -.
DR PDBsum; 1WT1; -.
DR PDBsum; 1WT2; -.
DR PDBsum; 1WT3; -.
DR PDBsum; 1XZ6; -.
DR PDBsum; 1ZHJ; -.
DR PDBsum; 1ZI1; -.
DR PDBsum; 1ZI3; -.
DR PDBsum; 1ZI4; -.
DR PDBsum; 1ZI5; -.
DR PDBsum; 1ZIZ; -.
DR PDBsum; 1ZJ0; -.
DR PDBsum; 1ZJ1; -.
DR PDBsum; 1ZJ2; -.
DR PDBsum; 1ZJ3; -.
DR PDBsum; 1ZJO; -.
DR PDBsum; 1ZJP; -.
DR PDBsum; 2A8U; -.
DR PDBsum; 2A8W; -.
DR PDBsum; 2I7B; -.
DR PDBsum; 2O1F; -.
DR PDBsum; 2O1G; -.
DR PDBsum; 2O1H; -.
DR PDBsum; 2PGV; -.
DR PDBsum; 2PGY; -.
DR PDBsum; 2RIT; -.
DR PDBsum; 2RIX; -.
DR PDBsum; 2RIY; -.
DR PDBsum; 2RIZ; -.
DR PDBsum; 2RJ0; -.
DR PDBsum; 2RJ1; -.
DR PDBsum; 2RJ4; -.
DR PDBsum; 2RJ5; -.
DR PDBsum; 2RJ6; -.
DR PDBsum; 2RJ7; -.
DR PDBsum; 2RJ8; -.
DR PDBsum; 2RJ9; -.
DR PDBsum; 2Y7A; -.
DR PDBsum; 3I0C; -.
DR PDBsum; 3I0D; -.
DR PDBsum; 3I0E; -.
DR PDBsum; 3I0F; -.
DR PDBsum; 3I0G; -.
DR PDBsum; 3I0H; -.
DR PDBsum; 3I0I; -.
DR PDBsum; 3I0J; -.
DR PDBsum; 3I0K; -.
DR PDBsum; 3I0L; -.
DR PDBsum; 3IOH; -.
DR PDBsum; 3IOI; -.
DR PDBsum; 3IOJ; -.
DR PDBsum; 3SX3; -.
DR PDBsum; 3SX5; -.
DR PDBsum; 3SX7; -.
DR PDBsum; 3SX8; -.
DR PDBsum; 3SXA; -.
DR PDBsum; 3SXB; -.
DR PDBsum; 3SXC; -.
DR PDBsum; 3SXD; -.
DR PDBsum; 3SXE; -.
DR PDBsum; 3SXG; -.
DR PDBsum; 3U0X; -.
DR PDBsum; 3U0Y; -.
DR PDBsum; 3V0L; -.
DR PDBsum; 3V0M; -.
DR PDBsum; 3V0N; -.
DR PDBsum; 3V0O; -.
DR PDBsum; 3V0P; -.
DR PDBsum; 3V0Q; -.
DR PDBsum; 3ZGF; -.
DR PDBsum; 3ZGG; -.
DR PDBsum; 4C2S; -.
DR PDBsum; 4FQW; -.
DR PDBsum; 4FRA; -.
DR PDBsum; 4FRB; -.
DR PDBsum; 4FRD; -.
DR PDBsum; 4FRE; -.
DR PDBsum; 4FRH; -.
DR PDBsum; 4FRL; -.
DR PDBsum; 4FRM; -.
DR PDBsum; 4FRO; -.
DR PDBsum; 4FRP; -.
DR PDBsum; 4FRQ; -.
DR PDBsum; 4GBP; -.
DR PDBsum; 4KC1; -.
DR PDBsum; 4KC2; -.
DR PDBsum; 4KC4; -.
DR PDBsum; 4KXO; -.
DR PDBsum; 4Y62; -.
DR PDBsum; 4Y63; -.
DR PDBsum; 4Y64; -.
