B3GN4_HUMAN
ID B3GN4_HUMAN Reviewed; 378 AA.
AC Q9C0J1; Q8N5W4; Q8N934; Q8ND21; Q8WWR5; Q8WY02; Q96QH5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4;
DE EC=2.4.1.149 {ECO:0000269|PubMed:11042166};
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4;
DE Short=BGnT-4;
DE Short=Beta-1,3-Gn-T4;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 4;
DE Short=Beta3Gn-T4;
GN Name=B3GNT4; ORFNames=UNQ1898/PRO4344;
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), TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RX PubMed=11042166; DOI=10.1074/jbc.m004800200;
RA Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., Yamada Y.,
RA Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., Sasaki K.;
RT "Identification and characterization of three novel beta 1,3-N-
RT acetylglucosaminyltransferases structurally related to the beta 1,3-
RT galactosyltransferase family.";
RL J. Biol. Chem. 276:3498-3507(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-6.
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-378.
RA Leu J.H., Chou C.M., Huang C.J.;
RT "Cloning and expression of a novel human beta-1,3-galactosyltransferase-
RT related gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-378.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-378.
RA Bennett E.P.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
CC synthesis of poly-N-acetyllactosamine. Has activity for type 2
CC oligosaccharides. {ECO:0000269|PubMed:11042166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:14389,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:134090; EC=2.4.1.149;
CC Evidence={ECO:0000269|PubMed:11042166};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0J1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0J1-2; Sequence=VSP_025962;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain tissues such as whole
CC brain, hippocampus, amygdala, cerebellum and caudate nucleus. Also
CC expressed in colon, esophagus and kidney.
CC {ECO:0000269|PubMed:11042166}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL37219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB049586; BAB21532.1; -; mRNA.
DR EMBL; AY358940; AAQ89299.1; -; mRNA.
DR EMBL; AK095746; BAC04622.1; -; mRNA.
DR EMBL; AL834452; CAD39112.2; -; mRNA.
DR EMBL; BC031399; AAH31399.1; -; mRNA.
DR EMBL; AF321825; AAL37219.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ130848; CAC45045.1; -; mRNA.
DR EMBL; AJ278962; CAC82375.1; -; mRNA.
DR CCDS; CCDS81751.1; -. [Q9C0J1-2]
DR CCDS; CCDS9227.1; -. [Q9C0J1-1]
DR RefSeq; NP_001317421.1; NM_001330492.1. [Q9C0J1-2]
DR RefSeq; NP_110392.1; NM_030765.3. [Q9C0J1-1]
DR AlphaFoldDB; Q9C0J1; -.
DR SMR; Q9C0J1; -.
DR BioGRID; 122657; 7.
DR IntAct; Q9C0J1; 2.
DR STRING; 9606.ENSP00000319636; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9C0J1; 1 site.
DR iPTMnet; Q9C0J1; -.
DR PhosphoSitePlus; Q9C0J1; -.
DR BioMuta; B3GNT4; -.
DR DMDM; 74752494; -.
DR EPD; Q9C0J1; -.
DR MassIVE; Q9C0J1; -.
DR PaxDb; Q9C0J1; -.
DR PeptideAtlas; Q9C0J1; -.
DR PRIDE; Q9C0J1; -.
DR ProteomicsDB; 80060; -. [Q9C0J1-1]
DR ProteomicsDB; 80061; -. [Q9C0J1-2]
DR Antibodypedia; 31630; 88 antibodies from 19 providers.
DR DNASU; 79369; -.
DR Ensembl; ENST00000324189.5; ENSP00000319636.4; ENSG00000176383.9. [Q9C0J1-1]
DR Ensembl; ENST00000535274.1; ENSP00000444534.1; ENSG00000176383.9. [Q9C0J1-2]
DR Ensembl; ENST00000546192.1; ENSP00000438840.1; ENSG00000176383.9. [Q9C0J1-2]
DR GeneID; 79369; -.
DR KEGG; hsa:79369; -.
DR MANE-Select; ENST00000324189.5; ENSP00000319636.4; NM_030765.4; NP_110392.1.
DR UCSC; uc001ubx.4; human. [Q9C0J1-1]
DR CTD; 79369; -.
DR DisGeNET; 79369; -.
DR GeneCards; B3GNT4; -.
DR HGNC; HGNC:15683; B3GNT4.
DR HPA; ENSG00000176383; Tissue enhanced (brain, skin).
DR MIM; 605864; gene.
DR neXtProt; NX_Q9C0J1; -.
DR OpenTargets; ENSG00000176383; -.
DR PharmGKB; PA25220; -.
DR VEuPathDB; HostDB:ENSG00000176383; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000162236; -.
DR HOGENOM; CLU_036849_5_3_1; -.
DR InParanoid; Q9C0J1; -.
DR OMA; WDFAEDF; -.
DR PhylomeDB; Q9C0J1; -.
DR TreeFam; TF318639; -.
DR PathwayCommons; Q9C0J1; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9C0J1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79369; 24 hits in 1078 CRISPR screens.
DR ChiTaRS; B3GNT4; human.
DR GenomeRNAi; 79369; -.
DR Pharos; Q9C0J1; Tbio.
DR PRO; PR:Q9C0J1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9C0J1; protein.
DR Bgee; ENSG00000176383; Expressed in oocyte and 144 other tissues.
DR ExpressionAtlas; Q9C0J1; baseline and differential.
DR Genevisible; Q9C0J1; 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:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..378
FT /note="N-acetyllactosaminide beta-1,3-N-
FT acetylglucosaminyltransferase 4"
FT /id="PRO_0000289207"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 59..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025962"
FT VARIANT 6
FT /note="P -> A (in dbSNP:rs7136356)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032600"
FT VARIANT 83
FT /note="S -> T (in dbSNP:rs1001178)"
FT /id="VAR_032601"
FT VARIANT 87
FT /note="L -> P (in dbSNP:rs35203505)"
FT /id="VAR_032602"
FT CONFLICT 49
FT /note="L -> V (in Ref. 6; CAC45045 and 7; CAC82375)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="A -> T (in Ref. 6; CAC45045 and 7; CAC82375)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> S (in Ref. 6; CAC45045)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="R -> Q (in Ref. 3; BAC04622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42310 MW; E8EE88665A36057E CRC64;
MLPPQPSAAH QGRGGRSGLL PKGPAMLCRL CWLVSYSLAV LLLGCLLFLR KAAKPAGDPT
AHQPFWAPPT PRHSRCPPNH TVSSASLSLP SRHRLFLTYR HCRNFSILLE PSGCSKDTFL
LLAIKSQPGH VERRAAIRST WGRVGGWARG RQLKLVFLLG VAGSAPPAQL LAYESREFDD
ILQWDFTEDF FNLTLKELHL QRWVVAACPQ AHFMLKGDDD VFVHVPNVLE FLDGWDPAQD
LLVGDVIRQA LPNRNTKVKY FIPPSMYRAT HYPPYAGGGG YVMSRATVRR LQAIMEDAEL
FPIDDVFVGM CLRRLGLSPM HHAGFKTFGI RRPLDPLDPC LYRGLLLVHR LSPLEMWTMW
ALVTDEGLKC AAGPIPQR
