ID   CLIC1_PIG               Reviewed;         110 AA.
AC   Q29238;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Chloride intracellular channel protein 1;
DE   AltName: Full=Nuclear chloride ion channel 27;
DE   Flags: Fragment;
GN   Name=CLIC1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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; F14837; CAA23286.1; -; mRNA.
DR   AlphaFoldDB; Q29238; -.
DR   SMR; Q29238; -.
DR   PeptideAtlas; Q29238; -.
DR   PRIDE; Q29238; -.
DR   InParanoid; Q29238; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002946; CLIC.
DR   InterPro; IPR030259; CLIC-1.
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   SUPFAM; SSF52833; SSF52833; 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   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00299"
FT   CHAIN           2..>110
FT                   /note="Chloride intracellular channel protein 1"
FT                   /id="PRO_0000144203"
FT   TRANSMEM        26..46
FT                   /note="Helical; Note=After insertion into the membrane"
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:0000250|UniProtKB:O00299"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00299"
FT   DISULFID        24..59
FT                   /evidence="ECO:0000250"
FT   NON_TER         110
SQ   SEQUENCE   110 AA;  12184 MW;  3053B3371935623F CRC64;
     MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
     GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI