CLIC1_RAT
ID CLIC1_RAT Reviewed; 241 AA.
AC Q6MG61;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Chloride intracellular channel protein 1 {ECO:0000250|UniProtKB:O00299, ECO:0000312|EMBL:CAE83985.1};
GN Name=Clic1 {ECO:0000312|EMBL:CAE83985.1, ECO:0000312|RGD:1303043};
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] {ECO:0000312|EMBL:CAE83985.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:CAE83985.1};
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:EDL83493.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL83493.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAH99823.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH99823.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:EDL83493.1}
RP PROTEIN SEQUENCE OF 2-13 AND 120-131, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [5] {ECO:0000305, ECO:0000312|EMBL:EDL83493.1}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Can insert into membranes and form chloride ion channels.
CC Channel activity depends on the pH. Membrane insertion seems to be
CC redox-regulated and may occur only under oxydizing conditions (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2.
CC Dimerization requires a conformation change that leads to the exposure
CC of a large hydrophobic surface. In vivo, this may lead to membrane
CC insertion (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00299}. Nucleus
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Cytoplasm {ECO:0000250|UniProtKB:O00299}. Cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus
CC including in the nuclear membrane. Small amount in the cytoplasm and
CC the plasma membrane. Exists both as soluble cytoplasmic protein and as
CC membrane protein with probably a single transmembrane domain (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Members of this family may change from a globular, soluble
CC state to a state where the N-terminal domain is inserted into the
CC membrane and functions as chloride channel. A conformation change of
CC the N-terminal domain is thought to expose hydrophobic surfaces that
CC trigger membrane insertion (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000255}.
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DR EMBL; BX883045; CAE83985.1; -; Genomic_DNA.
DR EMBL; CH474121; EDL83493.1; -; Genomic_DNA.
DR EMBL; BC099823; AAH99823.1; -; mRNA.
DR RefSeq; NP_001002807.1; NM_001002807.2.
DR AlphaFoldDB; Q6MG61; -.
DR SMR; Q6MG61; -.
DR STRING; 10116.ENSRNOP00000060240; -.
DR iPTMnet; Q6MG61; -.
DR PhosphoSitePlus; Q6MG61; -.
DR jPOST; Q6MG61; -.
DR PaxDb; Q6MG61; -.
DR PRIDE; Q6MG61; -.
DR GeneID; 406864; -.
DR KEGG; rno:406864; -.
DR UCSC; RGD:1303043; rat.
DR CTD; 1192; -.
DR RGD; 1303043; Clic1.
DR VEuPathDB; HostDB:ENSRNOG00000029682; -.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q6MG61; -.
DR OMA; EEIHIAY; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q6MG61; -.
DR TreeFam; TF315438; -.
DR PRO; PR:Q6MG61; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Proteomes; UP000234681; Chromosome 20.
DR Bgee; ENSRNOG00000029682; Expressed in ileum and 19 other tissues.
DR Genevisible; Q6MG61; RN.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; ISO:RGD.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; TAS:RGD.
DR GO; GO:0006821; P:chloride transport; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030259; CLIC-1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43920:SF2; PTHR43920:SF2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00862; O-ClC; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Ion channel; Ion transport;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..241
FT /note="Chloride intracellular channel protein 1"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT /id="PRO_0000365103"
FT TRANSMEM 26..46
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 93..233
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT REGION 2..90
FT /note="Required for insertion into the membrane"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q5"
FT DISULFID 24..59
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 26981 MW; 1774F7190D44B01C CRC64;
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTSGLDI FAKFSAYIKN
SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GISQRKFLDG NELTLADCNL
LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVARAL
K
