B4GT4_HUMAN
ID B4GT4_HUMAN Reviewed; 344 AA.
AC O60513; Q68D68; Q9BSW3; Q9C078;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Beta-1,4-galactosyltransferase 4 {ECO:0000305};
DE Short=Beta-1,4-GalTase 4;
DE Short=Beta4Gal-T4;
DE Short=b4Gal-T4;
DE EC=2.4.1.- {ECO:0000269|PubMed:12511560, ECO:0000269|PubMed:9792633};
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Lactotriaosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.275 {ECO:0000269|PubMed:9792633};
DE AltName: Full=N-acetyllactosamine synthase;
DE EC=2.4.1.90 {ECO:0000269|PubMed:9792633};
DE AltName: Full=Nal synthase;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4;
GN Name=B4GALT4 {ECO:0000303|PubMed:17690104, ECO:0000312|HGNC:HGNC:927};
GN ORFNames=UNQ552/PRO1109;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=9792633; DOI=10.1074/jbc.273.45.29331;
RA Schwientek T., Almeida R., Levery S.B., Holmes E.H., Bennett E.,
RA Clausen H.;
RT "Cloning of a novel member of the UDP-galactose:beta-N-acetylglucosamine
RT beta1,4-galactosyltransferase family, beta4Gal-T4, involved in
RT glycosphingolipid biosynthesis.";
RL J. Biol. Chem. 273:29331-29340(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [MRNA], AND VARIANT GLU-116.
RA Fan Y., Yu L., Zhang Q., Jiang Y., Dai F., Chen C., Tu Q., Bi A., Xu Y.,
RA Zhao S.;
RT "Cloning and characterization of a novel member of the human beta-1,4-
RT galactosyltransferase gene family.";
RL Sci. China, Ser. C, Life Sci. 42:337-345(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-116.
RC TISSUE=Fetal kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-116.
RC TISSUE=Colon, and Muscle;
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).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12511560; DOI=10.1074/jbc.m211480200;
RA Seko A., Dohmae N., Takio K., Yamashita K.;
RT "Beta 1,4-galactosyltransferase (beta 4GalT)-IV is specific for GlcNAc 6-O-
RT sulfate. Beta 4GalT-IV acts on keratan sulfate-related glycans and a
RT precursor glycan of 6-sulfosialyl-Lewis X.";
RL J. Biol. Chem. 278:9150-9158(2003).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17690104; DOI=10.1074/jbc.m703695200;
RA Kitayama K., Hayashida Y., Nishida K., Akama T.O.;
RT "Enzymes responsible for synthesis of corneal keratan sulfate
RT glycosaminoglycans.";
RL J. Biol. Chem. 282:30085-30096(2007).
RN [11]
RP FUNCTION, GLYCOSYLATION AT ASN-220 AND ASN-335, MUTAGENESIS OF THR-6;
RP THR-222 AND THR-337, SUBCELLULAR LOCATION, AND INTERACTION WITH SLC35A2.
RX PubMed=32827291; DOI=10.1007/s10719-020-09941-z;
RA Shauchuk A., Szulc B., Maszczak-Seneczko D., Wiertelak W., Skurska E.,
RA Olczak M.;
RT "N-glycosylation of the human beta1,4-galactosyltransferase 4 is crucial
RT for its activity and Golgi localization.";
RL Glycoconj. J. 37:577-588(2020).
CC -!- FUNCTION: Galactose (Gal) transferase involved in the synthesis of
CC terminal N-acetyllactosamine (LacNac) unit present on glycan chains of
CC glycoproteins and glycosphingolipids (PubMed:9792633, PubMed:17690104,
CC PubMed:12511560, PubMed:32827291). Catalyzes the transfer of Gal
CC residue via a beta1->4 linkage from UDP-Gal to the non-reducing
CC terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the
CC linearly growing chain of both N- and O-linked keratan sulfate
CC proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase
CC and CHST6 and CHST1 sulfotransferases to construct and elongate
CC mono- and disulfated disaccharide units [->3Galbeta1->4(6-
CC sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-
CC sulfoGlcNAcbeta)1->] within keratan sulfate polymer (PubMed:17690104).
CC Transfers Gal residue via a beta1->4 linkage to terminal 6-O-
CC sulfoGlcNAc within the LacNac unit of core 2 O-glycans forming 6-sulfo-
CC sialyl-Lewis X (sLex). May contribute to the generation of sLex epitope
CC on mucin-type glycoproteins that serve as ligands for SELL/L-selectin,
CC a major regulator of leukocyte migration (PubMed:12511560). In the
CC biosynthesis pathway of neolacto-series glycosphingolipids, transfers
CC Gal residue via a beta1->4 linkage to terminal GlcNAc of a
CC lactotriaosylceramide (Lc3Cer) acceptor to form a
CC neolactotetraosylceramide (PubMed:9792633).
CC {ECO:0000269|PubMed:12511560, ECO:0000269|PubMed:17690104,
CC ECO:0000269|PubMed:9792633}.
