EXC4_CAEEL
ID EXC4_CAEEL Reviewed; 290 AA.
AC Q8WQA4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Chloride intracellular channel exc-4;
DE AltName: Full=Excretory canal abnormal protein 4;
GN Name=exc-4; ORFNames=Y105E8A.22;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DOMAIN, AND MUTAGENESIS OF LEU-46 AND PRO-238.
RC STRAIN=Bristol N2;
RX PubMed=14684823; DOI=10.1126/science.1087667;
RA Berry K.L., Buelow H.E., Hall D.H., Hobert O.;
RT "A C. elegans CLIC-like protein required for intracellular tube formation
RT and maintenance.";
RL Science 302:2134-2137(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=17985355; DOI=10.1002/prot.21704;
RA Littler D.R., Harrop S.J., Brown L.J., Pankhurst G.J., Mynott A.V.,
RA Luciani P., Mandyam R.A., Mazzanti M., Tanda S., Berryman M.A., Breit S.N.,
RA Curmi P.M.G.;
RT "Comparison of vertebrate and invertebrate CLIC proteins: the crystal
RT structures of Caenorhabditis elegans EXC-4 and Drosophila melanogaster
RT DmCLIC.";
RL Proteins 71:364-378(2008).
CC -!- FUNCTION: May insert into membranes and form chloride ion channels.
CC Involved in the formation of the excretory canal. Required to prevent
CC cystic lumenal expansions in the excretory cell. Not required for
CC formation of the initial tube, but is required for regulating the size
CC of the tube lumen as it grows. {ECO:0000269|PubMed:17985355}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17985355}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Note=Exists both as soluble cytoplasmic
CC protein and as membrane protein with probably a single transmembrane
CC domain. Localizes to various tubular membranes in distinct cell types,
CC including the lumenal membrane of the excretory tubes.
CC -!- TISSUE SPECIFICITY: Expressed in the secretory system, hypodermis,
CC vulva, pharyngeal muscle, rectal gland, tubular rectal epithelium
CC cells, and tubular neuronal support cells in the head and tail.
CC {ECO:0000269|PubMed:14684823}.
CC -!- DOMAIN: The N-terminal part (1-55) is necessary and sufficient for
CC translocation from the cytosol to the membrane.
CC {ECO:0000269|PubMed:14684823}.
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; AY308063; AAQ75554.1; -; mRNA.
DR EMBL; AL132876; CAD21669.2; -; Genomic_DNA.
DR RefSeq; NP_740950.2; NM_170954.2.
DR PDB; 2YV9; X-ray; 1.60 A; A/B=1-290.
DR PDBsum; 2YV9; -.
DR AlphaFoldDB; Q8WQA4; -.
DR SMR; Q8WQA4; -.
DR BioGRID; 38700; 16.
DR STRING; 6239.Y105E8A.22; -.
DR EPD; Q8WQA4; -.
DR PaxDb; Q8WQA4; -.
DR PeptideAtlas; Q8WQA4; -.
DR EnsemblMetazoa; Y105E8A.22.1; Y105E8A.22.1; WBGene00001365.
DR GeneID; 173314; -.
DR KEGG; cel:CELE_Y105E8A.22; -.
DR UCSC; Y105E8A.22; c. elegans.
DR CTD; 173314; -.
DR WormBase; Y105E8A.22; CE36222; WBGene00001365; exc-4.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000173425; -.
DR HOGENOM; CLU_061051_0_0_1; -.
DR InParanoid; Q8WQA4; -.
DR OMA; IHTCPED; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q8WQA4; -.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR EvolutionaryTrace; Q8WQA4; -.
DR PRO; PR:Q8WQA4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001365; Expressed in embryo and 3 other tissues.
DR GO; GO:0043296; C:apical junction complex; IDA:WormBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0002064; P:epithelial cell development; IMP:WormBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0035150; P:regulation of tube size; IMP:WormBase.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloride; Chloride channel; Cytoplasm; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..290
FT /note="Chloride intracellular channel exc-4"
FT /id="PRO_0000144221"
FT TRANSMEM 37..57
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT MUTAGEN 46
FT /note="L->P: Abolishes membrane localization."
FT /evidence="ECO:0000269|PubMed:14684823"
FT MUTAGEN 238
FT /note="P->L: In n2400; induces defects in tubular
FT morphology of the excretory canal."
FT /evidence="ECO:0000269|PubMed:14684823"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2YV9"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:2YV9"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2YV9"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YV9"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 116..139
FT /evidence="ECO:0007829|PDB:2YV9"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 154..177
FT /evidence="ECO:0007829|PDB:2YV9"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:2YV9"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:2YV9"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:2YV9"
SQ SEQUENCE 290 AA; 33703 MW; 59256CC9BFB165DE CRC64;
MAEAYQIQSN GDPQSKPLLE LYVKASGIDA RRIGADLFCQ EFWMELYALY EIGVARVEVK
TVNVNSEAFK KNFLGAQPPI MIEEEKELTY TDNREIEGRI FHLAKEFNVP LFEKDPSAEK
RIENLYRNFK LFLRAKVEFD KGKKEPSRVE DLPAQIKVHY NRVCEQLSNI DQLLSERKSR
YLLGNSMTEY DCELMPRLHH IRIIGLSLLG FDIPHNFTHL WAYILTAYRT AAFIESCPAD
QDIIHHYKEQ MNLFTNQRET LQSPTKTHTI PEKVLSDIRV KGLAPDVNVH
