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 B3GN2_MOUSE             Reviewed;         397 AA.
Q9Z222; Q91V18;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 3.
25-OCT-2017, entry version 130.
RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2;
EC=2.4.1.149 {ECO:0000250|UniProtKB:Q9NY97};
AltName: Full=Beta-1,3-N-acetylglucosaminyltransferase 1;
Short=BGnT-1;
Short=Beta-1,3-Gn-T1;
Short=Beta3Gn-T1;
AltName: Full=Beta-1,3-galactosyltransferase 7;
Short=Beta-1,3-GalTase 7;
Short=Beta3Gal-T7;
Short=Beta3GalT7;
Short=b3Gal-T7;
AltName: Full=Beta-3-Gx-T7;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7;
AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2;
Short=BGnT-2;
Short=Beta-1,3-Gn-T2;
Short=Beta-1,3-N-acetylglucosaminyltransferase 2;
Short=Beta3Gn-T2;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7;
Name=B3GNT2; Synonyms=B3gnt1, Beta3gnt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND TISSUE
SPECIFICITY.
STRAIN=ICR {ECO:0000269|PubMed:9892646};
TISSUE=Neonatal brain {ECO:0000269|PubMed:9892646};
PubMed=9892646; DOI=10.1073/pnas.96.2.406;
Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
Vliegenthart J.F.G., Berger E.G., Hennet T.;
"A beta-1,3-N-acetylglucosaminyltransferase with poly-N-
acetyllactosamine synthase activity is structurally related to beta-
1,3-galactosyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999).
[2] {ECO:0000305}
SEQUENCE REVISION.
Zhou D., Berger E.G., Hennet T.;
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:AAK95359.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C.B17 {ECO:0000312|EMBL:AAK95359.1};
PubMed=11511811; DOI=10.1023/A:1010921313314;
Egan S., Cohen B., Sarkar M., Ying Y., Cohen S., Singh N., Wang W.,
Flock G., Goh T., Schachter H.;
"Molecular cloning and expression analysis of a mouse UDP-
GlcNAc:Gal(beta1-4)Glc(NAc)-R beta1,3-N-acetylglucosaminyltransferase
homologous to Drosophila melanogaster Brainiac and the beta1,3-
galactosyltransferase family.";
Glycoconj. J. 17:867-875(2000).
[4] {ECO:0000312|EMBL:AAH09075.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI {ECO:0000312|EMBL:AAH09075.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH09075.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17890318; DOI=10.1073/pnas.0707426104;
Togayachi A., Kozono Y., Ishida H., Abe S., Suzuki N., Tsunoda Y.,
Hagiwara K., Kuno A., Ohkura T., Sato N., Sato T., Hirabayashi J.,
Ikehara Y., Tachibana K., Narimatsu H.;
"Polylactosamine on glycoproteins influences basal levels of
lymphocyte and macrophage activation.";
Proc. Natl. Acad. Sci. U.S.A. 104:15829-15834(2007).
[6]
INTERACTION WITH B3GNT8.
PubMed=18826941; DOI=10.1074/jbc.M806933200;
Seko A., Yamashita K.;
"Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2)
by beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-
N-acetyllactosamine chains in differentiated HL-60 cells.";
J. Biol. Chem. 283:33094-33100(2008).
[7]
DISRUPTION PHENOTYPE.
PubMed=18008318; DOI=10.1002/mrd.20828;
Biellmann F., Henion T.R., Burki K., Hennet T.;
"Impaired sexual behavior in male mice deficient for the beta1-3 N-
acetylglucosaminyltransferase-I gene.";
Mol. Reprod. Dev. 75:699-706(2008).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-173.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[9]
DISRUPTION PHENOTYPE.
PubMed=23006775; DOI=10.1016/j.mcn.2012.09.003;
Henion T.R., Madany P.A., Faden A.A., Schwarting G.A.;
"beta3GnT2 null mice exhibit defective accessory olfactory bulb
innervation.";
Mol. Cell. Neurosci. 52:73-86(2013).
-!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
synthesis of poly-N-acetyllactosamine. Catalyzes the initiation
and elongation of poly-N-acetyllactosamine chains
(PubMed:9892646). Probably constitutes the main polylactosamine
synthase (PubMed:17890318). {ECO:0000269|PubMed:17890318,
ECO:0000269|PubMed:9892646}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + beta-D-
galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-
beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-
D-glucosaminyl-R. {ECO:0000250|UniProtKB:Q9NY97}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:9892646};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Interacts with B3GNT8; this interaction greatly increases
B3GNT2 catalytic activity, independently of B3GNT8 enzymatic
activity. {ECO:0000269|PubMed:18826941}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, kidney and
testis and, to a lesser extent, in liver and skeletal muscle. No
expression in spleen. {ECO:0000269|PubMed:9892646}.
