CLIC4_PONAB
ID CLIC4_PONAB Reviewed; 253 AA.
AC Q5R957;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chloride intracellular channel protein 4;
GN Name=CLIC4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can insert into membranes and form poorly selective ion
CC channels that may also transport chloride ions. Channel activity
CC depends on the pH. Membrane insertion seems to be redox-regulated and
CC may occur only under oxydizing conditions. Promotes cell-surface
CC expression of HRH3. May play a role in angiogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with HRH3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Note=Exists both as soluble cytoplasmic
CC protein and as membrane protein with probably a single transmembrane
CC domain. Present in an intracellular vesicular compartment that likely
CC represent trans-Golgi network vesicles (By 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:0000305}.
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DR EMBL; CR859537; CAH91703.1; -; mRNA.
DR RefSeq; NP_001124560.1; NM_001131088.1.
DR AlphaFoldDB; Q5R957; -.
DR SMR; Q5R957; -.
DR STRING; 9601.ENSPPYP00000001982; -.
DR PRIDE; Q5R957; -.
DR GeneID; 100169733; -.
DR KEGG; pon:100169733; -.
DR CTD; 25932; -.
DR eggNOG; KOG1422; Eukaryota.
DR InParanoid; Q5R957; -.
DR OrthoDB; 974249at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030257; CLIC-4/6.
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; PTHR45476:SF1; PTHR45476:SF1; 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 Cytoplasmic vesicle; 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:Q9Y696"
FT CHAIN 2..253
FT /note="Chloride intracellular channel protein 4"
FT /id="PRO_0000236803"
FT TRANSMEM 37..57
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 104..244
FT /note="GST C-terminal"
FT REGION 2..101
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:Q9Y696"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y696"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y696"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB1"
FT MOD_RES 244
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q5"
SQ SEQUENCE 253 AA; 28759 MW; AFAE4114EF60FF64 CRC64;
MALSMPLNGL KEEDKEPLIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVSTVDLK
RKPADLQNLA PGTHPPFITF NSEVKTDVNK IEEFLEEVLC PPKYLKLSPK HPESNTAGMD
IFAKFSAYIK NSRPEANEAL ERGLLKTLQK LDEYLNSPLP DEIDENSMED IKFSTRKFLD
GDEMTLADCN LLPKLHIVKV VAKKYRNFDI PKEMTGIWRY LTNAYSRDEF TNTCPSDKEV
EIAYSDVAKR LTK