DR PDBsum; 5BXC; -.
DR PDBsum; 5C1G; -.
DR PDBsum; 5C1H; -.
DR PDBsum; 5C1L; -.
DR PDBsum; 5C36; -.
DR PDBsum; 5C38; -.
DR PDBsum; 5C3A; -.
DR PDBsum; 5C3B; -.
DR PDBsum; 5C3D; -.
DR PDBsum; 5C47; -.
DR PDBsum; 5C48; -.
DR PDBsum; 5C49; -.
DR PDBsum; 5C4B; -.
DR PDBsum; 5C4C; -.
DR PDBsum; 5C4D; -.
DR PDBsum; 5C4E; -.
DR PDBsum; 5C4F; -.
DR PDBsum; 5C8R; -.
DR PDBsum; 5CMF; -.
DR PDBsum; 5CMG; -.
DR PDBsum; 5CMH; -.
DR PDBsum; 5CMI; -.
DR PDBsum; 5CMJ; -.
DR PDBsum; 5CQL; -.
DR PDBsum; 5CQM; -.
DR PDBsum; 5CQN; -.
DR PDBsum; 5CQO; -.
DR PDBsum; 5CQP; -.
DR PDBsum; 5M79; -.
DR PDBsum; 5M7A; -.
DR PDBsum; 5M7B; -.
DR PDBsum; 5M7C; -.
DR PDBsum; 5M7D; -.
DR PDBsum; 5TJK; -.
DR PDBsum; 5TJL; -.
DR PDBsum; 5TJN; -.
DR PDBsum; 5TJO; -.
DR PDBsum; 6BJI; -.
DR PDBsum; 6BJJ; -.
DR PDBsum; 6BJK; -.
DR PDBsum; 6BJL; -.
DR PDBsum; 6BJM; -.
DR PDBsum; 6GWY; -.
DR PDBsum; 6GWZ; -.
DR PDBsum; 6GX0; -.
DR PDBsum; 6GX1; -.
DR PDBsum; 6GX2; -.
DR AlphaFoldDB; P16442; -.
DR SMR; P16442; -.
DR BioGRID; 106546; 5.
DR STRING; 9606.ENSP00000483018; -.
DR BindingDB; P16442; -.
DR ChEMBL; CHEMBL2321639; -.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB03772; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,5-Diol.
DR DrugBank; DB07357; 4-AMINO-2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL.
DR DrugBank; DB07378; 4-AMINO-2-OCTYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL.
DR DrugBank; DB04681; BETA-METHYLLACTOSIDE.
DR DrugBank; DB04680; GALACTOSE GREASE.
DR DrugBank; DB03501; Galactose-uridine-5'-diphosphate.
DR DrugBank; DB04678; H TYPE II TRISACCHARIDE.
DR DrugBank; DB04679; Human blood group H type 1 trisaccharide.
DR DrugBank; DB07341; octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranoside.
DR DrugBank; DB07633; octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR DrugBank; DB02196; Uridine-Diphosphate-N-Acetylgalactosamine.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; P16442; 1 site.
DR iPTMnet; P16442; -.
DR PhosphoSitePlus; P16442; -.
DR BioMuta; ABO; -.
DR DMDM; 114949; -.
DR jPOST; P16442; -.
DR MassIVE; P16442; -.
DR PeptideAtlas; P16442; -.
DR PRIDE; P16442; -.
DR ProteomicsDB; 53361; -.
DR DNASU; 28; -.
DR GeneID; 28; -.
DR KEGG; hsa:28; -.
DR CTD; 28; -.
DR DisGeNET; 28; -.
DR GeneCards; ABO; -.
DR HGNC; HGNC:79; ABO.
DR MIM; 110300; gene.
DR MIM; 616093; phenotype.
DR neXtProt; NX_P16442; -.
DR PharmGKB; PA24415; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR InParanoid; P16442; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; P16442; -.
DR BioCyc; MetaCyc:HS10887-MON; -.
