B3GT5_HUMAN
ID B3GT5_HUMAN Reviewed; 310 AA.
AC Q9Y2C3; A8KA86; D3DSI3; Q2M3L5; Q53Z19; Q9NY96; Q9P1X6; Q9P1X7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Beta-1,3-galactosyltransferase 5 {ECO:0000305};
DE Short=Beta-1,3-GalTase 5;
DE Short=Beta3Gal-T5;
DE Short=Beta3GalT5;
DE Short=b3Gal-T5;
DE EC=2.4.1.- {ECO:0000269|PubMed:10406968, ECO:0000269|PubMed:10837462};
DE AltName: Full=Beta-3-Gx-T5;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5;
GN Name=B3GALT5 {ECO:0000312|HGNC:HGNC:920};
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].
RC TISSUE=Colon adenocarcinoma;
RX PubMed=10212226; DOI=10.1074/jbc.274.18.12499;
RA Isshiki S., Togayachi A., Kudo T., Nishihara S., Watanabe M., Kubota T.,
RA Kitajima M., Shiraishi N., Sasaki K., Andoh T., Narimatsu H.;
RT "Cloning, expression, and characterization of a novel UDP-galactose:beta-N-
RT acetylglucosamine beta1,3-galactosyltransferase (beta3Gal-T5) responsible
RT for synthesis of type 1 chain in colorectal and pancreatic epithelia and
RT tumor cells derived therefrom.";
RL J. Biol. Chem. 274:12499-12507(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=10406968; DOI=10.1046/j.1432-1327.1999.00541.x;
RA Zhou D., Berger E.G., Hennet T.;
RT "Molecular cloning of a human UDP-galactose:GlcNAcbeta1,3GalNAc beta1, 3
RT galactosyltransferase gene encoding an O-linked core3-elongation enzyme.";
RL Eur. J. Biochem. 263:571-576(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-85.
RA Amado M., Carneiro F., Clausen H.;
RT "Cloning and expression of two beta-1,3-galactosyltransferases: beta3gal-T5
RT and beta3gal-T6.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14534330; DOI=10.1073/pnas.2134464100;
RA Dunn C.A., Medstrand P., Mager D.L.;
RT "An endogenous retroviral long terminal repeat is the dominant promoter for
RT human beta1,3-galactosyltransferase 5 in the colon.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12841-12846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-85.
RC TISSUE=Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-85.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-85.
RC TISSUE=Colon;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-298, AND VARIANT THR-85.
RA Liu Y., Saitou N.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
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).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10837462; DOI=10.1074/jbc.c000263200;
RA Zhou D., Henion T.R., Jungalwala F.B., Berger E.G., Hennet T.;
RT "The beta1,3-galactosyltransferase beta3GalT-V is a stage-specific
RT embryonic antigen-3 (SSEA-3) synthase.";
RL J. Biol. Chem. 275:22631-22634(2000).
CC -!- FUNCTION: Catalyzes the transfer of Gal to GlcNAc-based acceptors with
CC a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc
CC structure. Can use glycolipid LC3Cer as an efficient acceptor.
CC {ECO:0000269|PubMed:10406968, ECO:0000269|PubMed:10837462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer (d18:1(4E)) + UDP-alpha-D-galactose =
CC globoside GalGb4Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41996,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18259, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62571, ChEBI:CHEBI:66914;
CC Evidence={ECO:0000269|PubMed:10406968, ECO:0000269|PubMed:10837462};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41997;
CC Evidence={ECO:0000269|PubMed:10406968, ECO:0000269|PubMed:10837462};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q9Y2C3; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-14141066, EBI-11749983;
CC Q9Y2C3; P81534: DEFB103B; NbExp=3; IntAct=EBI-14141066, EBI-12074168;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stomach, jejunum, colon, pancreas,
CC small intestine, testis and gastrointestinal and pancreatic cancer cell
CC lines. Hardly detected in lung, liver, adrenal gland and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:10406968}.
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 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_432";
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DR EMBL; AB020337; BAA77664.1; -; mRNA.
DR EMBL; AF145784; AAF07880.1; -; Genomic_DNA.
DR EMBL; AJ006078; CAB91547.1; -; Genomic_DNA.
DR EMBL; AY372061; AAR08910.1; -; mRNA.
DR EMBL; AK292951; BAF85640.1; -; mRNA.
DR EMBL; AL163280; CAB90446.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09629.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09630.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09631.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09632.1; -; Genomic_DNA.
DR EMBL; BC104862; AAI04863.1; -; mRNA.
DR EMBL; BC104864; AAI04865.1; -; mRNA.
DR EMBL; AB041413; BAA94498.1; -; Genomic_DNA.
DR EMBL; AB041416; BAA94501.1; -; Genomic_DNA.
DR CCDS; CCDS13667.1; -.
DR RefSeq; NP_001265579.1; NM_001278650.1.
DR RefSeq; NP_006048.1; NM_006057.2.
DR RefSeq; NP_149360.1; NM_033170.2.
DR RefSeq; NP_149361.1; NM_033171.2.
DR RefSeq; NP_149362.2; NM_033172.2.
DR RefSeq; XP_016883716.1; XM_017028227.1.
DR RefSeq; XP_016883717.1; XM_017028228.1.
DR RefSeq; XP_016883718.1; XM_017028229.1.
DR RefSeq; XP_016883719.1; XM_017028230.1.
DR RefSeq; XP_016883720.1; XM_017028231.1.
DR RefSeq; XP_016883721.1; XM_017028232.1.
DR RefSeq; XP_016883722.1; XM_017028233.1.
