Histo-blood group ABO system transferase

Names and origin

Protein names

Recommended name:
    Histo-blood group ABO system transferase
Alternative name(s):
    NAGAT
Cleaved into the following 2 chains:
    1- Recommended name:
            Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
    2- Recommended name:
            Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Including the following 2 domains:
    1- Recommended name:
            Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
              EC=2.4.1.40
        Alternative name(s):
            Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
            Histo-blood group A transferase
              Short name=A transferase
    2- Recommended name:
            Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
              EC=2.4.1.37
        Alternative name(s):
            Fucosylglycoprotein 3-alpha-galactosyltransferase
            Histo-blood group B transferase
              Short name=B transferase

Gene names

Name:

ABO

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
Catalytic activity	UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactose. UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.
Cofactor	Binds 1 manganese ion per subunit. Ref.20
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note= Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Domain	The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.
Post-translational modification	The soluble form derives from the membrane form by proteolytic processing.
Polymorphism	The sequence shown is that of the A transferase. The B form differs by a few residues substitutions. The O phenotype results from a single base frameshift in the N-terminal extremity of the gene, resulting in a severly truncated protein without catalytic activity.
Sequence similarities	Belongs to the glycosyltransferase 6 family.

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Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Blood group antigen Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid glycosylation Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB integral to Golgi membrane Non-traceable author statement. Source: UniProtKB
Molecular function	fucosylgalactoside 3-alpha-galactosyltransferase activity Non-traceable author statement. Source: UniProtKB glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Non-traceable author statement. Source: UniProtKB manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase

PRO_0000012268

Chain

54 – 354

301

Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form

PRO_0000012269

Regions

Topological domain

1 – 32

32

Cytoplasmic Potential

Transmembrane

33 – 53

21

Signal-anchor for type II membrane protein Potential

Topological domain

54 – 354

301

Lumenal Potential

Region

121 – 123

3

UDP-N-acetyl-galactosamine binding

Region

211 – 213

3

UDP-N-acetyl-galactosamine binding

Sites

Metal binding

211

1

Manganese

Metal binding

213

1

Manganese

Binding site

126

1

UDP-N-acetyl-galactosamine

Binding site

233

1

Glycoprotein fucosyl-galactosyl group

Binding site

245

1

Glycoprotein fucosyl-galactosyl group

Binding site

303

1

Glycoprotein fucosyl-galactosyl group

Binding site

326

1

Glycoprotein fucosyl-galactosyl group

Amino acid modifications

Glycosylation

113

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

35

1

G → R: dbSNP rs8176696. Ref.6

VAR_019147

Natural variant

36

1

V → F: dbSNP rs688976. Ref.6

VAR_019148

Natural variant

63

1

R → H: dbSNP rs549446. Ref.6

VAR_019149

Natural variant

74

1

P → S: dbSNP rs512770. Ref.6 Ref.8

VAR_019150

Natural variant

80 – 81

2

CR → W

VAR_003408

Natural variant

156

1

P → L in allele A2. dbSNP rs1053878. Ref.6 Ref.8 Ref.3 Ref.5 Ref.9

VAR_003409

Natural variant

161

1

R → H: dbSNP rs8176738. Ref.6

VAR_019151

Natural variant

163

1

T → M in allele Aw08. Ref.8

VAR_036738

Natural variant

176

1

R → G in group B transferase. dbSNP rs7853989. Ref.6 Ref.8 Ref.5 Ref.9 Ref.7 Ref.11 Ref.12

VAR_003410

Natural variant

198

1

R → W in allele Aw07.

VAR_036739

Natural variant

199

1

R → C: dbSNP rs8176739. Ref.6

VAR_019152

Natural variant

214

1

M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. Ref.20 Ref.9

VAR_036740

Natural variant

216

1

F → I: dbSNP rs8176740. Ref.6 Ref.9

VAR_019153

Natural variant

223

1

E → D in allele B106. Ref.9

VAR_036741

Natural variant

235

1

G → S in group B transferase. dbSNP rs8176743. Ref.6 Ref.8 Ref.5 Ref.9 Ref.7 Ref.11 Ref.12

VAR_003411

Natural variant

257

1

P → L: dbSNP rs8176745.

VAR_033540

Natural variant

266

1

L → M in group B transferase; important for the specificity. dbSNP rs8176746. Ref.6 Ref.8 Ref.5 Ref.9 Ref.7 Ref.11 Ref.13

VAR_003412

Natural variant

268

1

G → A in group B transferase; important for the specificity. dbSNP rs8176747. Ref.6 Ref.8 Ref.9 Ref.7 Ref.11 Ref.13

VAR_003413

Natural variant

268

1

G → R: dbSNP rs8176747. Ref.6 Ref.8 Ref.9 Ref.7 Ref.11 Ref.13

VAR_033541

Natural variant

277

1

V → M: dbSNP rs8176748. Ref.6 Ref.9

VAR_019154

Natural variant

288

1

M → R Ref.8

VAR_036742

Natural variant

291

1

D → N in allele B104. Ref.9

VAR_036743

Natural variant

346

1

K → M in allele Bw08. Ref.8 Ref.12

VAR_036744

Natural variant

352

1

R → G in allele A107. Ref.9

VAR_036745

Natural variant

352

1

R → W in allele A106 and allele B3. Ref.9

VAR_003414

Experimental info

Mutagenesis

214

1

M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized Ref.20

Mutagenesis

234

1

P → S: Alters substrate specificity of group B transferase

Mutagenesis

303

1

E → A: Decreases specific activity of group B transferase almost to zero Ref.15

Secondary structure

1

.

354

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P16442-1 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: A03DA16E630C1608
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FASTA

354

40,934

        10         20         30         40         50         60 
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH 

        70         80         90        100        110        120 
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV 

       130        140        150        160        170        180 
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR 

       190        200        210        220        230        240 
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS 

       250        260        270        280        290        300 
REAFTYERRP QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW 

       310        320        330        340        350 
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-blood group A transferase) mRNA." Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S. J. Biol. Chem. 265:1146-1151(1990) [PubMed: 2104828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Molecular genetic basis of the histo-blood group ABO system." Yamamoto F., Clausen H., White T., Marken J., Hakomori S. Nature 345:229-233(1990) [PubMed: 2333095] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Genomic cloning of the human histo-blood group ABO locus." Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A. Biochem. Biophys. Res. Commun. 206:318-325(1995) [PubMed: 7598760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-156.
[4]	Erratum Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A. Biochem. Biophys. Res. Commun. 211:347-347(1995) [

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References