B4GT3_HUMAN
ID B4GT3_HUMAN Reviewed; 393 AA.
AC O60512; D3DVG3; O60910; Q9BPZ4; Q9H8T2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Beta-1,4-galactosyltransferase 3 {ECO:0000305};
DE Short=Beta-1,4-GalTase 3 {ECO:0000303|PubMed:9405390};
DE Short=Beta4Gal-T3;
DE Short=b4Gal-T3 {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.- {ECO:0000269|PubMed:9405390};
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.38 {ECO:0000269|PubMed:9405390};
DE AltName: Full=N-acetyllactosamine synthase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.90 {ECO:0000269|PubMed:9405390};
DE AltName: Full=Nal synthase;
DE AltName: Full=Neolactotriaosylceramide beta-1,4-galactosyltransferase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.275 {ECO:0000269|PubMed:9405390};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3;
GN Name=B4GALT3 {ECO:0000312|HGNC:HGNC:926};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9405390; DOI=10.1074/jbc.272.51.31979;
RA Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G.,
RA van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.;
RT "A family of human beta4-galactosyltransferases. Cloning and expression of
RT two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-
RT galactosyltransferases, beta4Gal-T2 and beta4Gal-T3.";
RL J. Biol. Chem. 272:31979-31991(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9597550; DOI=10.1093/glycob/8.5.517;
RA Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
RT "The expanding beta 4-galactosyltransferase gene family: messages from the
RT databanks.";
RL Glycobiology 8:517-526(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RX PubMed=11588157; DOI=10.1093/glycob/11.10.813;
RA Guo S., Sato T., Shirane K., Furukawa K.;
RT "Galactosylation of N-linked oligosaccharides by human beta-1,4-
RT galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.";
RL Glycobiology 11:813-820(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Eye, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP REVIEW.
RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA Amado M., Almeida R., Schwientek T., Clausen H.;
RT "Identification and characterization of large galactosyltransferase gene
RT families: galactosyltransferases for all functions.";
RL Biochim. Biophys. Acta 1473:35-53(1999).
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:0000269|PubMed:11588157,
CC ECO:0000269|PubMed:9405390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133507; EC=2.4.1.38;
CC Evidence={ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC EC=2.4.1.90; Evidence={ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000269|PubMed:9405390};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside
CC nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC Evidence={ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000269|PubMed:9405390};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP;
CC Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264;
CC Evidence={ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000269|PubMed:9405390};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) +
CC UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378;
CC Evidence={ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000269|PubMed:9405390};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157};
CC KM=0.084 mM for UDP-galactose {ECO:0000269|PubMed:9405390};
CC KM=0.58 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390};
CC KM=13.1 mM for D-GlcNAc {ECO:0000269|PubMed:9405390};
CC Vmax=64.35 pmol/min/mg enzyme towards UDP-galactose
CC {ECO:0000269|PubMed:9405390};
CC Vmax=66.25 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC Vmax=60.85 pmol/min/mg enzyme towards D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Trans cisternae of Golgi stack.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60512-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60512-2; Sequence=VSP_014106, VSP_014107;
CC -!- TISSUE SPECIFICITY: Found in various tissues. Highest expression in
CC placenta, prostate, testis, ovary, intestine and muscle, and in fetal
CC brain. {ECO:0000269|PubMed:9405390}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4-
CC galactosyltransferase 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_438";
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DR EMBL; Y12509; CAA73111.1; -; mRNA.
DR EMBL; AF038661; AAC39734.1; -; mRNA.
DR EMBL; AB024435; BAA75820.1; -; mRNA.
DR EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK023311; BAB14520.1; -; mRNA.
DR EMBL; CH471121; EAW52628.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52629.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52630.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52631.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52632.1; -; Genomic_DNA.
DR EMBL; BC000276; AAH00276.1; -; mRNA.
DR EMBL; BC006099; AAH06099.1; -; mRNA.
DR EMBL; BC009985; AAH09985.1; -; mRNA.
DR CCDS; CCDS1222.1; -. [O60512-1]
DR RefSeq; NP_001186802.1; NM_001199873.1. [O60512-1]
DR RefSeq; NP_001186803.1; NM_001199874.1. [O60512-1]
DR RefSeq; NP_003770.1; NM_003779.3. [O60512-1]
DR RefSeq; XP_005245623.1; XM_005245566.1. [O60512-1]
DR AlphaFoldDB; O60512; -.
DR SMR; O60512; -.
DR BioGRID; 114246; 124.
