C1GLC_HUMAN
ID C1GLC_HUMAN Reviewed; 318 AA.
AC Q96EU7; A8K246; Q8WWS3; Q9NZX1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=C1GALT1-specific chaperone 1;
DE AltName: Full=C38H2-like protein 1;
DE Short=C38H2-L1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 2;
DE Short=C1Gal-T2;
DE Short=C1GalT2;
DE Short=Core 1 beta3-Gal-T2;
DE AltName: Full=Core 1 beta3-galactosyltransferase-specific molecular chaperone;
GN Name=C1GALT1C1; Synonyms=COSMC; ORFNames=HSPC067, MSTP143, UNQ273/PRO310;
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], AND TISSUE SPECIFICITY.
RX PubMed=12361956; DOI=10.1074/jbc.m205839200;
RA Kudo T., Iwai T., Kubota T., Iwasaki H., Takayma Y., Hiruma T., Inaba N.,
RA Zhang Y., Gotoh M., Togayachi A., Narimatsu H.;
RT "Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha)
RT peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a
RT core 1 structure of O-glycan.";
RL J. Biol. Chem. 277:47724-47731(2002).
RN [2]
RP ERRATUM OF PUBMED:12361956.
RA Kudo T., Iwai T., Kubota T., Iwasaki H., Takayma Y., Hiruma T., Inaba N.,
RA Zhang Y., Gotoh M., Togayachi A., Narimatsu H.;
RL J. Biol. Chem. 281:24999-24999(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH C1GALT1.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rubboli F., Marchitiello A., Ballabio A., Banfi S.;
RT "Identification and characterization of C38H2-L1.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Aorta;
RA Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
RA Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [10]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Ovary;
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 [12]
RP VARIANT TNPS LYS-152, VARIANT GLU-131, CHARACTERIZATION OF VARIANT TNPS
RP LYS-152, AND CHARACTERIZATION OF VARIANT GLU-131.
RX PubMed=16251947; DOI=10.1038/4371252a;
RA Ju T., Cummings R.D.;
RT "Protein glycosylation: chaperone mutation in Tn syndrome.";
RL Nature 437:1252-1252(2005).
RN [13]
RP INVOLVEMENT IN PRODUCTION OF TUMOR-SPECIFIC ANTIGEN.
RX PubMed=17038624; DOI=10.1126/science.1129200;
RA Schietinger A., Philip M., Yoshida B.A., Azadi P., Liu H., Meredith S.C.,
RA Schreiber H.;
RT "A mutant chaperone converts a wild-type protein into a tumor-specific
RT antigen.";
RL Science 314:304-308(2006).
RN [14]
RP VARIANTS GLU-131; VAL-143 AND HIS-222, AND VARIANTS TNPS LYS-152 AND
RP PRO-193.
RX PubMed=18537974; DOI=10.1111/j.1365-2141.2008.07215.x;
RA Crew V.K., Singleton B.K., Green C., Parsons S.F., Daniels G., Anstee D.J.;
RT "New mutations in C1GALT1C1 in individuals with Tn positive phenotype.";
RL Br. J. Haematol. 142:657-667(2008).
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). {ECO:0000269|PubMed:12464682}.
CC -!- SUBUNIT: Associates with core 1 beta-3-galactosyltransferase (C1GALT1),
CC probably not with the soluble active form.
CC -!- INTERACTION:
CC Q96EU7; Q9NS00: C1GALT1; NbExp=4; IntAct=EBI-2837343, EBI-8628584;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Abundantly expressed in
CC salivary gland, stomach, small intestine, kidney, and testis and at
CC intermediate levels in whole brain, cerebellum, spinal cord, thymus,
CC spleen, trachea, lung, pancreas, ovary, and uterus.
CC {ECO:0000269|PubMed:12361956}.
CC -!- DISEASE: Tn polyagglutination syndrome (TNPS) [MIM:300622]: A clonal
CC disorder characterized by the polyagglutination of red blood cells by
CC naturally occurring anti-Tn antibodies following exposure of the Tn
CC antigen on the surface of erythrocytes. Only a subset of red cells
CC express the antigen, which can also be expressed on platelets and
CC leukocytes. This condition may occur in healthy individuals who
CC manifest asymptomatic anemia, leukopenia, or thrombocytopenia. However,
CC there is also an association between the Tn antigen and leukemia or
CC myelodysplastic disorders. {ECO:0000269|PubMed:16251947,
CC ECO:0000269|PubMed:18537974}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Defects in C1GALT1C1 in Ag104A cell line create a tumor-
CC specific glycopeptidic neo-epitope. This epitope induces a high-
CC affinity, highly specific, syngeneic monoclonal antibody. This is
CC caused by the abolition of function of a glycosyltransferase,
CC disrupting O-glycan Core 1 synthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:12361956) assigned to be a
CC glycosyltransferase. However, it was later shown (Ref.2 and
CC PubMed:12464682) that it has no transferase activity and rather acts as
CC a chaperone. {ECO:0000305|PubMed:12361956}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29039.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC80277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=C1GALT1-
CC specific chaperone 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_443";
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DR EMBL; AB084170; BAC41493.1; -; mRNA.
DR EMBL; AY159319; AAN78129.1; -; mRNA.
DR EMBL; AJ238398; CAC80277.1; ALT_INIT; mRNA.
DR EMBL; AF161552; AAF29039.1; ALT_FRAME; mRNA.
DR EMBL; AF177284; AAQ13670.1; -; mRNA.
DR EMBL; AY358642; AAQ89005.1; -; mRNA.
DR EMBL; AC011890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK290111; BAF82800.1; -; mRNA.
DR EMBL; CH471107; EAX11873.1; -; Genomic_DNA.
DR EMBL; BC011930; AAH11930.1; -; mRNA.