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:9792633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000269|PubMed:9792633};
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:9792633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000269|PubMed:9792633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-
CC [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:67948, Rhea:RHEA-COMP:17367, Rhea:RHEA-
CC COMP:17398, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:176494, ChEBI:CHEBI:176635;
CC Evidence={ECO:0000305|PubMed:12511560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67949;
CC Evidence={ECO:0000305|PubMed:12511560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+)
CC + UDP; Xref=Rhea:RHEA:67872, Rhea:RHEA-COMP:17370, Rhea:RHEA-
CC COMP:17397, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:176493, ChEBI:CHEBI:176634;
CC Evidence={ECO:0000305|PubMed:12511560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67873;
CC Evidence={ECO:0000305|PubMed:12511560};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Up-regulated by LALBA.
CC {ECO:0000269|PubMed:9792633}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.031 mM for UDP-Gal {ECO:0000269|PubMed:9792633};
CC KM=238 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157};
CC KM=0.43 mM for SO3->6GlcNAc (6SGN) {ECO:0000269|PubMed:12511560};
CC KM=330 mM for GlcNAc {ECO:0000269|PubMed:12511560};
CC KM=0.11 mM for SO3
CC ->6GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(
CC Fucalpha1->6)GlcNAc (6S-biGP) {ECO:0000269|PubMed:12511560};
CC KM=7.7 mM for
CC GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fuc
CC alpha1->6)GlcNAc (biGP) {ECO:0000269|PubMed:12511560};
CC KM=0.091 mM for SO3->6GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP
CC (6S-core2-O-pNP) {ECO:0000269|PubMed:12511560};
CC KM=0.50 mM for GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (core2-
CC O-pNP) {ECO:0000269|PubMed:12511560};
CC KM=0.38 mM for SO3->6GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (agL2L2)
CC {ECO:0000269|PubMed:12511560};
CC KM=0.63 mM for SO3->6GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc
CC (agL2L4) {ECO:0000269|PubMed:12511560};
CC Vmax=3.6 nmol/min/mg enzyme toward SO3->6GlcNAc (6SGN)
CC {ECO:0000269|PubMed:12511560};
CC Vmax=1.5 nmol/min/mg enzyme toward GlcNAc
CC {ECO:0000269|PubMed:12511560};
CC Vmax=3.2 nmol/min/mg enzyme toward
CC 6GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fu
CC calpha1->6)GlcNAc (6S-biGP) {ECO:0000269|PubMed:12511560};
CC Vmax=0.42 nmol/min/mg enzyme toward
CC GlcNAcbeta1->2Manalpha1->3(Manalpha1->6)Manbeta1->4GlcNAcbeta1->4(Fuc
CC alpha1->6)GlcNAc (biGP) {ECO:0000269|PubMed:12511560};
CC Vmax=4.8 nmol/min/mg enzyme toward
CC SO3->6GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (6S-core2-O-pNP)
CC {ECO:0000269|PubMed:12511560};
CC Vmax=1.2 nmol/min/mg enzyme toward
CC GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP (core2-O-pNP)
CC {ECO:0000269|PubMed:12511560};
CC Vmax=7.8 nmol/min/mg enzyme toward
CC SO3->6GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (agL2L2)
CC {ECO:0000269|PubMed:12511560};
CC Vmax=7.8 nmol/min/mg enzyme toward
CC SO3->6GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc (agL2L4)
CC {ECO:0000269|PubMed:12511560};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:12511560}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:9792633}.
CC -!- SUBUNIT: Interacts with SLC35A2 (isoform 2; UGT1).
CC {ECO:0000269|PubMed:32827291}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:32827291}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000269|PubMed:32827291}.
CC -!- TISSUE SPECIFICITY: Highest expression is observed in placenta,
CC pancreas, kidney and heart (PubMed:9792633). Expressed in corneal
CC epithelial cells (PubMed:17690104). {ECO:0000269|PubMed:17690104,
CC ECO:0000269|PubMed:9792633}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:32827291}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4-
CC galactosyltransferase 4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_439";
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DR EMBL; AF038662; AAC39735.1; -; mRNA.
DR EMBL; AF022367; AAC72493.1; -; mRNA.
DR EMBL; AB024436; BAA75821.1; -; mRNA.
DR EMBL; AF020920; AAG50147.1; -; mRNA.
DR EMBL; AY359008; AAQ89367.1; -; mRNA.
DR EMBL; CR749555; CAH18352.1; -; mRNA.
DR EMBL; BC004523; AAH04523.1; -; mRNA.
DR EMBL; BC062618; AAH62618.1; -; mRNA.
DR CCDS; CCDS2986.1; -.
DR RefSeq; NP_003769.1; NM_003778.3.
DR RefSeq; NP_997708.1; NM_212543.1.
DR RefSeq; XP_005247912.1; XM_005247855.1.
DR RefSeq; XP_006713861.1; XM_006713798.2.
DR RefSeq; XP_006713862.1; XM_006713799.2.
DR RefSeq; XP_006713863.1; XM_006713800.1.
DR RefSeq; XP_006713864.1; XM_006713801.2.