DR BRENDA; 2.4.1.37; 2681.
DR BRENDA; 2.4.1.40; 2681.
DR BRENDA; 2.4.1.88; 2681.
DR PathwayCommons; P16442; -.
DR Reactome; R-HSA-9033807; ABO blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 28; 12 hits in 207 CRISPR screens.
DR ChiTaRS; ABO; human.
DR EvolutionaryTrace; P16442; -.
DR GeneWiki; ABO_(gene); -.
DR GenomeRNAi; 28; -.
DR Pharos; P16442; Tbio.
DR PRO; PR:P16442; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P16442; protein.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IMP:CAFA.
DR GO; GO:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004380; F:glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IMP:CAFA.
DR GO; GO:0000166; F:nucleotide binding; IMP:CAFA.
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 DisProt; DP00339; -.
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 3D-structure; Blood group antigen; Direct protein sequencing; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..354
FT /note="Histo-blood group ABO system transferase"
FT /id="PRO_0000012268"
FT CHAIN 54..354
FT /note="Fucosylglycoprotein alpha-N-
FT acetylgalactosaminyltransferase soluble form"
FT /id="PRO_0000012269"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 121..123
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000269|PubMed:12198488,
FT ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:15475562,
FT ECO:0000269|PubMed:16326711, ECO:0000269|PubMed:17259183,
FT ECO:0007744|PDB:1LZI, ECO:0007744|PDB:1LZJ,
FT ECO:0007744|PDB:1R7Y, ECO:0007744|PDB:1R80,
FT ECO:0007744|PDB:1R81, ECO:0007744|PDB:1R82,
FT ECO:0007744|PDB:1WT3, ECO:0007744|PDB:1ZI5,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJO,
FT ECO:0007744|PDB:1ZJP, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2A8W, ECO:0007744|PDB:2O1H,
FT ECO:0007744|PDB:2RIX, ECO:0007744|PDB:2RJ0,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ5, ECO:0007744|PDB:2RJ7,
FT ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9,
FT ECO:0007744|PDB:2Y7A, ECO:0007744|PDB:3I0D,
FT ECO:0007744|PDB:3I0F, ECO:0007744|PDB:3I0G,
FT ECO:0007744|PDB:3I0I, ECO:0007744|PDB:3I0K,
FT ECO:0007744|PDB:3I0L, ECO:0007744|PDB:3IOI,
FT ECO:0007744|PDB:3IOJ, ECO:0007744|PDB:3SX3,
FT ECO:0007744|PDB:3SX5, ECO:0007744|PDB:3SX7,
FT ECO:0007744|PDB:3SX8, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXC,
FT ECO:0007744|PDB:3SXD, ECO:0007744|PDB:3SXE,
FT ECO:0007744|PDB:3SXG, ECO:0007744|PDB:3U0Y,
FT ECO:0007744|PDB:3V0L, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FQW, ECO:0007744|PDB:4FRA,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRE, ECO:0007744|PDB:4FRH,
FT ECO:0007744|PDB:4FRL, ECO:0007744|PDB:4FRM,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP,
FT ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2,
FT ECO:0007744|PDB:4KC4"
FT BINDING 126
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000269|PubMed:12198488,
FT ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:15475562,
