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   27-MAR-2024, entry version 200.
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 mono-
CC       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=0.5 mM for GlcNAcbeta1->6(Galbeta1->3)GalNAcalpha1-O-pNP
CC         (core2-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;
CC       Note=Beta-1,4-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; 44.
DR   IntAct; O60513; 10.
DR   STRING; 9606.ENSP00000420161; -.
DR   DrugBank; DB00141; N-Acetylglucosamine.
DR   SwissLipids; SLP:000000791; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyCosmos; O60513; 3 sites, 1 glycan.
DR   GlyGen; O60513; 4 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; O60513; -.
DR   PhosphoSitePlus; O60513; -.
DR   BioMuta; B4GALT4; -.
DR   EPD; O60513; -.
DR   jPOST; O60513; -.
DR   MassIVE; O60513; -.
DR   MaxQB; O60513; -.
DR   PaxDb; 9606-ENSP00000420161; -.
DR   PeptideAtlas; O60513; -.
DR   ProteomicsDB; 49453; -.
DR   Pumba; O60513; -.
DR   Antibodypedia; 32692; 228 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   AGR; HGNC:927; -.
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; QVWRKDG; -.
DR   OrthoDB; 306273at2759; -.
DR   PhylomeDB; O60513; -.
DR   TreeFam; TF312834; -.
DR   BioCyc; MetaCyc:HS04504-MONOMER; -.
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; 11 hits in 1153 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 205 other cell types or tissues.
DR   ExpressionAtlas; O60513; baseline and differential.
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:0016020; C: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   CDD; cd00899; b4GalT; 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; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF9; BETA-1,4-GALACTOSYLTRANSFERASE 4; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; O60513; HS.
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
//