DR RefSeq; XP_016883723.1; XM_017028234.1.
DR RefSeq; XP_016883724.1; XM_017028235.1.
DR RefSeq; XP_016883725.1; XM_017028236.1.
DR RefSeq; XP_016883726.1; XM_017028237.1.
DR RefSeq; XP_016883727.1; XM_017028238.1.
DR RefSeq; XP_016883728.1; XM_017028239.1.
DR RefSeq; XP_016883729.1; XM_017028240.1.
DR RefSeq; XP_016883730.1; XM_017028241.1.
DR AlphaFoldDB; Q9Y2C3; -.
DR SMR; Q9Y2C3; -.
DR BioGRID; 115601; 49.
DR IntAct; Q9Y2C3; 2.
DR STRING; 9606.ENSP00000381699; -.
DR ChEMBL; CHEMBL2321635; -.
DR SwissLipids; SLP:000000792; -.
DR SwissLipids; SLP:000000844; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9Y2C3; 3 sites.
DR iPTMnet; Q9Y2C3; -.
DR PhosphoSitePlus; Q9Y2C3; -.
DR BioMuta; B3GALT5; -.
DR DMDM; 13123995; -.
DR EPD; Q9Y2C3; -.
DR jPOST; Q9Y2C3; -.
DR MassIVE; Q9Y2C3; -.
DR PaxDb; Q9Y2C3; -.
DR PeptideAtlas; Q9Y2C3; -.
DR PRIDE; Q9Y2C3; -.
DR ProteomicsDB; 85724; -.
DR Antibodypedia; 23457; 109 antibodies from 24 providers.
DR DNASU; 10317; -.
DR Ensembl; ENST00000343118.6; ENSP00000343318.4; ENSG00000183778.19.
DR Ensembl; ENST00000380618.5; ENSP00000369992.1; ENSG00000183778.19.
DR Ensembl; ENST00000380620.8; ENSP00000369994.3; ENSG00000183778.19.
DR Ensembl; ENST00000398714.4; ENSP00000381699.4; ENSG00000183778.19.
DR Ensembl; ENST00000615480.5; ENSP00000480285.1; ENSG00000183778.19.
DR Ensembl; ENST00000682542.1; ENSP00000507453.1; ENSG00000183778.19.
DR Ensembl; ENST00000683344.1; ENSP00000508165.1; ENSG00000183778.19.
DR Ensembl; ENST00000684187.2; ENSP00000506797.1; ENSG00000183778.19.
DR Ensembl; ENST00000684495.1; ENSP00000507285.1; ENSG00000183778.19.
DR GeneID; 10317; -.
DR KEGG; hsa:10317; -.
DR MANE-Select; ENST00000684187.2; ENSP00000506797.1; NM_001356336.2; NP_001343265.1.
DR UCSC; uc002yyb.3; human.
DR CTD; 10317; -.
DR DisGeNET; 10317; -.
DR GeneCards; B3GALT5; -.
DR HGNC; HGNC:920; B3GALT5.
DR HPA; ENSG00000183778; Tissue enriched (intestine).
DR MIM; 604066; gene.
DR neXtProt; NX_Q9Y2C3; -.
DR OpenTargets; ENSG00000183778; -.
DR PharmGKB; PA25213; -.
DR VEuPathDB; HostDB:ENSG00000183778; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000160964; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q9Y2C3; -.
DR OMA; TCHGIKP; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9Y2C3; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:MON-20081; -.
DR PathwayCommons; Q9Y2C3; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q9Y2C3; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10317; 14 hits in 1063 CRISPR screens.
DR ChiTaRS; B3GALT5; human.
DR GeneWiki; B3GALT5; -.
DR GenomeRNAi; 10317; -.
DR Pharos; Q9Y2C3; Tbio.
DR PRO; PR:Q9Y2C3; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9Y2C3; protein.
DR Bgee; ENSG00000183778; Expressed in palpebral conjunctiva and 103 other tissues.
DR ExpressionAtlas; Q9Y2C3; baseline and differential.
DR Genevisible; Q9Y2C3; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:UniProtKB.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; TAS:ProtInc.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..310
FT /note="Beta-1,3-galactosyltransferase 5"
FT /id="PRO_0000219164"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..310
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 27
FT /note="S -> R (in dbSNP:rs12627708)"
FT /id="VAR_049347"
FT VARIANT 85
FT /note="M -> T (in dbSNP:rs3746887)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.9"
FT /id="VAR_020460"
FT VARIANT 144
FT /note="R -> H (in dbSNP:rs734411)"
FT /id="VAR_033536"
FT CONFLICT 23
FT /note="F -> Y (in Ref. 3; CAB91547)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="Y -> N (in Ref. 3; CAB91547)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..297
FT /note="LDYWQ -> WTTGR (in Ref. 9; BAA94498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 36189 MW; 4DD7A19E3E648AA9 CRC64;
MAFPKMRLMY ICLLVLGALC LYFSMYSLNP FKEQSFVYKK DGNFLKLPDT DCRQTPPFLV
LLVTSSHKQL AERMAIRQTW GKERMVKGKQ LKTFFLLGTT SSAAETKEVD QESQRHGDII
QKDFLDVYYN LTLKTMMGIE WVHRFCPQAA FVMKTDSDMF INVDYLTELL LKKNRTTRFF
TGFLKLNEFP IRQPFSKWFV SKSEYPWDRY PPFCSGTGYV FSGDVASQVY NVSKSVPYIK
LEDVFVGLCL ERLNIRLEEL HSQPTFFPGG LRFSVCLFRR IVACHFIKPR TLLDYWQALE
NSRGEDCPPV
