B3GT2_HUMAN
ID B3GT2_HUMAN Reviewed; 422 AA.
AC O43825; B2RAB1; Q9BZQ9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Beta-1,3-galactosyltransferase 2 {ECO:0000305};
DE Short=Beta-1,3-GalTase 2;
DE Short=Beta3Gal-T2;
DE Short=Beta3GalT2;
DE EC=2.4.1.86 {ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303};
DE AltName: Full=UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2;
GN Name=B3GALT2 {ECO:0000312|HGNC:HGNC:917};
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9417100; DOI=10.1074/jbc.273.1.433;
RA Kolbinger F., Streiff M.B., Katopodis A.G.;
RT "Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-
RT galactosyltransferase catalyzing the formation of type 1 chains.";
RL J. Biol. Chem. 273:433-440(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=9582303; DOI=10.1074/jbc.273.21.12770;
RA Amado M., Almeida R., Carneiro F., Levery S.B., Holmes E.H., Nomoto M.,
RA Hollingsworth M.A., Hassan H., Schwientek T., Nielsen P.A., Bennett E.P.,
RA Clausen H.;
RT "A family of human beta3-galactosyltransferases. Characterization of four
RT members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-N-acetyl-
RT galactosamine beta-1,3-galactosyltransferase family.";
RL J. Biol. Chem. 273:12770-12778(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human RGS8
RT gene from the 1q25 region encompassing the hereditary prostate cancer
RT (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-galactose to substrates with a terminal beta-N-acetylglucosamine
CC (beta-GlcNAc) residue. Can also utilize substrates with a terminal
CC galactose residue, albeit with lower efficiency. Involved in the
CC biosynthesis of the carbohydrate moieties of glycolipids and
CC glycoproteins. Inactive towards substrates with terminal alpha-N-
CC acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-
CC GalNAc) residues. {ECO:0000269|PubMed:9417100,
CC ECO:0000269|PubMed:9582303}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133506; EC=2.4.1.86;
CC Evidence={ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303};
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 beta-D-Gal-(1->3)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.86;
CC Evidence={ECO:0000269|PubMed:9582303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC Evidence={ECO:0000269|PubMed:9582303};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-
CC alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-
CC GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:78565, ChEBI:CHEBI:142448;
CC Evidence={ECO:0000269|PubMed:9582303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937;
CC Evidence={ECO:0000269|PubMed:9582303};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9582303};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in heart and brain.
CC {ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC galactosyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_430";
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DR EMBL; Y15014; CAA75245.1; -; mRNA.
DR EMBL; Y15060; CAA75344.1; -; mRNA.
DR EMBL; AF288390; AAG60610.1; -; mRNA.
DR EMBL; AK314116; BAG36808.1; -; mRNA.
DR EMBL; AL390863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91251.1; -; Genomic_DNA.
DR EMBL; BC022507; AAH22507.1; -; mRNA.
DR CCDS; CCDS1383.1; -.
DR RefSeq; NP_003774.1; NM_003783.3.
DR AlphaFoldDB; O43825; -.
DR SMR; O43825; -.
DR BioGRID; 114250; 11.
DR IntAct; O43825; 6.
DR STRING; 9606.ENSP00000356404; -.
DR SwissLipids; SLP:000000773; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O43825; 5 sites.
DR iPTMnet; O43825; -.
DR PhosphoSitePlus; O43825; -.
DR BioMuta; B3GALT2; -.
DR PaxDb; O43825; -.
DR PeptideAtlas; O43825; -.
DR PRIDE; O43825; -.
DR ProteomicsDB; 49191; -.
DR Antibodypedia; 34468; 165 antibodies from 26 providers.
DR DNASU; 8707; -.
DR Ensembl; ENST00000367434.5; ENSP00000356404.4; ENSG00000162630.6.
DR GeneID; 8707; -.
DR KEGG; hsa:8707; -.
DR MANE-Select; ENST00000367434.5; ENSP00000356404.4; NM_003783.3; NP_003774.1.
DR UCSC; uc001gtc.5; human.
DR CTD; 8707; -.
DR GeneCards; B3GALT2; -.
DR HGNC; HGNC:917; B3GALT2.
DR HPA; ENSG00000162630; Tissue enhanced (brain, gallbladder, heart muscle).
DR MIM; 603018; gene.
DR neXtProt; NX_O43825; -.
DR OpenTargets; ENSG00000162630; -.
DR PharmGKB; PA25210; -.
DR VEuPathDB; HostDB:ENSG00000162630; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000155117; -.
DR HOGENOM; CLU_036849_2_1_1; -.
DR InParanoid; O43825; -.
DR OMA; TSYHFKY; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; O43825; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.62; 2681.
DR PathwayCommons; O43825; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; O43825; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8707; 9 hits in 1060 CRISPR screens.
DR GenomeRNAi; 8707; -.
DR Pharos; O43825; Tbio.
DR PRO; PR:O43825; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43825; protein.
DR Bgee; ENSG00000162630; Expressed in cortical plate and 137 other tissues.
DR Genevisible; O43825; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; TAS:ProtInc.
DR InterPro; IPR045821; B3GT2_N.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF19341; B3GALT2_N; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..422
FT /note="Beta-1,3-galactosyltransferase 2"
FT /id="PRO_0000219150"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..422
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 172
FT /note="Q -> R (in Ref. 3; AAG60610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 49213 MW; BA62942D6AFB4B0C CRC64;
MLQWRRRHCC FAKMTWNAKR SLFRTHLIGV LSLVFLFAMF LFFNHHDWLP GRAGFKENPV
TYTFRGFRST KSETNHSSLR NIWKETVPQT LRPQTATNSN NTDLSPQGVT GLENTLSANG
SIYNEKGTGH PNSYHFKYII NEPEKCQEKS PFLILLIAAE PGQIEARRAI RQTWGNESLA
PGIQITRIFL LGLSIKLNGY LQRAILEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT
YCPHIPYVMK TDSDMFVNTE YLINKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP
DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK LRIDPVPPPN
EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN KHNACANAAK EKAGRYRHRK
LH
