A4GAT_HUMAN
ID A4GAT_HUMAN Reviewed; 353 AA.
AC Q9NPC4; B2R7C4; Q9P1X5;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Lactosylceramide 4-alpha-galactosyltransferase;
DE EC=2.4.1.228 {ECO:0000269|PubMed:10748143};
DE AltName: Full=Alpha-1,4-N-acetylglucosaminyltransferase;
DE AltName: Full=Alpha-1,4-galactosyltransferase;
DE AltName: Full=Alpha4Gal-T1;
DE AltName: Full=CD77 synthase;
DE AltName: Full=Globotriaosylceramide synthase;
DE Short=Gb3 synthase;
DE AltName: Full=P1/Pk synthase;
DE AltName: Full=UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase;
GN Name=A4GALT; Synonyms=A14GALT, A4GALT1;
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, FUNCTION (MICROBIAL INFECTION),
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC TISSUE=Melanoma;
RX PubMed=10748143; DOI=10.1074/jbc.m909620199;
RA Kojima Y., Fukumoto S., Furukawa K., Okajima T., Wiels J., Yokoyama K.,
RA Suzuki Y., Urano T., Ohta M., Furukawa K.;
RT "Molecular cloning of globotriaosylceramide/CD77 synthase, a
RT glycosyltransferase that initiates the synthesis of globo series
RT glycosphingolipids.";
RL J. Biol. Chem. 275:15152-15156(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS VAL-37 AND LYS-183.
RX PubMed=10747952; DOI=10.1074/jbc.m000728200;
RA Steffensen R., Carlier K., Wiels J., Levery S.B., Stroud M., Cedergren B.,
RA Nilsson Sojka B., Bennett E.P., Jersild C., Clausen H.;
RT "Cloning and expression of the histo-blood group Pk UDP-galactose:Galbeta1-
RT 4Glcbeta1-Cer alpha1,4-galactosyltransferase. Molecular genetic basis of
RT the p phenotype.";
RL J. Biol. Chem. 275:16723-16729(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-37 AND ARG-163.
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 VARIANTS VAL-37; LYS-183; ASP-187 AND LEU-251, AND POLYMORPHISM.
RX PubMed=10993874; DOI=10.1074/jbc.c000625200;
RA Furukawa K., Iwamura K., Uchikawa M., Sojka B.N., Wiels J., Okajima T.,
RA Urano T., Furukawa K.;
RT "Molecular basis for the p phenotype. Identification of distinct and
RT multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish
RT and Japanese individuals.";
RL J. Biol. Chem. 275:37752-37756(2000).
RN [10]
RP VARIANT PHE-80 DEL, AND POLYMORPHISM.
RX PubMed=11896312; DOI=10.1046/j.1537-2995.2002.00014.x;
RA Koda Y., Soejima M., Sato H., Maeda Y., Kimura H.;
RT "Three-base deletion and one-base insertion of the
RT alpha(1,4)galactosyltransferase gene responsible for the P phenotype.";
RL Transfusion 42:48-51(2002).
RN [11]
RP VARIANT GLU-211, AND POLYMORPHISM.
RX PubMed=22965229; DOI=10.1074/jbc.m112.408286;
RA Suchanowska A., Kaczmarek R., Duk M., Lukasiewicz J., Smolarek D.,
RA Majorczyk E., Jaskiewicz E., Laskowska A., Wasniowska K., Grodecka M.,
RA Lisowska E., Czerwinski M.;
RT "A single point mutation in the gene encoding Gb3/CD77 synthase causes a
RT rare inherited polyagglutination syndrome.";
RL J. Biol. Chem. 287:38220-38230(2012).
CC -!- FUNCTION: Catalyzes the transfer of galactose from UDP-alpha-D-
CC galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside
CC Gb3Cer (d18:1(4E)) (PubMed:10748143). Also able to transfer galactose
CC to galactosylceramide/beta-D-Gal-(1<->1')-Cer (PubMed:10748143).
CC Globoside Gb3Cer is a glycosphingolipid of the globo serie, one of the
CC major types of neutral root structures of glycosphingolipids, that
CC constitute a significant portion of mammalian cell membranes
CC (Probable). Globotriaosylceramide/globoside Gb3Cer in blood and tissue
CC cell membranes is the antigen Pk of blood histogroup P
CC (PubMed:10747952). {ECO:0000269|PubMed:10747952,
CC ECO:0000269|PubMed:10748143, ECO:0000305|PubMed:10748143}.
CC -!- FUNCTION: (Microbial infection) Globotriaosylceramide is one of the
CC cellular ligands for bacterial verotoxins.
