Reviewed, UniProtKB/Swiss-Prot Q3V1N9 (A3LT2_MOUSE)

Names and origin

Protein names

Recommended name:
    Alpha 1,3-galactosyltransferase 2
      Short name=A3galt2
    EC=2.4.1.87
Alternative name(s):
    Isoglobotriaosylceramide synthase
    iGb3 synthase
      Short name=iGb3S

Gene names

Name:	A3galt2
Synonyms:	Igb3s

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

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.

Ontologies

Keywords
Cellular component	Golgi apparatus
Domain	Signal
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	N-acetyllactosaminide 3-alpha-galactosyltransferase activity Inferred from electronic annotation. Source: EC 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
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 370	354	Alpha 1,3-galactosyltransferase 2		PRO_0000314871
Sites
	Metal binding	229	1	Manganese By similarity
	Metal binding	231	1	Manganese By similarity
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	130	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3V1N9-1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 12F4AEB917F2C380	FASTA	370	42,649
	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

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. , 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]	The mouse genome sequencing consortium Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK132334 mRNA. Translation: BAE21111.1. AL611983 Genomic DNA. Translation: CAP19394.1.
IPI	IPI00347406.
RefSeq	NP_001009819.1.
UniGene	Mm.300900
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT6. Glycosyltransferase Family 6.
Genome annotation databases
Ensembl	ENSMUSG00000028794. Mus musculus. [Contig view]
GeneID	215493.
KEGG	mmu:215493.
Organism-specific databases
MGI	MGI:2685279. A3galt2.
Phylogenomic databases
HOGENOM	Q3V1N9.
HOVERGEN	Q3V1N9.
OMA	Q3V1N9. ARWHDES.
Enzyme and pathway databases
BRENDA	2.4.1.87. 244.
Gene expression databases
Bgee	Q3V1N9.
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
NextBio	374760.
SOURCE	Search...

Entry information

Entry name

A3LT2_MOUSE

Accession

Primary (citable) accession number: Q3V1N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 11, 2005
Last modified:	June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)