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   03-AUG-2022, entry version 119.
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}.
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}. Nucleus membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}. Note=Mostly in the nucleus including in the
CC       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       {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: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; Q5E9B7; -.
DR   PeptideAtlas; Q5E9B7; -.
DR   PRIDE; Q5E9B7; -.
DR   Ensembl; ENSBTAT00000017995; ENSBTAP00000017995; ENSBTAG00000013533.
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; EEIHIAY; -.
DR   OrthoDB; 974249at2759; -.
DR   TreeFam; TF315438; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000013533; Expressed in abomasum and 106 other tissues.
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; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW   Disulfide bond; Ion channel; Ion transport; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   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