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Entry: B3GT4_MOUSE A0A068BIS6_MOUSE
LinkDB: B3GT4_MOUSE A0A068BIS6_MOUSE
Original site: B3GT4_MOUSE A0A068BIS6_MOUSE 
ID   B3GT4_MOUSE             Reviewed;         371 AA.
AC   Q9Z0F0; Q91VC1; Q920U8; Q920U9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-OCT-2017, entry version 131.
DE   RecName: Full=Beta-1,3-galactosyltransferase 4;
DE            Short=Beta-1,3-GalTase 4;
DE            Short=Beta3Gal-T4;
DE            Short=Beta3GalT4;
DE            Short=b3Gal-T4;
DE            EC=2.4.1.62 {ECO:0000269|PubMed:10502288};
DE   AltName: Full=Gal-T2;
DE   AltName: Full=Ganglioside galactosyltransferase;
DE   AltName: Full=UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase;
GN   Name=B3galt4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Fetus;
RX   PubMed=10502288;
RX   DOI=10.1002/(SICI)1097-4547(19991015)58:2<318::AID-JNR12>3.0.CO;2-U;
RA   Daniotti J.L., Martina J.A., Zurita A.R., Maccioni H.J.F.;
RT   "Mouse beta 1,3-galactosyltransferase (GA1/GM1/GD1b synthase): protein
RT   characterization, tissue expression, and developmental regulation in
RT   neural retina.";
RL   J. Neurosci. Res. 58:318-327(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA   Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT   "Sequence of the mouse major histocompatibility complex class II
RT   region.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-370.
RC   STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
RC   NJL/Msf, Pgn2, and SWN/Msf;
RA   Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
RT   "Conspicuous differences among gene genealogies of 21 nuclear genes of
RT   five Mus musculus subspecies.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC       {ECO:0000269|PubMed:10502288}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + an N-acetyl-beta-D-
CC       galactosaminyl-(1->4)-(alpha-N-acetylneuraminyl-(2->3))-beta-D-
CC       galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + a beta-
CC       D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-(alpha-
CC       N-acetylneuraminyl-(2->3))-beta-D-galactosyl-(1->4)-beta-D-
CC       glucosyl-(1<->1)-ceramide. {ECO:0000269|PubMed:10502288}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, kidney,
CC       lung and testis. {ECO:0000269|PubMed:10502288}.
CC   -!- DEVELOPMENTAL STAGE: First expressed at embryonic day 3.
CC       Maintained at high levels between days 4 and 7 and declines
CC       thereafter to stabilize at low levels after day 10.
CC       {ECO:0000269|PubMed:10502288}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=b3GalT4;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_457";
DR   EMBL; AF082504; AAC69622.1; -; mRNA.
DR   EMBL; AF110520; AAC97977.1; -; Genomic_DNA.
DR   EMBL; AF100956; AAC69897.1; -; Genomic_DNA.
DR   EMBL; AB039164; BAB68688.1; -; Genomic_DNA.
DR   EMBL; AB039165; BAB68689.1; -; Genomic_DNA.
DR   EMBL; AB039167; BAB68691.1; -; Genomic_DNA.
DR   EMBL; AB039168; BAB68692.1; -; Genomic_DNA.
DR   EMBL; AB039170; BAB68694.1; -; Genomic_DNA.
DR   EMBL; AB039171; BAB68695.1; -; Genomic_DNA.
DR   EMBL; AB039172; BAB68696.1; -; Genomic_DNA.
DR   EMBL; AB039169; BAB68693.1; -; Genomic_DNA.
DR   EMBL; AB039166; BAB68690.1; -; Genomic_DNA.
DR   CCDS; CCDS28638.1; -.
DR   RefSeq; NP_062293.1; NM_019420.2.
DR   UniGene; Mm.11132; -.
DR   ProteinModelPortal; Q9Z0F0; -.
DR   SMR; Q9Z0F0; -.
DR   STRING; 10090.ENSMUSP00000084823; -.
DR   SwissLipids; SLP:000001417; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PhosphoSitePlus; Q9Z0F0; -.
DR   MaxQB; Q9Z0F0; -.
DR   PaxDb; Q9Z0F0; -.
DR   PRIDE; Q9Z0F0; -.
DR   Ensembl; ENSMUST00000087543; ENSMUSP00000084823; ENSMUSG00000067370.
DR   GeneID; 54218; -.
DR   KEGG; mmu:54218; -.
DR   UCSC; uc008caj.2; mouse.
DR   CTD; 8705; -.
DR   MGI; MGI:1859517; B3galt4.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   GeneTree; ENSGT00760000118879; -.
DR   HOGENOM; HOG000064523; -.
DR   HOVERGEN; HBG050651; -.
DR   InParanoid; Q9Z0F0; -.
DR   KO; K00715; -.