DR IntAct; O60512; 25.
DR STRING; 9606.ENSP00000480428; -.
DR SwissLipids; SLP:000000790; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyConnect; 1032; 6 N-Linked glycans (2 sites).
DR GlyGen; O60512; 5 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; O60512; -.
DR PhosphoSitePlus; O60512; -.
DR SwissPalm; O60512; -.
DR BioMuta; B4GALT3; -.
DR EPD; O60512; -.
DR jPOST; O60512; -.
DR MassIVE; O60512; -.
DR MaxQB; O60512; -.
DR PaxDb; O60512; -.
DR PeptideAtlas; O60512; -.
DR PRIDE; O60512; -.
DR ProteomicsDB; 49451; -. [O60512-1]
DR ProteomicsDB; 49452; -. [O60512-2]
DR Antibodypedia; 2534; 223 antibodies from 27 providers.
DR DNASU; 8703; -.
DR Ensembl; ENST00000319769.10; ENSP00000320965.5; ENSG00000158850.15. [O60512-1]
DR Ensembl; ENST00000367998.5; ENSP00000356977.1; ENSG00000158850.15. [O60512-1]
DR Ensembl; ENST00000622395.4; ENSP00000480428.1; ENSG00000158850.15. [O60512-1]
DR GeneID; 8703; -.
DR KEGG; hsa:8703; -.
DR MANE-Select; ENST00000319769.10; ENSP00000320965.5; NM_003779.4; NP_003770.1.
DR UCSC; uc001fyq.3; human. [O60512-1]
DR CTD; 8703; -.
DR DisGeNET; 8703; -.
DR GeneCards; B4GALT3; -.
DR HGNC; HGNC:926; B4GALT3.
DR HPA; ENSG00000158850; Low tissue specificity.
DR MIM; 604014; gene.
DR neXtProt; NX_O60512; -.
DR OpenTargets; ENSG00000158850; -.
DR PharmGKB; PA25225; -.
DR VEuPathDB; HostDB:ENSG00000158850; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158549; -.
DR HOGENOM; CLU_044391_1_2_1; -.
DR InParanoid; O60512; -.
DR OMA; CDPGGPR; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; O60512; -.
DR TreeFam; TF312834; -.
DR BioCyc; MetaCyc:HS08336-MON; -.
DR PathwayCommons; O60512; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; O60512; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8703; 31 hits in 1079 CRISPR screens.
DR ChiTaRS; B4GALT3; human.
DR GeneWiki; B4GALT3; -.
DR GenomeRNAi; 8703; -.
DR Pharos; O60512; Tbio.
DR PRO; PR:O60512; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60512; protein.
DR Bgee; ENSG00000158850; Expressed in oocyte and 196 other tissues.
DR ExpressionAtlas; O60512; baseline and differential.
DR Genevisible; O60512; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 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; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Beta-1,4-galactosyltransferase 3"
FT /id="PRO_0000080537"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 339..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..134
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 196..197
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 260..263
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 291..293
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..119
FT /evidence="ECO:0000250"
FT DISULFID 190..209
FT /evidence="ECO:0000250"
FT VAR_SEQ 116..145
FT /note="PAGCEPRSRTAIIVPHRAREHHLRLLLYHL -> PAALPPAPLLAAPAACLW
FT HLCHPPGWKWNI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014106"
FT VAR_SEQ 146..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014107"
FT CONFLICT 64
FT /note="A -> R (in Ref. 2; AAC39734)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="G -> A (in Ref. 2; AAC39734)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="K -> S (in Ref. 2; AAC39734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43928 MW; CA0BF955F95ED1F4 CRC64;
MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DQGPTFDYSH PRDVYSNLSH
LPGAPGGPPA PQGLPYCPER SPLLVGPVSV SFSPVPSLAE IVERNPRVEP GGRYRPAGCE
PRSRTAIIVP HRAREHHLRL LLYHLHPFLQ RQQLAYGIYV IHQAGNGTFN RAKLLNVGVR
EALRDEEWDC LFLHDVDLLP ENDHNLYVCD PRGPRHVAVA MNKFGYSLPY PQYFGGVSAL
TPDQYLKMNG FPNEYWGWGG EDDDIATRVR LAGMKISRPP TSVGHYKMVK HRGDKGNEEN
PHRFDLLVRT QNSWTQDGMN SLTYQLLARE LGPLYTNITA DIGTDPRGPR APSGPRYPPG
SSQAFRQEML QRRPPARPGP LSTANHTALR GSH
