C1GLC_MOUSE
ID C1GLC_MOUSE Reviewed; 316 AA.
AC Q9JMG2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=C1GALT1-specific chaperone 1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 2;
DE Short=C1Gal-T2;
DE Short=C1GalT2;
DE Short=Core 1 beta3-Gal-T2;
DE Short=mC1Gal-T2;
DE AltName: Full=Core 1 beta3-galactosyltransferase-specific molecular chaperone;
GN Name=C1galt1c1; Synonyms=Cosmc;
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].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Liver;
RA Kudo T., Takayama Y., Narimatsu H.;
RT "Molecular cloning of a UDP-Gal: GalNAcalpha-peptide mouse beta1,3-
RT galactosyltransferase (mC1Gal-T2), an enzyme synthesizing a core 1
RT structure of O-glycan.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Probable chaperone required for the generation of 1 O-glycan
CC Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for
CC many extended O-glycans in glycoproteins. Probably acts as a specific
CC molecular chaperone assisting the folding/stability of core 1 beta-3-
CC galactosyltransferase (C1GALT1) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with core 1 beta-3-galactosyltransferase (C1GALT1),
CC probably not with the soluble active form. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally assigned to be a glycosyltransferase.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=C1GALT2
CC (same seq as COSMC);
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_467";
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DR EMBL; AB030184; BAA92748.1; -; mRNA.
DR EMBL; AY159320; AAN78130.1; -; mRNA.
DR EMBL; AB091728; BAD13521.1; -; mRNA.
DR EMBL; AK008040; BAB25426.1; -; mRNA.
DR EMBL; AL590633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029909; AAH29909.1; -; mRNA.
DR CCDS; CCDS30095.1; -.
DR RefSeq; NP_067525.1; NM_021550.3.
DR AlphaFoldDB; Q9JMG2; -.
DR SMR; Q9JMG2; -.
DR BioGRID; 208512; 2.
DR STRING; 10090.ENSMUSP00000059224; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q9JMG2; -.
DR PhosphoSitePlus; Q9JMG2; -.
DR EPD; Q9JMG2; -.
DR MaxQB; Q9JMG2; -.
DR PaxDb; Q9JMG2; -.
DR PeptideAtlas; Q9JMG2; -.
DR PRIDE; Q9JMG2; -.
DR ProteomicsDB; 273724; -.
DR Antibodypedia; 545; 93 antibodies from 25 providers.
DR DNASU; 59048; -.
DR Ensembl; ENSMUST00000058265; ENSMUSP00000059224; ENSMUSG00000048970.
DR GeneID; 59048; -.
DR KEGG; mmu:59048; -.
DR UCSC; uc009tag.2; mouse.
DR CTD; 29071; -.
DR MGI; MGI:1913493; C1galt1c1.
DR VEuPathDB; HostDB:ENSMUSG00000048970; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155145; -.
DR HOGENOM; CLU_874237_0_0_1; -.
DR InParanoid; Q9JMG2; -.
DR OMA; CIIMVQP; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q9JMG2; -.
DR TreeFam; TF317293; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR BioGRID-ORCS; 59048; 4 hits in 73 CRISPR screens.
DR ChiTaRS; C1galt1c1; mouse.
DR PRO; PR:Q9JMG2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JMG2; protein.
DR Bgee; ENSMUSG00000048970; Expressed in choroid plexus epithelium and 241 other tissues.
DR Genevisible; Q9JMG2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0036344; P:platelet morphogenesis; IMP:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
DR InterPro; IPR026731; C1GALT1C1.
DR PANTHER; PTHR23033:SF2; PTHR23033:SF2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..316
FT /note="C1GALT1-specific chaperone 1"
FT /id="PRO_0000285075"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..316
FT /note="Lumenal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 316 AA; 36067 MW; 9B7BFCBD6E834B2B CRC64;
MLSESSSFLK GVMLGSIFCA LITMLGHIRI GNRMHHHEHH HLQAPNKDDI SKISEAERME
LSKSFRVYCI VLVKPKDVSL WAAVKETWTK HCDKAEFFSS ENVKVFESIN MDTNDMWLMM
RKAYKYAYDQ YRDQYNWFFL ARPTTFAVIE NLKYFLLKKD QSQPFYLGHT VKSGDLEYVS
VDGGIVLSIE SMKRLNSLLS VPEKCPEQGG MIWKISEDKQ LAVCLKYAGV FAENAEDADG
KDVFNTKSVG LFIKEAMTNQ PNQVVEGCCS DMAVTFNGLT PNQMHVMMYG VYRLRAFGHV
FNDALVFLPP NGSEND
