B4GT2_HUMAN
ID B4GT2_HUMAN Reviewed; 372 AA.
AC O60909; B3KTP0; B4DE14; D3DPY6; D3DPY7; O60511; Q4V9L9; Q5T4X5; Q5T4Y5;
AC Q9BUP6; Q9NSY7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Beta-1,4-galactosyltransferase 2 {ECO:0000305};
DE Short=Beta-1,4-GalTase 2 {ECO:0000303|PubMed:9405390};
DE Short=Beta4Gal-T2;
DE Short=b4Gal-T2 {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=Lactose synthase A protein;
DE EC=2.4.1.22;
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=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2;
GN Name=B4GALT2 {ECO:0000312|HGNC:HGNC:925};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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.
RC TISSUE=Erythroleukemia;
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 MRNA] (ISOFORMS 1 AND 3).
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-122.
RC TISSUE=Chondrosarcoma;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-372 (ISOFORMS 1/2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
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 (PubMed:9405390). Can produce lactose
CC (PubMed:9405390). {ECO:0000269|PubMed:9405390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC Evidence={ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC Evidence={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:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={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:11588157,
CC ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
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=71 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157};
CC KM=0.011 mM for UDP-galactose {ECO:0000269|PubMed:9405390};
CC KM=0.16 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390};
CC KM=2.65 mM for D-GlcNAc {ECO:0000269|PubMed:9405390};
CC Vmax=207.6 pmol/min/mg enzyme towards UDP-galactose
CC {ECO:0000269|PubMed:9405390};
CC Vmax=352 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC Vmax=237.6 pmol/min/mg enzyme towards D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC O60909-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12261054, EBI-16439278;
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=3;
CC Name=1;
CC IsoId=O60909-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60909-2; Sequence=VSP_014103, VSP_014104;
CC Name=3;
CC IsoId=O60909-3; Sequence=VSP_043010;
CC -!- TISSUE SPECIFICITY: Weakly expressed in various tissues. Highest
CC expression in prostate, testis, ovary, intestine, 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 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_437";
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DR EMBL; Y12510; CAA73112.1; -; mRNA.
DR EMBL; AF038660; AAC39733.1; -; mRNA.
DR EMBL; AB024434; BAA75819.1; -; mRNA.
DR EMBL; AK095873; BAG53152.1; -; mRNA.
DR EMBL; AK293418; BAG56925.1; -; mRNA.
DR EMBL; AL139220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07062.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07063.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07064.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07065.1; -; Genomic_DNA.
DR EMBL; BC096821; AAH96821.1; -; mRNA.
DR EMBL; AL137647; CAB70857.1; -; mRNA.
DR CCDS; CCDS506.1; -. [O60909-1]
DR CCDS; CCDS55596.1; -. [O60909-3]
DR PIR; T46511; T46511.
DR RefSeq; NP_001005417.1; NM_001005417.2. [O60909-1]
DR RefSeq; NP_003771.1; NM_003780.4. [O60909-1]
DR RefSeq; NP_085076.2; NM_030587.2. [O60909-3]
DR RefSeq; XP_016858205.1; XM_017002716.1. [O60909-1]
DR RefSeq; XP_016858206.1; XM_017002717.1. [O60909-1]
DR AlphaFoldDB; O60909; -.
DR SMR; O60909; -.
DR BioGRID; 114247; 142.
DR IntAct; O60909; 4.
DR MINT; O60909; -.
DR STRING; 9606.ENSP00000310696; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; O60909; 3 sites.
DR iPTMnet; O60909; -.
DR PhosphoSitePlus; O60909; -.
DR BioMuta; B4GALT2; -.
DR jPOST; O60909; -.
DR MassIVE; O60909; -.
DR MaxQB; O60909; -.
DR PaxDb; O60909; -.
DR PeptideAtlas; O60909; -.
DR PRIDE; O60909; -.
