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Protein

Histo-blood group ABO system transferase

Gene

Abo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose.
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051UDP-N-acetyl-galactosamineBy similarity
Metal bindingi190 – 1901ManganeseBy similarity
Metal bindingi192 – 1921ManganeseBy similarity
Binding sitei212 – 2121Glycoprotein fucosyl-galactosyl groupBy similarity
Binding sitei224 – 2241Glycoprotein fucosyl-galactosyl groupBy similarity
Binding sitei282 – 2821Glycoprotein fucosyl-galactosyl groupBy similarity
Binding sitei305 – 3051Glycoprotein fucosyl-galactosyl groupBy similarity

GO - Molecular functioni

  1. fucosylgalactoside 3-alpha-galactosyltransferase activity Source: MGI
  2. glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Histo-blood group ABO system transferase
Alternative name(s):
Cis-AB transferase
Fucosylglycoprotein 3-alpha-galactosyltransferase
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC:2.4.1.40)
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.37)
Histo-blood group A transferase
Short name:
A transferase
Histo-blood group B transferase
Short name:
B transferase
NAGAT
Gene namesi
Name:Abo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2135738. Abo.

Subcellular locationi

Golgi apparatusGolgi 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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 332298LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. Golgi cisterna membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Histo-blood group ABO system transferasePRO_0000157293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP38649.
PRIDEiP38649.

PTM databases

PhosphoSiteiP38649.

Expressioni

Tissue specificityi

Submaxillary glands (at protein level).1 Publication

Gene expression databases

BgeeiP38649.
ExpressionAtlasiP38649. baseline and differential.
GenevestigatoriP38649.

Structurei

3D structure databases

ProteinModelPortaliP38649.
SMRiP38649. Positions 52-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1023UDP-N-acetyl-galactosamine bindingBy similarity
Regioni190 – 1923UDP-N-acetyl-galactosamine bindingBy similarity

Domaini

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 similaritiesi

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43612.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP38649.
KOiK00709.
OrthoDBiEOG7BZVSQ.
PhylomeDBiP38649.
TreeFamiTF330991.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P38649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLRGRPKCN FLHLGILPFA VFVLVFFGYL FLSFRSQNLG HPGAVTRNAY
60 70 80 90 100
LQPRVLKPTR KDVLVLTPWL APIIWEGTFN IDILNEQFRI RNTTIGLTVF
110 120 130 140 150
AIKKYVVFLK LFLETAEQHF MVGHKVIYYV FTDRPADVPQ VILGAGRQLV
160 170 180 190 200
VLTVRNYTRW QDVSMHRMEM ISHFSERRFL REVDYLVCAD ADMKFSDHVG
210 220 230 240 250
VEILSTFFGT LHPGFYSSSR EAFTYERRPQ SQAYIPWDRG DFYYGGAFFG
260 270 280 290 300
GSVLEVYHLT KACHEAMMED KANGIEPVWH DESYLNKYLL YHKPTKVLSP
310 320 330
EYLWDQQLLG WPSIMKKLRY VAVPKDHQAI RN
Length:332
Mass (Da):38,777
Last modified:December 16, 2008 - v2
Checksum:iC48DB1090EA0D3E4
GO

Sequence cautioni

The sequence CAM23695.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771G → R in BAC29005 (PubMed:16141072).Curated
Sequence conflicti109 – 1091L → I in BAC29005 (PubMed:16141072).Curated
Sequence conflicti160 – 1601W → C in BAC28473 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15811.1.
RefSeqiNP_001277373.1. NM_001290444.1.
NP_109643.3. NM_030718.5.
UniGeneiMm.160386.

Genome annotation databases

EnsembliENSMUST00000102900; ENSMUSP00000099964; ENSMUSG00000015787.
GeneIDi80908.
KEGGimmu:80908.
UCSCiuc008iwb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15811.1.
RefSeqiNP_001277373.1. NM_001290444.1.
NP_109643.3. NM_030718.5.
UniGeneiMm.160386.

3D structure databases

ProteinModelPortaliP38649.
SMRiP38649. Positions 52-324.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

PTM databases

PhosphoSiteiP38649.

Proteomic databases

PaxDbiP38649.
PRIDEiP38649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102900; ENSMUSP00000099964; ENSMUSG00000015787.
GeneIDi80908.
KEGGimmu:80908.
UCSCiuc008iwb.1. mouse.

Organism-specific databases

CTDi28.
MGIiMGI:2135738. Abo.

Phylogenomic databases

eggNOGiNOG43612.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP38649.
KOiK00709.
OrthoDBiEOG7BZVSQ.
PhylomeDBiP38649.
TreeFamiTF330991.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi350270.
PROiP38649.
SOURCEiSearch...

Gene expression databases

BgeeiP38649.
ExpressionAtlasiP38649. baseline and differential.
GenevestigatoriP38649.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Epididymis and Urinary bladder.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
    Tissue: Fibroblast.

Entry informationi

Entry nameiBGAT_MOUSE
AccessioniPrimary (citable) accession number: P38649
Secondary accession number(s): A2AL98
, Q8BZH3, Q8BZQ6, Q9EQW2, Q9EQW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 16, 2008
Last modified: January 7, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.