FT ECO:0000269|PubMed:16326711, ECO:0000269|PubMed:17259183,
FT ECO:0007744|PDB:1LZI, ECO:0007744|PDB:1LZJ,
FT ECO:0007744|PDB:1R7Y, ECO:0007744|PDB:1R80,
FT ECO:0007744|PDB:1R81, ECO:0007744|PDB:1R82,
FT ECO:0007744|PDB:1WT1, ECO:0007744|PDB:1WT2,
FT ECO:0007744|PDB:1WT3, ECO:0007744|PDB:1ZI5,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJO,
FT ECO:0007744|PDB:1ZJP, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2A8W, ECO:0007744|PDB:2O1H,
FT ECO:0007744|PDB:2RIX, ECO:0007744|PDB:2RJ0,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ5, ECO:0007744|PDB:2RJ7,
FT ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9,
FT ECO:0007744|PDB:2Y7A, ECO:0007744|PDB:3I0D,
FT ECO:0007744|PDB:3I0F, ECO:0007744|PDB:3I0G,
FT ECO:0007744|PDB:3I0I, ECO:0007744|PDB:3I0K,
FT ECO:0007744|PDB:3I0L, ECO:0007744|PDB:3IOI,
FT ECO:0007744|PDB:3IOJ, ECO:0007744|PDB:3SX3,
FT ECO:0007744|PDB:3SX5, ECO:0007744|PDB:3SX7,
FT ECO:0007744|PDB:3SX8, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXC,
FT ECO:0007744|PDB:3SXD, ECO:0007744|PDB:3SXE,
FT ECO:0007744|PDB:3SXG, ECO:0007744|PDB:3U0Y,
FT ECO:0007744|PDB:3V0L, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FQW, ECO:0007744|PDB:4FRA,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRE, ECO:0007744|PDB:4FRH,
FT ECO:0007744|PDB:4FRL, ECO:0007744|PDB:4FRM,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP,
FT ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2,
FT ECO:0007744|PDB:4KC4"
FT BINDING 211..213
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000269|PubMed:12198488,
FT ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:15475562,
FT ECO:0000269|PubMed:16326711, ECO:0000269|PubMed:17259183,
FT ECO:0007744|PDB:1LZI, ECO:0007744|PDB:1LZJ,
FT ECO:0007744|PDB:1R7Y, ECO:0007744|PDB:1R80,
FT ECO:0007744|PDB:1R81, ECO:0007744|PDB:1R82,
FT ECO:0007744|PDB:1WT1, ECO:0007744|PDB:1WT2,
FT ECO:0007744|PDB:1WT3, ECO:0007744|PDB:1ZI5,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJO,
FT ECO:0007744|PDB:1ZJP, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2A8W, ECO:0007744|PDB:2O1H,
FT ECO:0007744|PDB:2RIX, ECO:0007744|PDB:2RJ0,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ5, ECO:0007744|PDB:2RJ7,
FT ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9,
FT ECO:0007744|PDB:2Y7A, ECO:0007744|PDB:3I0D,
FT ECO:0007744|PDB:3I0F, ECO:0007744|PDB:3I0G,
FT ECO:0007744|PDB:3I0I, ECO:0007744|PDB:3I0K,
FT ECO:0007744|PDB:3I0L, ECO:0007744|PDB:3IOI,
FT ECO:0007744|PDB:3IOJ, ECO:0007744|PDB:3SX3,
FT ECO:0007744|PDB:3SX5, ECO:0007744|PDB:3SX7,
FT ECO:0007744|PDB:3SX8, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXC,
FT ECO:0007744|PDB:3SXD, ECO:0007744|PDB:3SXE,
FT ECO:0007744|PDB:3SXG, ECO:0007744|PDB:3U0Y,
FT ECO:0007744|PDB:3V0L, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FQW, ECO:0007744|PDB:4FRA,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRE, ECO:0007744|PDB:4FRH,
