C1GLT_MOUSE
ID C1GLT_MOUSE Reviewed; 363 AA.
AC Q9JJ06; Q6P218; Q8R0Z7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE AltName: Full=Core 1 O-glycan T-synthase;
DE Short=T-syn;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1;
DE Short=C1GalT1;
DE Short=Core 1 beta3-Gal-T1;
GN Name=C1galt1; Synonyms=Plt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr, and FVB/N; TISSUE=Hematopoietic stem cell, and 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 [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14745002; DOI=10.1083/jcb.200311112;
RA Xia L., Ju T., Westmuckett A., An G., Ivanciu L., McDaniel J.M., Lupu F.,
RA Cummings R.D., McEver R.P.;
RT "Defective angiogenesis and fatal embryonic hemorrhage in mice lacking core
RT 1-derived O-glycans.";
RL J. Cell Biol. 164:451-459(2004).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF TYR-321.
RX PubMed=17062753; DOI=10.1073/pnas.0607872103;
RA Alexander W.S., Viney E.M., Zhang J.-G., Metcalf D., Kauppi M.,
RA Hyland C.D., Carpinelli M.R., Stevenson W., Croker B.A., Hilton A.A.,
RA Ellis S., Selan C., Nandurkar H.H., Goodnow C.C., Kile B.T., Nicola N.A.,
RA Roberts A.W., Hilton D.J.;
RT "Thrombocytopenia and kidney disease in mice with a mutation in the C1galt1
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16442-16447(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:14745002,
CC ECO:0000269|PubMed:17062753}.
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:0000250|UniProtKB:Q9NS00};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with the C1GALT1C1
CC chaperone; required for galactosyltransferase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Primarily expressed in endothelial, hematopoietic
CC and epithelial cells during development. {ECO:0000269|PubMed:14745002}.
CC -!- DISRUPTION PHENOTYPE: Mice develop brain hemorrhage that cause death at
CC 14 dpc during development. They express the nonsialylated Tn antigen
CC and brains form a chaotic microvascular network with distorted
CC capillary lumens and defective association of endothelial cells with
CC pericytes and extracellular matrix. {ECO:0000269|PubMed:14745002}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
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DR EMBL; AF157962; AAF81982.1; -; mRNA.
DR EMBL; BC025899; AAH25899.1; -; mRNA.
DR EMBL; BC064767; AAH64767.1; -; mRNA.
DR CCDS; CCDS19908.1; -.
DR RefSeq; NP_443719.3; NM_052993.3.
DR AlphaFoldDB; Q9JJ06; -.
DR SMR; Q9JJ06; -.
DR BioGRID; 220468; 2.
DR STRING; 10090.ENSMUSP00000047931; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q9JJ06; -.
DR PhosphoSitePlus; Q9JJ06; -.
DR EPD; Q9JJ06; -.
DR MaxQB; Q9JJ06; -.
DR PaxDb; Q9JJ06; -.
DR PeptideAtlas; Q9JJ06; -.
DR PRIDE; Q9JJ06; -.
DR ProteomicsDB; 273725; -.
DR Antibodypedia; 2308; 144 antibodies from 25 providers.
DR DNASU; 94192; -.
DR Ensembl; ENSMUST00000040159; ENSMUSP00000047931; ENSMUSG00000042460.
DR GeneID; 94192; -.
DR KEGG; mmu:94192; -.
DR UCSC; uc009axg.2; mouse.
DR CTD; 56913; -.
DR MGI; MGI:2151071; C1galt1.
DR VEuPathDB; HostDB:ENSMUSG00000042460; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155000; -.
DR HOGENOM; CLU_035857_0_0_1; -.
DR InParanoid; Q9JJ06; -.
DR OMA; EKRERFH; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q9JJ06; -.
DR TreeFam; TF317293; -.
DR BRENDA; 2.4.1.122; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 94192; 3 hits in 72 CRISPR screens.
DR ChiTaRS; C1galt1; mouse.
DR PRO; PR:Q9JJ06; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JJ06; protein.
DR Bgee; ENSMUSG00000042460; Expressed in epithelium of stomach and 246 other tissues.
DR Genevisible; Q9JJ06; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0008378; F:galactosyltransferase activity; ISO:MGI.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0016267; P:O-glycan processing, core 1; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
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 Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW Glycosyltransferase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..363
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1"
FT /id="PRO_0000285065"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..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 MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MUTAGEN 321
FT /note="Y->N: In plt1; loss of function inducing
FT thrombocytopenia and kidney disease."
FT /evidence="ECO:0000269|PubMed:17062753"
FT CONFLICT 187
FT /note="N -> D (in Ref. 2; AAH64767)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="H -> R (in Ref. 2; AAH64767)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="Y -> C (in Ref. 2; AAH64767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 42304 MW; 3279FBC5AE660EB4 CRC64;
MASKSWLNFL VFLCGSAIGF FLCSQLLSIL LREEAAIQPN MLHNDPHARH SDDNGHSHLK
GQMNFNADSS QHKDENIDVA ENLYQKVKIL CWVMTSPQNL EKKAKHVKAT WAQRCNKVLF
MSSEENQDFP TVGLKTKEGR EQLYWKTIKA FQYVHDHYLE DADWFMKADD DTYVIVDNLR
WLLSKYNPEQ PIYFGRRFKP YVKQGYMSGG AGYVLSKEAL RRFVNAFKTE KCTHSSSIED
LALGRCMEII NVEAGDSRDT IGKETFHPFV PEHHLIKGYL PKTFWYWNYN YYPPIEGPGC
CSDIAVSFHY VDGTTMYELE YLVYHLRPYG YLYRYQPALP ENILKEINQV NRKEDTKIKL
GNP