DR   OMA; PFCSWLQ; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   PhylomeDB; Q9Z0F0; -.
DR   TreeFam; TF318639; -.
DR   BRENDA; 2.4.1.62; 3474.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9Z0F0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000067370; -.
DR   ExpressionAtlas; Q9Z0F0; baseline and differential.
DR   Genevisible; Q9Z0F0; MM.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047915; F:ganglioside galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; ISO:MGI.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; ISO:MGI.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Polymorphism; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    371       Beta-1,3-galactosyltransferase 4.
FT                                /FTId=PRO_0000219161.
FT   TOPO_DOM      1      4       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      5     25       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     26    371       Lumenal. {ECO:0000255}.
FT   CARBOHYD    143    143       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     248    248       W -> R (in strain: pgn2).
FT   VARIANT     344    344       G -> W (in strain: BLG2/Msf).
SQ   SEQUENCE   371 AA;  41236 MW;  323A7FFA56B723B3 CRC64;
     MPLSLFRRVL LAVLLLVIIW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLISN
     SHACGGSGPP PFLLILVCTA PEHLNQRNAI RASWGAIREA RGFRVQTLFL LGKPRRQQLA
     DLSSESAAHR DILQASFQDS YRNLTLKTLS GLNWVNKYCP MARYILKTDD DVYVNVPELV
     SELIQRGGPS EQWQKGKEAQ EETTAIHEEH RGQAVPLLYL GRVHWRVRPT RTPESRHHVS
     EELWPENWGP FPPYASGTGY VLSISAVQLI LKVASRAPPL PLEDVFVGVS ARRGGLAPTH
     CVKLAGATHY PLDRCCYGKF LLTSHKVDPW QMQEAWKLVS GMNGERTAPF CSWLQGFLGT
     LRCRFIAWFS S
//
ID   A0A068BIS6_MOUSE        Unreviewed;       371 AA.
AC   A0A068BIS6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 31.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN   Name=B3galt4 {ECO:0000313|EMBL:AIC84001.1,
GN   ECO:0000313|MGI:MGI:1859517};
GN   ORFNames=mCG_22996 {ECO:0000313|EMBL:EDL10230.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AIC84001.1};
RN   [1] {ECO:0000313|EMBL:EDL10230.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL10230.1};
RX   PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [2] {ECO:0000313|EMBL:EDL10230.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL10230.1};
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AIC84001.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84001.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:AIC84001.1};
RA   Harrison E.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AIC84001.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84001.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:AIC84001.1};
RX   PubMed=26618355;
RA   Logunova N., Korotetskaya M., Polshakov V., Apt A.;
RT   "The QTL within the H2 Complex Involved in the Control of Tuberculosis
RT   Infection in Mice Is the Classical Class II H2-Ab1 Gene.";
RL   PLoS Genet. 11:E1005672-E1005672(2015).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane
CC       protein {ECO:0000256|RuleBase:RU363063}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000256|RuleBase:RU363063}.
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DR   EMBL; KJ650213; AIC84001.1; -; mRNA.
DR   EMBL; CH466660; EDL10230.1; -; Genomic_DNA.
DR   RefSeq; NP_062293.1; NM_019420.2.
DR   UniGene; Mm.11132; -.
DR   SMR; A0A068BIS6; -.
DR   GeneID; 54218; -.
DR   KEGG; mmu:54218; -.
DR   CTD; 8705; -.
DR   MGI; MGI:1859517; B3galt4.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   KO; K00715; -.
DR   OMA; PFCSWLQ; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   Bgee; ENSMUSG00000067370; -.
DR   ExpressionAtlas; A0A068BIS6; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100863, ECO:0000313|EMBL:AIC84001.1};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100862};
KW   Membrane {ECO:0000256|SAAS:SAAS00100854};
KW   Transferase {ECO:0000256|SAAS:SAAS00100874,
KW   ECO:0000313|EMBL:AIC84001.1};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00100864};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00100856}.
SQ   SEQUENCE   371 AA;  41236 MW;  323A7FFA56B723B3 CRC64;
     MPLSLFRRVL LAVLLLVIIW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLISN
     SHACGGSGPP PFLLILVCTA PEHLNQRNAI RASWGAIREA RGFRVQTLFL LGKPRRQQLA
     DLSSESAAHR DILQASFQDS YRNLTLKTLS GLNWVNKYCP MARYILKTDD DVYVNVPELV
     SELIQRGGPS EQWQKGKEAQ EETTAIHEEH RGQAVPLLYL GRVHWRVRPT RTPESRHHVS
     EELWPENWGP FPPYASGTGY VLSISAVQLI LKVASRAPPL PLEDVFVGVS ARRGGLAPTH
     CVKLAGATHY PLDRCCYGKF LLTSHKVDPW QMQEAWKLVS GMNGERTAPF CSWLQGFLGT
     LRCRFIAWFS S
//
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