Reviewed, UniProtKB/Swiss-Prot P38649 (BGAT_MOUSE)

Names and origin

Protein names

Recommended name:
    Histo-blood group ABO system transferase
Alternative name(s):
    NAGAT
    Cis-AB transferase
    Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
    EC=2.4.1.40
    Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
    Histo-blood group A transferase
      Short name=A transferase
    Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
    EC=2.4.1.37
    Fucosylglycoprotein 3-alpha-galactosyltransferase
    Histo-blood group B transferase
      Short name=B transferase

Gene names

Name:

Abo

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 By similarity.
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 By similarity.
Tissue specificity	Submaxillary glands (at protein level). Ref.1
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.
Sequence similarities	Belongs to the glycosyltransferase 6 family.
Sequence caution	The sequence CAM23695.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fucosylgalactoside 3-alpha-galactosyltransferase activity Ref.1 Inferred from direct assay. Source: MGI glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Ref.1 Inferred from direct assay. Source: MGI manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 332	332	Histo-blood group ABO system transferase		PRO_0000157293
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Signal-anchor for type II membrane protein Potential
	Topological domain	35 – 332	298	Lumenal Potential
	Region	100 – 102	3	UDP-N-acetyl-galactosamine binding By similarity
	Region	190 – 192	3	UDP-N-acetyl-galactosamine binding By similarity
Sites
	Metal binding	190	1	Manganese By similarity
	Metal binding	192	1	Manganese By similarity
	Binding site	105	1	UDP-N-acetyl-galactosamine By similarity
	Binding site	212	1	Glycoprotein fucosyl-galactosyl group By similarity
	Binding site	224	1	Glycoprotein fucosyl-galactosyl group By similarity
	Binding site	282	1	Glycoprotein fucosyl-galactosyl group By similarity
	Binding site	305	1	Glycoprotein fucosyl-galactosyl group By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	77	1	G → R in BAC29005. Ref.2
	Sequence conflict	109	1	L → I in BAC29005. Ref.2
	Sequence conflict	160	1	W → C in BAC28473. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38649-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: C48DB1090EA0D3E4	FASTA	332	38,777
	10 20 30 40 50 60 MNLRGRPKCN FLHLGILPFA VFVLVFFGYL FLSFRSQNLG HPGAVTRNAY LQPRVLKPTR 70 80 90 100 110 120 KDVLVLTPWL APIIWEGTFN IDILNEQFRI RNTTIGLTVF AIKKYVVFLK LFLETAEQHF 130 140 150 160 170 180 MVGHKVIYYV FTDRPADVPQ VILGAGRQLV VLTVRNYTRW QDVSMHRMEM ISHFSERRFL 190 200 210 220 230 240 REVDYLVCAD ADMKFSDHVG VEILSTFFGT LHPGFYSSSR EAFTYERRPQ SQAYIPWDRG 250 260 270 280 290 300 DFYYGGAFFG GSVLEVYHLT KACHEAMMED KANGIEPVWH DESYLNKYLL YHKPTKVLSP 310 320 330 EYLWDQQLLG WPSIMKKLRY VAVPKDHQAI RN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine equivalent of the human histo-blood group ABO gene is a cis-AB gene and encodes a glycosyltransferase with both A and B transferase activity." Yamamoto M., Lin X.-H., Kominato Y., Hata Y., Noda R., Saitou N., Yamamoto F. J. Biol. Chem. 276:13701-13708(2001) [PubMed: 11278752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Epididymis and Urinary bladder.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis." Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K. Electrophoresis 15:735-745(1994) [PubMed: 7523108] [Abstract] Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE. Tissue: Fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB041038 Genomic DNA. Translation: BAB20559.1. AB041039 mRNA. Translation: BAB20560.1. AK033786 mRNA. Translation: BAC28473.1. AK035261 mRNA. Translation: BAC29005.1. AL773563 Genomic DNA. Translation: CAM23695.1. Sequence problems. AL773563 Genomic DNA. Translation: CAM23696.1. CH466542 Genomic DNA. Translation: EDL08332.1. BC116759 mRNA. Translation: AAI16760.1. BC116761 mRNA. Translation: AAI16762.1.
IPI	IPI00331267.
RefSeq	NP_109643.3.
UniGene	Mm.160386
3D structure databases
SMR	P38649. Positions 44-332.
ModBase	Search...
Protein-protein interaction databases
STRING	P38649.
Protein family/group databases
CAZy	GT6. Glycosyltransferase Family 6.
Proteomic databases
PRIDE	P38649.
Genome annotation databases
Ensembl	ENSMUST00000102900; ENSMUSP00000099964; ENSMUSG00000015787; Mus musculus. [Genome view]
GeneID	80908.
KEGG	mmu:80908.
Organism-specific databases
CTD	80908.
MGI	MGI:2135738. Abo.
Phylogenomic databases
eggNOG	maNOG16072.
HOVERGEN	P38649.
PhylomeDB	P38649.
Enzyme and pathway databases
BRENDA	2.4.1.37. 244. 2.4.1.40. 244.
Gene expression databases
ArrayExpress	P38649.
Bgee	P38649.
Genevestigator	P38649.
Family and domain databases
InterPro	IPR005076. Glyco_trans_6. [Graphical view]
PANTHER	PTHR10462. Glyco_trans_6. 1 hit.
Pfam	PF03414. Glyco_transf_6. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

BGAT_MOUSE

Accession

Primary (citable) accession number: P38649
Secondary accession number(s): A2AL98 , Q8BZH3, Q8BZQ6, Q9EQW2, Q9EQW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	December 16, 2008
Last modified:	January 19, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)