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Reviewed, UniProtKB/Swiss-Prot Q3V1N9 (A3LT2_MOUSE)

Last modified February 9, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha 1,3-galactosyltransferase 2
      Short name=A3galt2
    EC=2.4.1.87
Alternative name(s):
    Isoglobotriaosylceramide synthase
      Short name=iGb3 synthase
      Short name=iGb3S
Gene names
Name: A3galt2
Synonyms: Igb3s
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Transfer of galactose from UDP-galactose to an acceptor molecule (R). Synthesizes the galactose-alpha(1,3)-galactose group, which is the most common carbohydrate containing terminal alpha-galactose. Preferentially glycosylates lipids.

Catalytic activity

UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus Potential.

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.

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Ontologies

Keywords
   Cellular componentGolgi apparatus
   DomainSignal
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionN-acetyllactosaminide 3-alpha-galactosyltransferase activity

Inferred from electronic annotation. Source: EC

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 370354Alpha 1,3-galactosyltransferase 2
PRO_0000314871

Sites

Metal binding2291Manganese By similarity
Metal binding2311Manganese By similarity

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q3V1N9-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 12F4AEB917F2C380

FASTA37042,649
        10         20         30         40         50         60 
MALGTELGVS WPGSHGSCRE QEGQRQRGPG KPTWGLSRAK KRLLWRFFLS AFGFLGLYHY 

        70         80         90        100        110        120 
RFIIIRLIEG SIPMGTCPTA IMPLPRDNFT GVLHHWARPE VLTCTSWGAP IIWDGTFDPH 

       130        140        150        160        170        180 
VAQQEARRRN LTIGLTVFAV GRYLEKYLEH FLVSAEQHFM VGQNVVYYVF TDRPEAVPYV 

       190        200        210        220        230        240 
ALGQGRLLRA KPVQRERRWQ DVSMARMPTL HEALGGQLGQ EADFVFCLDV DQYFTGNFGP 

       250        260        270        280        290        300 
EVLADLVAQL HAWHYRWPRW LLPYERDKRS AAALSLSEGD FYYHAAVFGG SVAALLKLTA 

       310        320        330        340        350        360 
HCATGQQLDH KRGIEALWHD ESHLNKFFWL NKPTKLLSPE FCWAEEIIWR REIHHPRLLW 

       370 
APKEYTLVRN

« Hide

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References

[1]"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. expand/collapse author list , 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: Head.
[2]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK132334 mRNA. Translation: BAE21111.1.
AL611983 Genomic DNA. Translation: CAP19394.1.
IPIIPI00347406.
RefSeqNP_001009819.1.
UniGeneMm.300900

3D structure databases

HSSPHSSP built from PDB template 1ZIZ based on UniProtKB Q4LAQ2.
SMRQ3V1N9. Positions 93-370.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3V1N9.

Protein family/group databases

CAZyGT6. Glycosyltransferase Family 6.

Proteomic databases

PRIDEQ3V1N9.

Genome annotation databases

EnsemblENSMUST00000030585; ENSMUSP00000030585; ENSMUSG00000028794; Mus musculus. [Genome view]
GeneID215493.
KEGGmmu:215493.
UCSCuc008uvm.1. mouse.

Organism-specific databases

CTD215493.
MGIMGI:2685279. A3galt2.

Phylogenomic databases

eggNOGroNOG11243.
HOGENOMHBG446077.
HOVERGENQ3V1N9.
InParanoidQ3V1N9.
OMAARWHDES.
PhylomeDBQ3V1N9.

Enzyme and pathway databases

BRENDA2.4.1.87. 244.

Gene expression databases

BgeeQ3V1N9.
GenevestigatorQ3V1N9.

Family and domain databases

InterProIPR005076. Glyco_trans_6.
[Graphical view]
PANTHERPTHR10462. Glyco_trans_6. 1 hit.
PfamPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio374760.
SOURCESearch...

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Entry information

Entry nameA3LT2_MOUSE
AccessionPrimary (citable) accession number: Q3V1N9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2005
Last modified: February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents