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 02-OCT-2024, entry version 166. 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 INVOLVEMENT IN AHUS8, AND VARIANT AHUS8 ILE-89. RX PubMed=36599939; DOI=10.1038/s41431-022-01278-5; RA Hadar N., Schreiber R., Eskin-Schwartz M., Kristal E., Shubinsky G., RA Ling G., Cohen I., Geylis M., Nahum A., Yogev Y., Birk O.S.; RT "X-linked C1GALT1C1 mutation causes atypical hemolytic uremic syndrome."; RL Eur. J. Hum. Genet. 31:1101-1107(2023). RN [15] 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). RN [16] RP VARIANT AHUS8 ASP-20, CHARACTERIZATION OF VARIANT AHUS8 ASP-20, AND RP FUNCTION. RX PubMed=37216524; DOI=10.1073/pnas.2211087120; RA Erger F., Aryal R.P., Reusch B., Matsumoto Y., Meyer R., Zeng J., Knopp C., RA Noel M., Muerner L., Wenzel A., Kohl S., Tschernoster N., Rappl G., RA Rouvet I., Schroeder-Braunstein J., Seibert F.S., Thiele H., Haeusler M.G., RA Weber L.T., Buettner-Herold M., Elbracht M., Cummings S.F., Altmueller J., RA Habbig S., Cummings R.D., Beck B.B.; RT "Germline C1GALT1C1 mutation causes a multisystem chaperonopathy."; RL Proc. Natl. Acad. Sci. U.S.A. 120:e2211087120-e2211087120(2023). 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 ECO:0000269|PubMed:37216524}. 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 -!- DISEASE: Hemolytic uremic syndrome, atypical, 8, with rhizomelic short CC stature (AHUS8) [MIM:301110]: An X-linked, atypical form of hemolytic CC uremic syndrome, characterized by microangiopathic hemolytic anemia, CC thrombocytopenia, renal failure and absence of episodes of CC enterocolitis and diarrhea. In contrast to typical hemolytic uremic CC syndrome, atypical forms have a poorer prognosis, with higher death CC rates and frequent progression to end-stage renal disease. AHUS8 CC patients have short stature with short limbs, in addition to acute CC renal dysfunction with proteinuria, thrombotic microangiopathy, anemia, CC thrombocytopenia, increased serum lactate dehydrogenase, and CC schistocytes on peripheral blood smear. More variable features include CC immunodeficiency with recurrent infections, developmental delay, and CC dysmorphic features. The age at onset of renal symptoms is variable, CC ranging from infancy to the early twenties. Female carriers may be CC mildly affected. {ECO:0000269|PubMed:36599939, CC ECO:0000269|PubMed:37216524}. 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; Note=Truncated N-terminus.; 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"; 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; 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; 34. DR IntAct; Q96EU7; 22. 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 jPOST; Q96EU7; -. DR MassIVE; Q96EU7; -. DR PaxDb; 9606-ENSP00000304364; -. DR PeptideAtlas; Q96EU7; -. DR ProteomicsDB; 76452; -. DR Pumba; Q96EU7; -. DR Antibodypedia; 545; 112 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 AGR; HGNC:24338; -. 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 MIM; 301110; 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; WVMMRKA; -. DR OrthoDB; 3534522at2759; -. 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; 20 hits in 776 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 100 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IMP:UniProtKB. 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:UniProtKB. DR Gene3D; 3.90.550.50; -; 1. DR InterPro; IPR026050; C1GALT1/C1GALT1_chp1. DR PANTHER; PTHR23033; BETA1,3-GALACTOSYLTRANSFERASE; 1. DR PANTHER; PTHR23033:SF2; C1GALT1-SPECIFIC CHAPERONE 1; 1. PE 1: Evidence at protein level; KW Chaperone; Disease variant; Hemolytic uremic syndrome; Membrane; KW Proteomics identification; 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 20 FT /note="A -> D (in AHUS8; likely pathogenic; decreased FT function in protein O-linked glycosylation; decreased FT protein abundance in patient lymphoblastoid cells; FT increased protein degradation by the proteasome-dependent FT pathway)" FT /evidence="ECO:0000269|PubMed:37216524" FT /id="VAR_088735" FT VARIANT 89 FT /note="T -> I (in AHUS8; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:36599939" FT /id="VAR_088736" 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 //