ID   C1GLC_RAT               Reviewed;         316 AA.
AC   Q499P3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=C1GALT1-specific chaperone 1;
GN   Name=C1galt1c1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [2]
RP   PROTEIN SEQUENCE OF 1-18, 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).
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.
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}.
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DR   EMBL; BC099818; AAH99818.1; -; mRNA.
DR   RefSeq; NP_001025204.1; NM_001030033.1.
DR   RefSeq; XP_006257549.1; XM_006257487.1.
DR   AlphaFoldDB; Q499P3; -.
DR   SMR; Q499P3; -.
DR   STRING; 10116.ENSRNOP00000003449; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q499P3; -.
DR   Ensembl; ENSRNOT00000105484; ENSRNOP00000081816; ENSRNOG00000069353.
DR   GeneID; 302499; -.
DR   KEGG; rno:302499; -.
DR   UCSC; RGD:1311230; rat.
DR   CTD; 29071; -.
DR   RGD; 1311230; C1galt1c1.
DR   eggNOG; KOG2246; Eukaryota.
DR   GeneTree; ENSGT00940000155145; -.
DR   HOGENOM; CLU_874237_0_0_1; -.
DR   InParanoid; Q499P3; -.
DR   OMA; CIIMVQP; -.
DR   OrthoDB; 1407357at2759; -.
DR   PhylomeDB; Q499P3; -.
DR   TreeFam; TF317293; -.
DR   Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR   PRO; PR:Q499P3; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000002536; Expressed in stomach and 20 other tissues.
DR   Genevisible; Q499P3; RN.
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; ISO:RGD.
DR   GO; GO:0036344; P:platelet morphogenesis; ISO:RGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
DR   InterPro; IPR026731; C1GALT1C1.
DR   PANTHER; PTHR23033:SF2; PTHR23033:SF2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="C1GALT1-specific chaperone 1"
FT                   /id="PRO_0000285076"
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;  36035 MW;  50CB306A457C1035 CRC64;
     MLSESSSFLK GVMLGSIFCA LITMLGHIRI GNRMHHHEHH HLQAPNKDDI LKISETERME
     LSKSFQVYCI VLVKPKDVSL WAAVKETWTK HCDKAEFFSS ENVKVFESIN MDTNDMWLMM
     RKAYKYAYDK YKDQYNWFFL ARPTTFAVIE NLKYFLLRKD PSQPFYLGHT VKSGDLEYVS
     VDGGIVLSIE SMKRLNGLLS VPEKCPEQGG MIWKISEDKQ LAVCLKYAGV FAENAEDADG
     KDVFNTKSVG LFIKEAMTNQ PNQVVEGCCS DMAVTFNGLT PNQMHVMMYG VYRLRAFGHV
     FNDALVFLPP NGSEND