C1GLT_HUMAN
ID C1GLT_HUMAN Reviewed; 363 AA.
AC Q9NS00; Q96QH4; Q9BTU1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE EC=2.4.1.122 {ECO:0000269|PubMed:11677243};
DE AltName: Full=B3Gal-T8;
DE AltName: Full=Core 1 O-glycan T-synthase;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1;
DE Short=Beta-1,3-galactosyltransferase;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1;
DE Short=C1GalT1;
DE Short=Core 1 beta3-Gal-T1;
GN Name=C1GALT1;
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), ENZYME ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11677243; DOI=10.1074/jbc.m109060200;
RA Ju T., Brewer K., D'Souza A., Cummings R.D., Canfield W.M.;
RT "Cloning and expression of human core 1 beta1,3-galactosyltransferase.";
RL J. Biol. Chem. 277:178-186(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Jensen M.P.A.;
RT "Cloning and expression of a novel beta-1,3-galactosyltransferase.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-363 (ISOFORM 1).
RC TISSUE=Kidney;
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 INTERACTION WITH C1GALT1C1.
RX PubMed=12464682; DOI=10.1073/pnas.262438199;
RA Ju T., Cummings R.D.;
RT "A unique molecular chaperone Cosmc required for activity of the mammalian
RT core 1 beta 3-galactosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16613-16618(2002).
RN [7]
RP INVOLVEMENT IN IGA NEPHROPATHY.
RX PubMed=17228361; DOI=10.1038/sj.ki.5002088;
RA Li G.-S., Zhang H., Lv J.-C., Shen Y., Wang H.-Y.;
RT "Variants of C1GALT1 gene are associated with the genetic susceptibility to
RT IgA nephropathy.";
RL Kidney Int. 71:448-453(2007).
RN [8]
RP INVOLVEMENT IN IGA NEPHROPATHY.
RX PubMed=19357720; DOI=10.1038/ki.2009.99;
RA Zhu L., Tang W., Li G., Lv J., Ding J., Yu L., Zhao M., Li Y., Zhang X.,
RA Shen Y., Zhang H., Wang H.;
RT "Interaction between variants of two glycosyltransferase genes in IgA
RT nephropathy.";
RL Kidney Int. 76:190-198(2009).
CC -!- FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-
CC beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many
CC extended O-glycans in glycoproteins. Plays a central role in many
CC processes, such as angiogenesis, thrombopoiesis and kidney homeostasis
CC development.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000269|PubMed:11677243};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC the C1GALT1C1 chaperone; required for galactosyltransferase activity.
CC {ECO:0000250, ECO:0000269|PubMed:12464682}.
CC -!- INTERACTION:
CC Q9NS00; Q96EU7: C1GALT1C1; NbExp=4; IntAct=EBI-8628584, EBI-2837343;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NS00-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NS00-2; Sequence=VSP_024809;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney,
CC heart, placenta and liver. {ECO:0000269|PubMed:11677243}.
CC -!- MISCELLANEOUS: Aberrant O-galactosylation of IgA1 molecules plays a
CC role in the development and progression of IgA nephropathy (IgAN).
CC Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1
CC O-glycosylation, disease predisposition, and disease severity, and may
CC contribute to the polygenic nature of IgAN.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Core1
CC UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-
CC galactosyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_447";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF155582; AAF81981.1; -; mRNA.
DR EMBL; AJ132443; CAC45046.1; -; mRNA.
DR EMBL; AJ278960; CAC82373.1; -; mRNA.
DR EMBL; AJ243256; CAC80435.1; -; mRNA.
DR EMBL; AC005532; AAQ96887.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24308.1; -; Genomic_DNA.
DR EMBL; BC003174; AAH03174.1; -; mRNA.
DR CCDS; CCDS5355.1; -. [Q9NS00-1]
DR RefSeq; NP_064541.1; NM_020156.4. [Q9NS00-1]
DR RefSeq; XP_011513755.1; XM_011515453.2. [Q9NS00-1]
DR RefSeq; XP_011513757.1; XM_011515455.2. [Q9NS00-1]
DR RefSeq; XP_011513758.1; XM_011515456.2. [Q9NS00-1]
DR RefSeq; XP_016867931.1; XM_017012442.1. [Q9NS00-1]
DR RefSeq; XP_016867932.1; XM_017012443.1.
DR RefSeq; XP_016867933.1; XM_017012444.1. [Q9NS00-1]
DR RefSeq; XP_016867934.1; XM_017012445.1. [Q9NS00-1]
DR RefSeq; XP_016867935.1; XM_017012446.1. [Q9NS00-1]
DR RefSeq; XP_016867936.1; XM_017012447.1. [Q9NS00-1]
DR RefSeq; XP_016867937.1; XM_017012448.1. [Q9NS00-1]
DR AlphaFoldDB; Q9NS00; -.