FT ECO:0007744|PDB:4FRL, ECO:0007744|PDB:4FRM,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP,
FT ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2,
FT ECO:0007744|PDB:4KC4"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:12198488,
FT ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:16326711,
FT ECO:0000269|PubMed:17259183, ECO:0007744|PDB:1LZJ,
FT ECO:0007744|PDB:1R80, ECO:0007744|PDB:1ZJ2,
FT ECO:0007744|PDB:1ZJP, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2O1H, ECO:0007744|PDB:2RIX,
FT ECO:0007744|PDB:2RJ0, ECO:0007744|PDB:2RJ1,
FT ECO:0007744|PDB:2RJ4, ECO:0007744|PDB:2RJ5,
FT ECO:0007744|PDB:2RJ7, ECO:0007744|PDB:2RJ8,
FT ECO:0007744|PDB:2RJ9, ECO:0007744|PDB:3I0F,
FT ECO:0007744|PDB:3IOI, ECO:0007744|PDB:3IOJ,
FT ECO:0007744|PDB:3SX3, ECO:0007744|PDB:3SX5,
FT ECO:0007744|PDB:3SX7, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXD,
FT ECO:0007744|PDB:3SXE, ECO:0007744|PDB:3SXG,
FT ECO:0007744|PDB:3U0Y, ECO:0007744|PDB:3V0L,
FT ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0O, ECO:0007744|PDB:3V0P,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRH, ECO:0007744|PDB:4FRL,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:12198488,
FT ECO:0000269|PubMed:12972418, ECO:0000269|PubMed:16326711,
FT ECO:0000269|PubMed:17259183, ECO:0007744|PDB:1LZJ,
FT ECO:0007744|PDB:1R80, ECO:0007744|PDB:1ZJ2,
FT ECO:0007744|PDB:1ZJP, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2O1H, ECO:0007744|PDB:2RIX,
FT ECO:0007744|PDB:2RJ0, ECO:0007744|PDB:2RJ1,
FT ECO:0007744|PDB:2RJ4, ECO:0007744|PDB:2RJ5,
FT ECO:0007744|PDB:2RJ7, ECO:0007744|PDB:2RJ8,
FT ECO:0007744|PDB:2RJ9, ECO:0007744|PDB:3I0F,
FT ECO:0007744|PDB:3IOI, ECO:0007744|PDB:3IOJ,
FT ECO:0007744|PDB:3SX3, ECO:0007744|PDB:3SX5,
FT ECO:0007744|PDB:3SX7, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXD,
FT ECO:0007744|PDB:3SXE, ECO:0007744|PDB:3SXG,
FT ECO:0007744|PDB:3U0Y, ECO:0007744|PDB:3V0L,
FT ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0O, ECO:0007744|PDB:3V0P,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRH, ECO:0007744|PDB:4FRL,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP"
FT BINDING 233
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000269|PubMed:16326711,
FT ECO:0007744|PDB:1ZHJ, ECO:0007744|PDB:1ZI3,
FT ECO:0007744|PDB:1ZI4, ECO:0007744|PDB:1ZI5,
FT ECO:0007744|PDB:1ZJ1, ECO:0007744|PDB:1ZJ2,
FT ECO:0007744|PDB:1ZJ3, ECO:0007744|PDB:2A8U,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ7, ECO:0007744|PDB:2RJ8,
FT ECO:0007744|PDB:2RJ9, ECO:0007744|PDB:3SX3,
FT ECO:0007744|PDB:3SX7, ECO:0007744|PDB:3SX8,
FT ECO:0007744|PDB:3SXA, ECO:0007744|PDB:3SXG,
FT ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0N,
FT ECO:0007744|PDB:3V0O, ECO:0007744|PDB:3V0P,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:3ZGF,
FT ECO:0007744|PDB:4C2S, ECO:0007744|PDB:4FQW,
FT ECO:0007744|PDB:4FRA, ECO:0007744|PDB:4FRB,
FT ECO:0007744|PDB:4FRD, ECO:0007744|PDB:4FRE,
FT ECO:0007744|PDB:4FRH, ECO:0007744|PDB:4FRL,