DR ProteomicsDB; 49666; -. [O60909-1]
DR ProteomicsDB; 49667; -. [O60909-2]
DR ProteomicsDB; 49668; -. [O60909-3]
DR Antibodypedia; 32429; 194 antibodies from 27 providers.
DR DNASU; 8704; -.
DR Ensembl; ENST00000309519.8; ENSP00000310696.7; ENSG00000117411.18. [O60909-3]
DR Ensembl; ENST00000356836.10; ENSP00000349293.6; ENSG00000117411.18. [O60909-1]
DR Ensembl; ENST00000372324.6; ENSP00000361399.1; ENSG00000117411.18. [O60909-1]
DR Ensembl; ENST00000434555.7; ENSP00000407468.3; ENSG00000117411.18. [O60909-1]
DR GeneID; 8704; -.
DR KEGG; hsa:8704; -.
DR MANE-Select; ENST00000372324.6; ENSP00000361399.1; NM_003780.5; NP_003771.1.
DR UCSC; uc001clg.4; human. [O60909-1]
DR CTD; 8704; -.
DR DisGeNET; 8704; -.
DR GeneCards; B4GALT2; -.
DR HGNC; HGNC:925; B4GALT2.
DR HPA; ENSG00000117411; Low tissue specificity.
DR MIM; 604013; gene.
DR neXtProt; NX_O60909; -.
DR OpenTargets; ENSG00000117411; -.
DR PharmGKB; PA25224; -.
DR VEuPathDB; HostDB:ENSG00000117411; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000159367; -.
DR HOGENOM; CLU_044391_0_0_1; -.
DR InParanoid; O60909; -.
DR OMA; RCGEQPR; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; O60909; -.
DR TreeFam; TF312834; -.
DR BioCyc; MetaCyc:HS04130-MON; -.
DR BRENDA; 2.4.1.38; 2681.
DR BRENDA; 2.4.1.90; 2681.
DR PathwayCommons; O60909; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SABIO-RK; O60909; -.
DR SignaLink; O60909; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8704; 19 hits in 1077 CRISPR screens.
DR ChiTaRS; B4GALT2; human.
DR GeneWiki; B4GALT2; -.
DR GenomeRNAi; 8704; -.
DR Pharos; O60909; Tbio.
DR PRO; PR:O60909; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60909; protein.
DR Bgee; ENSG00000117411; Expressed in cortical plate and 172 other tissues.
DR Genevisible; O60909; HS.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004461; F:lactose synthase activity; IEA:UniProtKB-EC.
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:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..372
FT /note="Beta-1,4-galactosyltransferase 2"
FT /id="PRO_0000080533"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..372
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 56..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150..154
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..139
FT /evidence="ECO:0000250"
FT DISULFID 211..230
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014103"
FT VAR_SEQ 1
FT /note="M -> MAVEVQEQWPCLPAAGCPGPLGGPVAACGM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043010"
FT VAR_SEQ 119
FT /note="E -> MPSTQLLAAAAAAATAPGPTPPPLAPGSLRSPVPCPVPRLPRCHPVL
FT TRHLVL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014104"
FT VARIANT 122
FT /note="Q -> H (in dbSNP:rs1859728)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020487"
FT VARIANT 338
FT /note="G -> R (in dbSNP:rs35904809)"
FT /id="VAR_054021"
FT CONFLICT 100
FT /note="S -> TS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="P -> S (in Ref. 2; AAC39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> C (in Ref. 2; AAC39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="KH -> ND (in Ref. 2; AAC39733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41972 MW; A6F7800251AA1E4F CRC64;
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP AHALHPAASS
SSSSSNCSRP NATASSSGLP EVPSALPGPT APTLPPCPDS PPGLVGRLLI EFTSPMPLER
VQRENPGVLM GGRYTPPDCT PAQTVAVIIP FRHREHHLRY WLHYLHPILR RQRLRYGVYV
INQHGEDTFN RAKLLNVGFL EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA
MDKFGFRLPY AGYFGGVSGL SKAQFLRING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD
IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS RQPLFTNITV
DIGRPPSWPP RG