-!- DISRUPTION PHENOTYPE: Strongly reduced number polylactosamine
structures on N-glycans in immunological tissues. B-cells and T-
cells proliferate show hyperproliferation (PubMed:17890318). Mice
also display defective accessory olfactory bulb innervation
(PubMed:23006775). Impaired sexual behaviour. While female mice
are fertile, males show a reduced rate of reproduction. Defects
cannot be attributed to any physical defect in their reproductive
organs, suggesting that the phenotype observed may result from an
impaired sexual response to female mating partners.
{ECO:0000269|PubMed:17890318, ECO:0000269|PubMed:18008318,
ECO:0000269|PubMed:23006775}.
-!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
{ECO:0000255}.
-!- CAUTION: There is some conflicting nomenclature, as some groups
still name this protein B3gnt1 (PubMed:18008318). The correct and
official nomenclature is however B3gnt2. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=MGC32391: hypothetical protein MGC32391/hypothetical protein
MGC32391;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_472";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=beta
3 GlcNAc-T I;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_571";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF092050; AAD09763.2; -; mRNA.
EMBL; AY043479; AAK95359.1; -; mRNA.
EMBL; BC009075; AAH09075.1; -; mRNA.
CCDS; CCDS24471.1; -.
RefSeq; NP_001162585.1; NM_001169114.1.
RefSeq; NP_058584.3; NM_016888.5.
UniGene; Mm.395495; -.
ProteinModelPortal; Q9Z222; -.
STRING; 10090.ENSMUSP00000053528; -.
CAZy; GT31; Glycosyltransferase Family 31.
iPTMnet; Q9Z222; -.
PhosphoSitePlus; Q9Z222; -.
MaxQB; Q9Z222; -.
PaxDb; Q9Z222; -.
PRIDE; Q9Z222; -.
DNASU; 53625; -.
Ensembl; ENSMUST00000055549; ENSMUSP00000053528; ENSMUSG00000051650.
Ensembl; ENSMUST00000062844; ENSMUSP00000060247; ENSMUSG00000051650.
GeneID; 53625; -.
KEGG; mmu:53625; -.
UCSC; uc007ieh.2; mouse.
CTD; 10678; -.
MGI; MGI:1889505; B3gnt2.
eggNOG; KOG2287; Eukaryota.
eggNOG; ENOG410ZZ1B; LUCA.
GeneTree; ENSGT00760000118879; -.
HOGENOM; HOG000232195; -.
HOVERGEN; HBG050653; -.
InParanoid; Q9Z222; -.
KO; K00741; -.
OMA; MDQPDIC; -.
OrthoDB; EOG091G0AXM; -.
PhylomeDB; Q9Z222; -.
TreeFam; TF318639; -.
Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
Reactome; R-MMU-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; B3gnt2; mouse.
PRO; PR:Q9Z222; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000051650; -.
ExpressionAtlas; Q9Z222; baseline and differential.
Genevisible; Q9Z222; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008378; F:galactosyltransferase activity; IEA:InterPro.
GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:UniProtKB.
GO; GO:0006486; P:protein glycosylation; IMP:MGI.
GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
InterPro; IPR002659; Glyco_trans_31.
PANTHER; PTHR11214; PTHR11214; 1.
Pfam; PF01762; Galactosyl_T; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 397 N-acetyllactosaminide beta-1,3-N-
acetylglucosaminyltransferase 2.
/FTId=PRO_0000219171.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 325 Lumenal. {ECO:0000255}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 283 283 R -> S (in Ref. 2; AAD09763).
{ECO:0000305}.
SEQUENCE 397 AA; 45883 MW; D8BBEA1866C1D106 CRC64;
MSVGRRRVKL LGILMMANVF IYLIVEVSKN SSQDKNGKGG VIIPKEKFWK PPSTPRAYWN
REQEKLNRWY NPILNRVANQ TGELATSPNT SHLSYCEPDS TVMTAVTDFN NLPDRFKDFL
LYLRCRNYSL LIDQPKKCAK KPFLLLAIKS LIPHFARRQA IRESWGRETN VGNQTVVRVF
LLGKTPPEDN HPDLSDMLKF ESDKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDAEF
VFKGDDDVFV NTHHILNYLN SLSKSKAKDL FIGDVIHNAG PHRDKKLKYY IPEVFYTGVY
PPYAGGGGFL YSGPLALRLY SATSRVHLYP IDDVYTGMCL QKLGLVPEKH KGFRTFDIEE
KNKKNICSYI DLMLVHSRKP QEMIDIWSQL QSPNLKC


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