FT ECO:0007744|PDB:4FRM, ECO:0007744|PDB:4FRO,
FT ECO:0007744|PDB:4FRP, ECO:0007744|PDB:4FRQ,
FT ECO:0007744|PDB:4GBP, ECO:0007744|PDB:4KC1,
FT ECO:0007744|PDB:4KC2, ECO:0007744|PDB:4KC4"
FT BINDING 245
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000269|PubMed:12972418,
FT ECO:0000269|PubMed:15475562, ECO:0000269|PubMed:16326711,
FT ECO:0007744|PDB:1R7T, ECO:0007744|PDB:1R7U,
FT ECO:0007744|PDB:1WT2, ECO:0007744|PDB:1ZHJ,
FT ECO:0007744|PDB:1ZI3, ECO:0007744|PDB:1ZI4,
FT ECO:0007744|PDB:1ZI5, ECO:0007744|PDB:1ZIZ,
FT ECO:0007744|PDB:1ZJ0, ECO:0007744|PDB:1ZJ1,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJ3,
FT ECO:0007744|PDB:2A8U, ECO:0007744|PDB:2RIY,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ6, ECO:0007744|PDB:2RJ7,
FT ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9,
FT ECO:0007744|PDB:3SX3, ECO:0007744|PDB:3SX5,
FT ECO:0007744|PDB:3SX7, ECO:0007744|PDB:3SX8,
FT ECO:0007744|PDB:3SXA, ECO:0007744|PDB:3SXB,
FT ECO:0007744|PDB:3SXC, ECO:0007744|PDB:3SXD,
FT ECO:0007744|PDB:3SXE, ECO:0007744|PDB:3SXG,
FT ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0O,
FT ECO:0007744|PDB:3V0P, ECO:0007744|PDB:3V0Q,
FT ECO:0007744|PDB:4C2S, ECO:0007744|PDB:4FQW,
FT ECO:0007744|PDB:4FRA, ECO:0007744|PDB:4FRB,
FT ECO:0007744|PDB:4FRD, ECO:0007744|PDB:4FRE,
FT ECO:0007744|PDB:4FRH, ECO:0007744|PDB:4FRL,
FT ECO:0007744|PDB:4FRM, ECO:0007744|PDB:4FRO,
FT ECO:0007744|PDB:4FRP, ECO:0007744|PDB:4FRQ,
FT ECO:0007744|PDB:4GBP, ECO:0007744|PDB:4KC1,
FT ECO:0007744|PDB:4KC2, ECO:0007744|PDB:4KC4"
FT BINDING 303
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000269|PubMed:12972418,
FT ECO:0000269|PubMed:15475562, ECO:0000269|PubMed:16326711,
FT ECO:0007744|PDB:1R7T, ECO:0007744|PDB:1R7U,
FT ECO:0007744|PDB:1WT2, ECO:0007744|PDB:1ZHJ,
FT ECO:0007744|PDB:1ZI3, ECO:0007744|PDB:1ZI4,
FT ECO:0007744|PDB:1ZI5, ECO:0007744|PDB:1ZIZ,
FT ECO:0007744|PDB:1ZJ0, ECO:0007744|PDB:1ZJ1,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJ3,
FT ECO:0007744|PDB:2A8U, ECO:0007744|PDB:2RIY,
FT ECO:0007744|PDB:2RJ1, ECO:0007744|PDB:2RJ4,
FT ECO:0007744|PDB:2RJ6, ECO:0007744|PDB:2RJ7,
FT ECO:0007744|PDB:2RJ8, ECO:0007744|PDB:2RJ9,
FT ECO:0007744|PDB:3I0G, ECO:0007744|PDB:3I0L,
FT ECO:0007744|PDB:3IOI, ECO:0007744|PDB:3SX3,
FT ECO:0007744|PDB:3SX5, ECO:0007744|PDB:3SX7,
FT ECO:0007744|PDB:3SX8, ECO:0007744|PDB:3SXA,
FT ECO:0007744|PDB:3SXB, ECO:0007744|PDB:3SXC,
FT ECO:0007744|PDB:3SXD, ECO:0007744|PDB:3SXE,
FT ECO:0007744|PDB:3SXG, ECO:0007744|PDB:3V0L,
FT ECO:0007744|PDB:3V0M, ECO:0007744|PDB:3V0O,
FT ECO:0007744|PDB:3V0P, ECO:0007744|PDB:3V0Q,
FT ECO:0007744|PDB:3ZGG, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4FQW, ECO:0007744|PDB:4FRA,
FT ECO:0007744|PDB:4FRB, ECO:0007744|PDB:4FRD,
FT ECO:0007744|PDB:4FRE, ECO:0007744|PDB:4FRH,
FT ECO:0007744|PDB:4FRL, ECO:0007744|PDB:4FRM,
FT ECO:0007744|PDB:4FRO, ECO:0007744|PDB:4FRP,
FT ECO:0007744|PDB:4FRQ, ECO:0007744|PDB:4GBP,
