ID CLIC1_BOVIN Reviewed; 241 AA.
AC Q5E9B7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Chloride intracellular channel protein 1;
GN Name=CLIC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:O00299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:O00299};
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|UniProtKB:O00299}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00299}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00299}. Cell membrane
CC {ECO:0000250|UniProtKB:O00299}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00299}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6MG61}. Note=Mostly in the nucleus including in
CC the nuclear membrane. Small amount in the cytoplasm and the plasma
CC membrane. Exists both as soluble cytoplasmic protein and as membrane
CC protein with probably a single transmembrane domain (By similarity).
CC Might not be present in the nucleus of cardiac cells (By similarity).
CC {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q6MG61}.
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 a 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:0000305}.
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DR EMBL; BT021003; AAX09020.1; -; mRNA.
DR EMBL; BC102103; AAI02104.1; -; mRNA.
DR RefSeq; NP_001015608.1; NM_001015608.1.
DR AlphaFoldDB; Q5E9B7; -.
DR SMR; Q5E9B7; -.
DR STRING; 9913.ENSBTAP00000017995; -.
DR PaxDb; 9913-ENSBTAP00000017995; -.
DR PeptideAtlas; Q5E9B7; -.
DR Ensembl; ENSBTAT00000017995.3; ENSBTAP00000017995.2; ENSBTAG00000013533.3.
DR GeneID; 515646; -.
DR KEGG; bta:515646; -.
DR CTD; 1192; -.
DR VEuPathDB; HostDB:ENSBTAG00000013533; -.
DR VGNC; VGNC:27439; CLIC1.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000154708; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q5E9B7; -.
DR OMA; SYMKSIF; -.
DR OrthoDB; 103277at2759; -.
DR TreeFam; TF315438; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000013533; Expressed in abomasum and 106 other cell types or tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR CDD; cd10300; GST_C_CLIC1; 1.
DR CDD; cd03061; GST_N_CLIC; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030259; CLIC-1_C.
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 NCBIfam; TIGR00862; O-ClC; 1.
DR PANTHER; PTHR45476:SF2; CHLORIDE INTRACELLULAR CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Disulfide bond; Endoplasmic reticulum; 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:0000250|UniProtKB:O00299"
FT CHAIN 2..241
FT /note="Chloride intracellular channel protein 1"
FT /id="PRO_0000236248"
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 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:0000250|UniProtKB:O00299"
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 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q5"
FT DISULFID 24..59
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 26992 MW; 7443E31C9A88100D CRC64;
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI FAKFSAYIKN
SNPALNDNLE KGLLKALKVL DNYLTSPLPD EVDETSAEDE GISQRKFLDG NELTLADCNL
LPKLHIVQVV CKKYRGFSIP DVFRGVHRYL RNAYAREEFA STCPDDEEIE LAYEQVAKAL
K
//