CC {ECO:0000269|PubMed:10748143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-
CC alpha-D-galactose = globoside Gb3Cer (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:11924, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC EC=2.4.1.228; Evidence={ECO:0000269|PubMed:10748143};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11925;
CC Evidence={ECO:0000305|PubMed:10748143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Gal-(1<->1')-Cer + UDP-alpha-D-galactose = alpha-D-Gal-
CC (1->4)-beta-D-Gal-(1<->1')-Cer + H(+) + UDP; Xref=Rhea:RHEA:60044,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:143593, ChEBI:CHEBI:143594;
CC Evidence={ECO:0000269|PubMed:10748143};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60045;
CC Evidence={ECO:0000305|PubMed:10748143};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54.5 uM for beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
CC ceramide(d18:1(4E)) {ECO:0000269|PubMed:10748143};
CC KM=132 uM for beta-D-Gal-(1<->1')-Cer {ECO:0000269|PubMed:10748143};
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:10748143}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, heart,
CC spleen, liver, testis and placenta.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250}.
CC -!- POLYMORPHISM: Genetic variation in A4GALT is responsible for the P1PK
CC system blood group phenotypes [MIM:111400]. Different combinations or
CC absence of the P blood group system antigens define 5 different
CC phenotypes: P1, P2, P1(k), P2(k), and p. Genetic variation in A4GALT
CC determines the p phenotype, which is rare and does not express any
CC antigens. It is also known as null phenotype; p individuals have
CC antibodies against P, P1 and Pk antigens in their sera. These
CC antibodies are clinically important because they can cause severe
CC transfusion reactions and miscarriage (PubMed:10993874,
CC PubMed:11896312). Genetic variation in A4GALT is also responsible for
CC the NOR polyagglutination syndrome [MIM:111400]. Polyagglutination is
CC the occurrence of red cell agglutination by virtually all human sera,
CC but not by autologous serum or sera from newborns, creating a risk of
CC complications during transfusions of NOR erythrocytes. It is caused by
CC the unusual Gal(alpha1-4)GalNAc glycolipid epitope (PubMed:22965229).
CC {ECO:0000269|PubMed:10993874, ECO:0000269|PubMed:11896312,
CC ECO:0000269|PubMed:22965229}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/a4galt/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Lactosylceramide 4-alpha-galactosyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_428";
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DR EMBL; AB037883; BAA95915.1; -; mRNA.
DR EMBL; AJ245581; CAB93532.1; -; mRNA.
DR EMBL; AB041418; BAA94503.1; -; Genomic_DNA.
DR EMBL; AY941797; AAX20109.1; -; Genomic_DNA.
DR EMBL; AK312927; BAG35771.1; -; mRNA.
DR EMBL; Z82176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73274.1; -; Genomic_DNA.
DR EMBL; BC017068; AAH17068.1; -; mRNA.
DR CCDS; CCDS14041.1; -.
DR RefSeq; NP_001304967.1; NM_001318038.1.
DR RefSeq; NP_059132.1; NM_017436.5.
DR RefSeq; XP_005261701.1; XM_005261644.2.
DR RefSeq; XP_005261703.1; XM_005261646.4.
DR RefSeq; XP_005261704.1; XM_005261647.2.
DR RefSeq; XP_005261705.1; XM_005261648.3.
DR RefSeq; XP_006724328.1; XM_006724265.3.
DR RefSeq; XP_006724329.1; XM_006724266.3.
DR RefSeq; XP_011528535.1; XM_011530233.2.
DR RefSeq; XP_016884320.1; XM_017028831.1.
DR AlphaFoldDB; Q9NPC4; -.
DR BioGRID; 119825; 13.
DR IntAct; Q9NPC4; 6.
DR MINT; Q9NPC4; -.
DR STRING; 9606.ENSP00000384794; -.
DR SwissLipids; SLP:000000760; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR GlyGen; Q9NPC4; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NPC4; -.
DR PhosphoSitePlus; Q9NPC4; -.
DR BioMuta; A4GALT; -.
DR DMDM; 25452796; -.
DR EPD; Q9NPC4; -.
DR jPOST; Q9NPC4; -.
DR MassIVE; Q9NPC4; -.
DR PaxDb; Q9NPC4; -.
DR PeptideAtlas; Q9NPC4; -.
DR PRIDE; Q9NPC4; -.
DR ProteomicsDB; 81966; -.
DR Antibodypedia; 239; 235 antibodies from 30 providers.
DR DNASU; 53947; -.
DR Ensembl; ENST00000249005.3; ENSP00000249005.2; ENSG00000128274.17.
DR Ensembl; ENST00000381278.4; ENSP00000370678.3; ENSG00000128274.17.
DR Ensembl; ENST00000401850.5; ENSP00000384794.1; ENSG00000128274.17.
DR Ensembl; ENST00000642412.2; ENSP00000494127.1; ENSG00000128274.17.
DR GeneID; 53947; -.