FT ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2,
FT ECO:0007744|PDB:4KC4"
FT BINDING 326
FT /ligand="an alpha-L-fucosyl-(1->2)-beta-D-galactosyl
FT derivative"
FT /ligand_id="ChEBI:CHEBI:140327"
FT /evidence="ECO:0000269|PubMed:12972418,
FT ECO:0000269|PubMed:16326711, ECO:0007744|PDB:1R7T,
FT ECO:0007744|PDB:1ZI4, ECO:0007744|PDB:1ZI5,
FT ECO:0007744|PDB:1ZJ2, ECO:0007744|PDB:1ZJ3,
FT ECO:0007744|PDB:2RIY, ECO:0007744|PDB:2RJ1,
FT ECO:0007744|PDB:2RJ4, ECO:0007744|PDB:2RJ6,
FT ECO:0007744|PDB:2RJ7, ECO:0007744|PDB:2RJ8,
FT ECO:0007744|PDB:2RJ9, ECO:0007744|PDB:3V0M,
FT ECO:0007744|PDB:3V0O, ECO:0007744|PDB:3V0P,
FT ECO:0007744|PDB:3V0Q, ECO:0007744|PDB:4C2S,
FT ECO:0007744|PDB:4KC1, ECO:0007744|PDB:4KC2,
FT ECO:0007744|PDB:4KC4"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 35
FT /note="G -> R (in dbSNP:rs8176696)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_019147"
FT VARIANT 36
FT /note="V -> F (in dbSNP:rs688976)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_019148"
FT VARIANT 63
FT /note="R -> H (in dbSNP:rs549446)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_019149"
FT VARIANT 74
FT /note="P -> S (in dbSNP:rs512770)"
FT /evidence="ECO:0000269|PubMed:12829588, ECO:0000269|Ref.9"
FT /id="VAR_019150"
FT VARIANT 80..81
FT /note="CR -> W"
FT /id="VAR_003408"
FT VARIANT 156
FT /note="P -> L (in allele A2; dbSNP:rs1053878)"
FT /evidence="ECO:0000269|PubMed:12829588,
FT ECO:0000269|PubMed:7598760, ECO:0000269|PubMed:8839869,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.9"
FT /id="VAR_003409"
FT VARIANT 161
FT /note="R -> H (in dbSNP:rs8176738)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_019151"
FT VARIANT 163
FT /note="T -> M (in allele Aw08; dbSNP:rs55756402)"
FT /evidence="ECO:0000269|PubMed:12829588"
FT /id="VAR_036738"
FT VARIANT 176
FT /note="R -> G (in allele Aw08 and allele Bw08;
FT dbSNP:rs7853989)"
FT /evidence="ECO:0000269|PubMed:12829588,
FT ECO:0000269|PubMed:15104652, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8839869, ECO:0000269|Ref.15,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.9"
FT /id="VAR_003410"
FT VARIANT 198
FT /note="R -> W (in allele Aw07)"
FT /evidence="ECO:0000269|PubMed:12829588"
FT /id="VAR_036739"
FT VARIANT 199
FT /note="R -> C (in dbSNP:rs8176739)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_019152"
FT VARIANT 214
FT /note="M -> R (in allele Bel01; loss of manganese binding
FT and reduced catalytic activity)"
FT /evidence="ECO:0000269|PubMed:17259183,
FT ECO:0000269|PubMed:8839869"
FT /id="VAR_036740"
FT VARIANT 216
FT /note="F -> I (in dbSNP:rs8176740)"
FT /evidence="ECO:0000269|PubMed:8839869, ECO:0000269|Ref.9"
FT /id="VAR_019153"
FT VARIANT 223
FT /note="E -> D (in allele B106)"
FT /evidence="ECO:0000269|PubMed:8839869"
FT /id="VAR_036741"
FT VARIANT 230
FT /note="G -> R (in group B transferase; lower-level protein
FT expression and intracellular cytoplasmic mislocation)"
