ID   A3LT2_MOUSE             Reviewed;         370 AA.
AC   Q3V1N9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Alpha 1,3-galactosyltransferase 2;
DE            Short=A3galt2;
DE            EC=2.4.1.87;
DE   AltName: Full=Isoglobotriaosylceramide synthase;
DE   AltName: Full=iGb3 synthase;
DE            Short=iGb3S;
DE   Flags: Precursor;
GN   Name=A3galt2; Synonyms=Igb3s;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RG   The mouse genome sequencing consortium;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfer of galactose from UDP-galactose to an acceptor
CC       molecule (R). Synthesizes the galactose-alpha(1,3)-galactose
CC       group, which is the most common carbohydrate containing terminal
CC       alpha-galactose. Preferentially glycosylates lipids.
CC   -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-beta-
CC       N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-
CC       D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus (Potential).
CC   -!- DOMAIN: The conserved DXD motif is involved in cofactor binding.
CC       The manganese ion interacts with the beta-phosphate group of UDP
CC       and may also have a role in catalysis.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 6 family.
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DR   EMBL; AK132334; BAE21111.1; -; mRNA.
DR   EMBL; AL611983; CAP19394.1; -; Genomic_DNA.
DR   IPI; IPI00347406; -.
DR   RefSeq; NP_001009819.1; -.
DR   UniGene; Mm.300900; -.
DR   CAZy; GT6; Glycosyltransferase Family 6.
DR   Ensembl; ENSMUSG00000028794; Mus musculus.
DR   GeneID; 215493; -.
DR   KEGG; mmu:215493; -.
DR   MGI; MGI:2685279; A3galt2.
DR   HOGENOM; Q3V1N9; -.
DR   HOVERGEN; Q3V1N9; -.
DR   OMA; Q3V1N9; ARWHDES.
DR   BRENDA; 2.4.1.87; 244.
DR   NextBio; 374760; -.
DR   Bgee; Q3V1N9; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047276; F:N-acetyllactosaminide 3-alpha-galactosyltra...; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR005076; Glyco_trans_6.
DR   PANTHER; PTHR10462; Glyco_trans_6; 1.
DR   Pfam; PF03414; Glyco_transf_6; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese;
KW   Metal-binding; Signal; Transferase.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    370       Alpha 1,3-galactosyltransferase 2.
FT                                /FTId=PRO_0000314871.
FT   METAL       229    229       Manganese (By similarity).
FT   METAL       231    231       Manganese (By similarity).
FT   CARBOHYD     88     88       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    130    130       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   370 AA;  42649 MW;  12F4AEB917F2C380 CRC64;
     MALGTELGVS WPGSHGSCRE QEGQRQRGPG KPTWGLSRAK KRLLWRFFLS AFGFLGLYHY
     RFIIIRLIEG SIPMGTCPTA IMPLPRDNFT GVLHHWARPE VLTCTSWGAP IIWDGTFDPH
     VAQQEARRRN LTIGLTVFAV GRYLEKYLEH FLVSAEQHFM VGQNVVYYVF TDRPEAVPYV
     ALGQGRLLRA KPVQRERRWQ DVSMARMPTL HEALGGQLGQ EADFVFCLDV DQYFTGNFGP
     EVLADLVAQL HAWHYRWPRW LLPYERDKRS AAALSLSEGD FYYHAAVFGG SVAALLKLTA
     HCATGQQLDH KRGIEALWHD ESHLNKFFWL NKPTKLLSPE FCWAEEIIWR REIHHPRLLW
     APKEYTLVRN
//