DR SMR; Q9NS00; -.
DR BioGRID; 121241; 47.
DR IntAct; Q9NS00; 7.
DR MINT; Q9NS00; -.
DR STRING; 9606.ENSP00000389176; -.
DR ChEMBL; CHEMBL2321633; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q9NS00; -.
DR PhosphoSitePlus; Q9NS00; -.
DR BioMuta; C1GALT1; -.
DR DMDM; 74719147; -.
DR EPD; Q9NS00; -.
DR jPOST; Q9NS00; -.
DR MassIVE; Q9NS00; -.
DR MaxQB; Q9NS00; -.
DR PaxDb; Q9NS00; -.
DR PeptideAtlas; Q9NS00; -.
DR PRIDE; Q9NS00; -.
DR ProteomicsDB; 82459; -. [Q9NS00-1]
DR ProteomicsDB; 82460; -. [Q9NS00-2]
DR Antibodypedia; 2308; 144 antibodies from 25 providers.
DR DNASU; 56913; -.
DR Ensembl; ENST00000223122.4; ENSP00000223122.2; ENSG00000106392.11. [Q9NS00-1]
DR Ensembl; ENST00000402468.3; ENSP00000384550.3; ENSG00000106392.11. [Q9NS00-2]
DR Ensembl; ENST00000436587.7; ENSP00000389176.2; ENSG00000106392.11. [Q9NS00-1]
DR GeneID; 56913; -.
DR KEGG; hsa:56913; -.
DR MANE-Select; ENST00000436587.7; ENSP00000389176.2; NM_020156.5; NP_064541.1.
DR UCSC; uc003sra.5; human. [Q9NS00-1]
DR CTD; 56913; -.
DR DisGeNET; 56913; -.
DR GeneCards; C1GALT1; -.
DR HGNC; HGNC:24337; C1GALT1.
DR HPA; ENSG00000106392; Low tissue specificity.
DR MIM; 610555; gene.
DR neXtProt; NX_Q9NS00; -.
DR OpenTargets; ENSG00000106392; -.
DR PharmGKB; PA134971259; -.
DR VEuPathDB; HostDB:ENSG00000106392; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155000; -.
DR HOGENOM; CLU_035857_0_0_1; -.
DR InParanoid; Q9NS00; -.
DR OMA; EKRERFH; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q9NS00; -.
DR TreeFam; TF317293; -.
DR BioCyc; MetaCyc:HS02901-MON; -.
DR BRENDA; 2.4.1.122; 2681.
DR PathwayCommons; Q9NS00; -.
DR Reactome; R-HSA-5083632; Defective C1GALT1C1 causes TNPS.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9NS00; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 56913; 14 hits in 1038 CRISPR screens.
DR ChiTaRS; C1GALT1; human.
DR GenomeRNAi; 56913; -.
DR Pharos; Q9NS00; Tbio.
DR PRO; PR:Q9NS00; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NS00; protein.
DR Bgee; ENSG00000106392; Expressed in amniotic fluid and 188 other tissues.
DR ExpressionAtlas; Q9NS00; baseline and differential.
DR Genevisible; Q9NS00; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
DR InterPro; IPR026842; C1GALT1.
DR InterPro; IPR003378; Fringe-like.
DR PANTHER; PTHR23033:SF13; PTHR23033:SF13; 1.
DR Pfam; PF02434; Fringe; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Developmental protein; Differentiation;
KW Disulfide bond; Glycosyltransferase; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1"
FT /id="PRO_0000285064"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..363
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 41..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJ06"
FT VAR_SEQ 297..363
FT /note="GPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEIS
FT QANKNEDTKVKLGNP -> VSLEILLLCQYLD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024809"
SQ SEQUENCE 363 AA; 42203 MW; 01F472B55C5F526F CRC64;
MASKSWLNFL TFLCGSAIGF LLCSQLFSIL LGEKVDTQPN VLHNDPHARH SDDNGQNHLE
GQMNFNADSS QHKDENTDIA ENLYQKVRIL CWVMTGPQNL EKKAKHVKAT WAQRCNKVLF
MSSEENKDFP AVGLKTKEGR DQLYWKTIKA FQYVHEHYLE DADWFLKADD DTYVILDNLR
WLLSKYDPEE PIYFGRRFKP YVKQGYMSGG AGYVLSKEAL KRFVDAFKTD KCTHSSSIED
LALGRCMEIM NVEAGDSRDT IGKETFHPFV PEHHLIKGYL PRTFWYWNYN YYPPVEGPGC
CSDLAVSFHY VDSTTMYELE YLVYHLRPYG YLYRYQPTLP ERILKEISQA NKNEDTKVKL
GNP