DR KEGG; hsa:53947; -.
DR MANE-Select; ENST00000642412.2; ENSP00000494127.1; NM_017436.7; NP_059132.1.
DR UCSC; uc062ewk.1; human.
DR CTD; 53947; -.
DR DisGeNET; 53947; -.
DR GeneCards; A4GALT; -.
DR HGNC; HGNC:18149; A4GALT.
DR HPA; ENSG00000128274; Low tissue specificity.
DR MalaCards; A4GALT; -.
DR MIM; 111400; phenotype.
DR MIM; 607922; gene.
DR neXtProt; NX_Q9NPC4; -.
DR OpenTargets; ENSG00000128274; -.
DR PharmGKB; PA24359; -.
DR VEuPathDB; HostDB:ENSG00000128274; -.
DR eggNOG; KOG1928; Eukaryota.
DR GeneTree; ENSGT00510000047981; -.
DR HOGENOM; CLU_049512_2_0_1; -.
DR InParanoid; Q9NPC4; -.
DR OMA; AFYPIRW; -.
DR OrthoDB; 1082380at2759; -.
DR PhylomeDB; Q9NPC4; -.
DR TreeFam; TF324053; -.
DR BioCyc; MetaCyc:HS05171-MON; -.
DR BRENDA; 2.4.1.228; 2681.
DR PathwayCommons; Q9NPC4; -.
DR SignaLink; Q9NPC4; -.
DR BioGRID-ORCS; 53947; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; A4GALT; human.
DR GeneWiki; A4GALT; -.
DR GenomeRNAi; 53947; -.
DR Pharos; Q9NPC4; Tbio.
DR PRO; PR:Q9NPC4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NPC4; protein.
DR Bgee; ENSG00000128274; Expressed in apex of heart and 123 other tissues.
DR ExpressionAtlas; Q9NPC4; baseline and differential.
DR Genevisible; Q9NPC4; HS.
DR GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0050512; F:lactosylceramide 4-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl.
DR GO; GO:0001576; P:globoside biosynthetic process; IEA:Ensembl.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IDA:MGI.
DR InterPro; IPR007652; A1-4-GlycosylTfrase_dom.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF04572; Gb3_synth; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="Lactosylceramide 4-alpha-galactosyltransferase"
FT /id="PRO_0000080578"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..353
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 192..194
FT /note="DXD motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 37
FT /note="M -> V (in dbSNP:rs11541159)"
FT /evidence="ECO:0000269|PubMed:10747952,
FT ECO:0000269|PubMed:10993874, ECO:0000269|Ref.4"
FT /id="VAR_014296"
FT VARIANT 80
FT /note="Missing (in p individuals)"
FT /evidence="ECO:0000269|PubMed:11896312"
FT /id="VAR_017507"
FT VARIANT 163
FT /note="Q -> R (in dbSNP:rs28915383)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022320"
FT VARIANT 183
FT /note="M -> K (in p individuals; complete loss of activity;
FT dbSNP:rs74315453)"
FT /evidence="ECO:0000269|PubMed:10747952,
FT ECO:0000269|PubMed:10993874"
FT /id="VAR_014297"
FT VARIANT 187
FT /note="G -> D (in p individuals; partial loss of activity;
FT dbSNP:rs28940572)"
FT /evidence="ECO:0000269|PubMed:10993874"
FT /id="VAR_017508"
FT VARIANT 211
FT /note="Q -> E (in individuals with NOR polyagglutination
FT syndrome; causes the synthesis of both Gal(alpha1-4)Gal and
FT Gal(alpha1-4)GalNAc moieties; dbSNP:rs397514502)"
FT /evidence="ECO:0000269|PubMed:22965229"
FT /id="VAR_080910"
FT VARIANT 251
FT /note="P -> L (in p individuals; complete loss of activity;
FT dbSNP:rs28940571)"
FT /evidence="ECO:0000269|PubMed:10993874"
FT /id="VAR_017509"
SQ SEQUENCE 353 AA; 40499 MW; 8755865BDA5DA205 CRC64;
MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG QLYNLPAEIP
CPTLTPPTPP SHGPTPGNIF FLETSDRTNP NFLFMCSVES AARTHPESHV LVLMKGLPGG
NASLPRHLGI SLLSCFPNVQ MLPLDLRELF RDTPLADWYA AVQGRWEPYL LPVLSDASRI
ALMWKFGGIY LDTDFIVLKN LRNLTNVLGT QSRYVLNGAF LAFERRHEFM ALCMRDFVDH
YNGWIWGHQG PQLLTRVFKK WCSIRSLAES RACRGVTTLP PEAFYPIPWQ DWKKYFEDIN
PEELPRLLSA TYAVHVWNKK SQGTRFEATS RALLAQLHAR YCPTTHEAMK MYL