DR RefSeq; XP_011511562.1; XM_011513260.1.
DR AlphaFoldDB; O60513; -.
DR SMR; O60513; -.
DR BioGRID; 114245; 41.
DR IntAct; O60513; 10.
DR STRING; 9606.ENSP00000420161; -.
DR DrugBank; DB00141; N-Acetylglucosamine.
DR SwissLipids; SLP:000000791; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; O60513; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O60513; -.
DR PhosphoSitePlus; O60513; -.
DR BioMuta; B4GALT4; -.
DR EPD; O60513; -.
DR jPOST; O60513; -.
DR MassIVE; O60513; -.
DR MaxQB; O60513; -.
DR PaxDb; O60513; -.
DR PeptideAtlas; O60513; -.
DR PRIDE; O60513; -.
DR ProteomicsDB; 49453; -.
DR Antibodypedia; 32692; 213 antibodies from 27 providers.
DR DNASU; 8702; -.
DR Ensembl; ENST00000359213.7; ENSP00000352144.3; ENSG00000121578.13.
DR Ensembl; ENST00000393765.7; ENSP00000377360.2; ENSG00000121578.13.
DR Ensembl; ENST00000483209.5; ENSP00000420161.1; ENSG00000121578.13.
DR GeneID; 8702; -.
DR KEGG; hsa:8702; -.
DR MANE-Select; ENST00000393765.7; ENSP00000377360.2; NM_003778.4; NP_003769.1.
DR UCSC; uc003ecg.4; human.
DR CTD; 8702; -.
DR DisGeNET; 8702; -.
DR GeneCards; B4GALT4; -.
DR HGNC; HGNC:927; B4GALT4.
DR HPA; ENSG00000121578; Tissue enhanced (epididymis).
DR MIM; 604015; gene.
DR neXtProt; NX_O60513; -.
DR OpenTargets; ENSG00000121578; -.
DR PharmGKB; PA25226; -.
DR VEuPathDB; HostDB:ENSG00000121578; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158378; -.
DR InParanoid; O60513; -.
DR OMA; CDNQPKH; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; O60513; -.
DR TreeFam; TF312834; -.
DR BioCyc; MetaCyc:HS04504-MON; -.
DR BRENDA; 2.4.1.275; 2681.
DR PathwayCommons; O60513; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; O60513; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8702; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; B4GALT4; human.
DR GeneWiki; B4GALT4; -.
DR GenomeRNAi; 8702; -.
DR Pharos; O60513; Tbio.
DR PRO; PR:O60513; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O60513; protein.
DR Bgee; ENSG00000121578; Expressed in tendon of biceps brachii and 203 other tissues.
DR ExpressionAtlas; O60513; baseline and differential.
DR Genevisible; O60513; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; IDA:UniProtKB.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001572; P:lactosylceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006643; P:membrane lipid metabolic process; TAS:ProtInc.
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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Beta-1,4-galactosyltransferase 4"
FT /id="PRO_0000080542"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..344
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 129..133
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 168..170
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 258..261
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 289..291
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32827291"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32827291"
FT DISULFID 77..118
FT /evidence="ECO:0000250"
FT DISULFID 189..208
FT /evidence="ECO:0000250"
FT VARIANT 116
FT /note="Q -> E (in dbSNP:rs3764779)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4"
FT /id="VAR_022697"
FT MUTAGEN 6
FT /note="T->A: Has no impact on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:32827291"
FT MUTAGEN 222
FT /note="T->A: Has no impact on localization to the Golgi
FT apparatus. Decreases N-glycosylation. Impairs the catalytic
FT activity. Impairs keratan sulfate biosynthesis; when
FT associated with A-337."
FT /evidence="ECO:0000269|PubMed:32827291"
FT MUTAGEN 337
FT /note="T->A: Impairs localization to the Golgi apparatus.
FT Abolishes N-glycosylation. Impairs the interaction with
FT SLC35A/UGT1. Impairs the catalytic activity. Impairs
FT keratan sulfate biosynthesis; when associated with A-222."
FT /evidence="ECO:0000269|PubMed:32827291"
FT CONFLICT 182
FT /note="L -> R (in Ref. 4; AAG50147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 40041 MW; 6B7742676FE8A58B CRC64;
MGFNLTFHLS YKFRLLLLLT LCLTVVGWAT SNYFVGAIQE IPKAKEFMAN FHKTLILGKG
KTLTNEASTK KVELDNCPSV SPYLRGQSKL IFKPDLTLEE VQAENPKVSR GRYRPQECKA
LQRVAILVPH RNREKHLMYL LEHLHPFLQR QQLDYGIYVI HQAEGKKFNR AKLLNVGYLE
ALKEENWDCF IFHDVDLVPE NDFNLYKCEE HPKHLVVGRN STGYRLRYSG YFGGVTALSR
EQFFKVNGFS NNYWGWGGED DDLRLRVELQ RMKISRPLPE VGKYTMVFHT RDKGNEVNAE
RMKLLHQVSR VWRTDGLSSC SYKLVSVEHN PLYINITVDF WFGA