FT /evidence="ECO:0000269|PubMed:18513251"
FT /id="VAR_055227"
FT VARIANT 234
FT /note="P -> A (in allele B(A))"
FT /evidence="ECO:0000269|PubMed:10462501"
FT /id="VAR_072628"
FT VARIANT 235
FT /note="G -> S (in allele Bw08; dbSNP:rs8176743)"
FT /evidence="ECO:0000269|PubMed:12829588,
FT ECO:0000269|PubMed:15104652, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18513251, ECO:0000269|PubMed:8839869,
FT ECO:0000269|Ref.15, ECO:0000269|Ref.5, ECO:0000269|Ref.9"
FT /id="VAR_003411"
FT VARIANT 257
FT /note="P -> L (in dbSNP:rs8176745)"
FT /id="VAR_033540"
FT VARIANT 266
FT /note="L -> M (in allele Bw08; dbSNP:rs8176746)"
FT /evidence="ECO:0000269|PubMed:12829588,
FT ECO:0000269|PubMed:1449469, ECO:0000269|PubMed:15104652,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18513251,
FT ECO:0000269|PubMed:8839869, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.9"
FT /id="VAR_003412"
FT VARIANT 268
FT /note="G -> A (in allele Bw08; dbSNP:rs8176747)"
FT /evidence="ECO:0000269|PubMed:12829588,
FT ECO:0000269|PubMed:1449469, ECO:0000269|PubMed:15104652,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18513251,
FT ECO:0000269|PubMed:8839869, ECO:0000269|Ref.9"
FT /id="VAR_003413"
FT VARIANT 268
FT /note="G -> R (in allele Aw08; dbSNP:rs41302905)"
FT /evidence="ECO:0000269|PubMed:12829588"
FT /id="VAR_033541"
FT VARIANT 277
FT /note="V -> M (in dbSNP:rs8176748)"
FT /evidence="ECO:0000269|PubMed:8839869, ECO:0000269|Ref.9"
FT /id="VAR_019154"
FT VARIANT 288
FT /note="M -> R"
FT /evidence="ECO:0000269|PubMed:12829588"
FT /id="VAR_036742"
FT VARIANT 291
FT /note="D -> N (in allele B104)"
FT /evidence="ECO:0000269|PubMed:8839869"
FT /id="VAR_036743"
FT VARIANT 346
FT /note="K -> M (in allele Bw08)"
FT /evidence="ECO:0000269|PubMed:12829588, ECO:0000269|Ref.15"
FT /id="VAR_036744"
FT VARIANT 352
FT /note="R -> G (in allele A107)"
FT /evidence="ECO:0000269|PubMed:8839869"
FT /id="VAR_036745"
FT VARIANT 352
FT /note="R -> W (in allele A106 and allele B3)"
FT /evidence="ECO:0000269|PubMed:8839869"
FT /id="VAR_003414"
FT MUTAGEN 214
FT /note="M->T,V: Alters substrate specificity so that both
FT UDP-N-acetyl-D-galactosamine and UDP-galactose are
FT utilized."
FT /evidence="ECO:0000269|PubMed:17259183"
FT MUTAGEN 234
FT /note="P->S: Alters substrate specificity of group B
FT transferase."
FT MUTAGEN 303
FT /note="E->A: Decreases specific activity of group B
FT transferase almost to zero."
FT /evidence="ECO:0000269|PubMed:12198488"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:6GX2"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 274..293
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:6GX2"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6GX2"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:6GX2"
SQ SEQUENCE 354 AA; 40934 MW; A03DA16E630C1608 CRC64;
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS
REAFTYERRP QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP
