CLIC4_BOVIN
ID CLIC4_BOVIN Reviewed; 253 AA.
AC Q9XSA7; Q3ZBJ4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chloride intracellular channel protein 4;
DE AltName: Full=Intracellular chloride ion channel protein p64H1;
GN Name=CLIC4;
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].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-253.
RC TISSUE=Retina;
RX PubMed=10191309; DOI=10.1523/jneurosci.19-08-02919.1999;
RA Chuang J.Z., Milner T.A., Zhu M., Sung C.H.;
RT "A 29 kDa intracellular chloride channel p64H1 is associated with large
RT dense-core vesicles in rat hippocampal neurons.";
RL J. Neurosci. 19:2919-2928(1999).
CC -!- FUNCTION: Can insert into membranes and form chloride ion channels.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=Exists both as soluble
CC cytoplasmic protein and as membrane protein with probably a single
CC transmembrane domain. {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; BC103261; AAI03262.1; -; mRNA.
DR EMBL; AF109198; AAD26138.1; -; mRNA.
DR RefSeq; NP_001073687.1; NM_001080218.2.
DR AlphaFoldDB; Q9XSA7; -.
DR SMR; Q9XSA7; -.
DR STRING; 9913.ENSBTAP00000048950; -.
DR PaxDb; Q9XSA7; -.
DR PeptideAtlas; Q9XSA7; -.
DR PRIDE; Q9XSA7; -.
DR Ensembl; ENSBTAT00000054397; ENSBTAP00000048950; ENSBTAG00000009470.
DR GeneID; 286823; -.
DR KEGG; bta:286823; -.
DR CTD; 25932; -.
DR VEuPathDB; HostDB:ENSBTAG00000009470; -.
DR VGNC; VGNC:27442; CLIC4.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000155017; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q9XSA7; -.
DR OMA; CHQIFMI; -.
DR OrthoDB; 974249at2759; -.
DR TreeFam; TF315438; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009470; Expressed in omental fat pad and 108 other tissues.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0007035; P:vacuolar acidification; IEA:Ensembl.
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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR45476:SF1; PTHR45476:SF1; 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; Chloride; Chloride channel; Cytoplasm; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; 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_0000144209"
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"
FT CONFLICT 100
FT /note="C -> F (in Ref. 2; AAD26138)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> R (in Ref. 2; AAD26138)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="K -> E (in Ref. 2; AAD26138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28727 MW; 408F7B7A7892DE74 CRC64;
MALSMPLNGL KEEDKEPIIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVTTVDLK
RKPADLQNLA PGTHPPFITF NNEVKTDVNK IEEFLEEVLC PPKYLKLSPK HPESNTAGMD
IFAKFSAYIK NSRPEANEAL ERGLLKTLQK LDEYLNSPLP DEIDENSMED IKFSTRKFLD
GNEMTLADCN LLPKLHIVKV VAKKYRNFDI PKGMTGIWRY LTNAYSRDEF TNTCPSDKEV
EIAYSDVAKR LTK