DR EMBL; BC050441; AAH50441.1; -; mRNA.
DR CCDS; CCDS14602.1; -.
DR RefSeq; NP_001011551.1; NM_001011551.2.
DR RefSeq; NP_689905.1; NM_152692.4.
DR AlphaFoldDB; Q96EU7; -.
DR SMR; Q96EU7; -.
DR BioGRID; 118844; 30.
DR IntAct; Q96EU7; 10.
DR MINT; Q96EU7; -.
DR STRING; 9606.ENSP00000304364; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q96EU7; -.
DR PhosphoSitePlus; Q96EU7; -.
DR BioMuta; C1GALT1C1; -.
DR DMDM; 74751849; -.
DR EPD; Q96EU7; -.
DR jPOST; Q96EU7; -.
DR MassIVE; Q96EU7; -.
DR MaxQB; Q96EU7; -.
DR PaxDb; Q96EU7; -.
DR PeptideAtlas; Q96EU7; -.
DR PRIDE; Q96EU7; -.
DR ProteomicsDB; 76452; -.
DR Antibodypedia; 545; 93 antibodies from 25 providers.
DR DNASU; 29071; -.
DR Ensembl; ENST00000304661.6; ENSP00000304364.5; ENSG00000171155.8.
DR Ensembl; ENST00000371313.2; ENSP00000360363.2; ENSG00000171155.8.
DR Ensembl; ENST00000673177.1; ENSP00000500356.1; ENSG00000288368.1.
DR Ensembl; ENST00000673568.1; ENSP00000500561.1; ENSG00000288368.1.
DR GeneID; 29071; -.
DR KEGG; hsa:29071; -.
DR MANE-Select; ENST00000304661.6; ENSP00000304364.5; NM_001011551.3; NP_001011551.1.
DR UCSC; uc004esy.4; human.
DR CTD; 29071; -.
DR DisGeNET; 29071; -.
DR GeneCards; C1GALT1C1; -.
DR HGNC; HGNC:24338; C1GALT1C1.
DR HPA; ENSG00000171155; Low tissue specificity.
DR MalaCards; C1GALT1C1; -.
DR MIM; 300611; gene.
DR MIM; 300622; phenotype.
DR neXtProt; NX_Q96EU7; -.
DR OpenTargets; ENSG00000171155; -.
DR PharmGKB; PA134974626; -.
DR VEuPathDB; HostDB:ENSG00000171155; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155145; -.
DR HOGENOM; CLU_874237_0_0_1; -.
DR InParanoid; Q96EU7; -.
DR OMA; CIIMVQP; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q96EU7; -.
DR TreeFam; TF317293; -.
DR BRENDA; 2.4.1.122; 2681.
DR PathwayCommons; Q96EU7; -.
DR Reactome; R-HSA-5083632; Defective C1GALT1C1 causes TNPS.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q96EU7; -.
DR BioGRID-ORCS; 29071; 18 hits in 702 CRISPR screens.
DR ChiTaRS; C1GALT1C1; human.
DR GenomeRNAi; 29071; -.
DR Pharos; Q96EU7; Tbio.
DR PRO; PR:Q96EU7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96EU7; protein.
DR Bgee; ENSG00000171155; Expressed in islet of Langerhans and 98 other tissues.
DR Genevisible; Q96EU7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; IEA:Ensembl.
DR GO; GO:0036344; P:platelet morphogenesis; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
DR InterPro; IPR026731; C1GALT1C1.
DR PANTHER; PTHR23033:SF2; PTHR23033:SF2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Disease variant; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="C1GALT1-specific chaperone 1"
FT /id="PRO_0000285074"
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..318
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT VARIANT 131
FT /note="D -> E (retains capacity to promote Tn synthase
FT activity; dbSNP:rs17261572)"
FT /evidence="ECO:0000269|PubMed:16251947,
FT ECO:0000269|PubMed:18537974"
FT /id="VAR_031910"
FT VARIANT 143
FT /note="A -> V (in dbSNP:rs45557031)"
FT /evidence="ECO:0000269|PubMed:18537974"
FT /id="VAR_069274"
FT VARIANT 152
FT /note="E -> K (in TNPS; loss capacity to promote Tn
FT synthase activity; dbSNP:rs137853599)"
FT /evidence="ECO:0000269|PubMed:16251947,
FT ECO:0000269|PubMed:18537974"
FT /id="VAR_031911"
FT VARIANT 193
FT /note="S -> P (in TNPS; dbSNP:rs397514537)"
FT /evidence="ECO:0000269|PubMed:18537974"
FT /id="VAR_069275"
FT VARIANT 222
FT /note="Q -> H (in dbSNP:rs200973382)"
FT /evidence="ECO:0000269|PubMed:18537974"
FT /id="VAR_069276"
FT CONFLICT 76
FT /note="K -> E (in Ref. 4; CAC80277)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> E (in Ref. 5; AAF29039)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> L (in Ref. 4; CAC80277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36382 MW; 5D766966A872CA84 CRC64;
MLSESSSFLK GVMLGSIFCA LITMLGHIRI GHGNRMHHHE HHHLQAPNKE DILKISEDER
MELSKSFRVY CIILVKPKDV SLWAAVKETW TKHCDKAEFF SSENVKVFES INMDTNDMWL
MMRKAYKYAF DKYRDQYNWF FLARPTTFAI IENLKYFLLK KDPSQPFYLG HTIKSGDLEY
VGMEGGIVLS VESMKRLNSL LNIPEKCPEQ GGMIWKISED KQLAVCLKYA GVFAENAEDA
DGKDVFNTKS VGLSIKEAMT YHPNQVVEGC CSDMAVTFNG LTPNQMHVMM YGVYRLRAFG
HIFNDALVFL PPNGSDND
