ID   Q3UUA9_MOUSE            Unreviewed;       382 AA.
AC   Q3UUA9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Beta-1,4-galactosyltransferase {ECO:0000256|RuleBase:RU368121};
DE            Short=Beta-1,4-GalTase {ECO:0000256|RuleBase:RU368121};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
GN   Name=B4galt6 {ECO:0000313|MGI:MGI:1928380};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE23718.1};
RN   [1] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE23718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23718.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23337.1}, Mammary gland
RC   {ECO:0000313|EMBL:BAE26177.1}, and Spinal cord
RC   {ECO:0000313|EMBL:BAE23718.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
CC   -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC       oligosaccharides in many glycoproteins as well as the carbohydrate
CC       moieties of glycolipids. {ECO:0000256|RuleBase:RU368121}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU368121};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU368121}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC       {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR   EMBL; AK137385; BAE23337.1; -; mRNA.
DR   EMBL; AK138610; BAE23718.1; -; mRNA.
DR   EMBL; AK144997; BAE26177.1; -; mRNA.
DR   RefSeq; NP_062711.1; NM_019737.2.
DR   AlphaFoldDB; Q3UUA9; -.
DR   SMR; Q3UUA9; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   Antibodypedia; 41869; 144 antibodies from 27 providers.
DR   DNASU; 56386; -.
DR   GeneID; 56386; -.
DR   KEGG; mmu:56386; -.
DR   AGR; MGI:1928380; -.
DR   CTD; 9331; -.
DR   MGI; MGI:1928380; B4galt6.
DR   VEuPathDB; HostDB:ENSMUSG00000056124; -.
DR   HOGENOM; CLU_044391_6_0_1; -.
DR   OMA; VVWDCII; -.
DR   OrthoDB; 306273at2759; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 56386; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; B4galt6; mouse.
DR   ExpressionAtlas; Q3UUA9; baseline and differential.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0001572; P:lactosylceramide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00899; b4GalT; 1.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF47; BETA-1,4-GALACTOSYLTRANSFERASE 6; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368121};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368121};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU368121}; Manganese {ECO:0000256|RuleBase:RU368121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|RuleBase:RU368121};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          108..242
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          247..324
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   382 AA;  44759 MW;  0223621127896358 CRC64;
     MSALKRMMRV SNRSLIAFIF FFSLSTSCLY FIYVAPGIAN TYLFMVQARG IMLRENVKTI
     GHMIRLYTNK NTTLNGTDYP EGNNTSDYLV QTTTYLPQNF TYLPHLPCPE KLPYMRGFLS
     VNVSEISFDE VHQLFSKDSE IGPGGHWRPK DCKPRWKVAV LIPFRNRHEH LPIFFLHLIP
     MLQKQRLEFA FYVIEQTGTQ PFNRAMLFNV GFKEAMKDRA WDCVIFHDVD HLPENDRNYY
     GCGEMPRHFA AKLDKYMYIL PYKEFFGGVS GLTVEQFRKI NGFPNAFWGW GGEDDDLWNR
     VHYAGYNVTR PEGDLGKYIS IPHHHRGEVQ FLGRYKLLRY SKERQYIDGL NNLLYTPKIL
     VDRLYTNISV NLMPELAPIE DY
//