CLIC6_RABIT
ID CLIC6_RABIT Reviewed; 637 AA.
AC Q9N2G5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chloride intracellular channel protein 6;
DE AltName: Full=Parchorin;
GN Name=CLIC6;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 376-384; 410-419; 434-444;
RP 492-502; 510-514; 536-544 AND 600-611, CHARACTERIZATION, AND
RP PHOSPHORYLATION.
RC TISSUE=Choroid plexus;
RX PubMed=10753923; DOI=10.1074/jbc.275.15.11164;
RA Nishizawa T., Nagao T., Iwatsubo T., Forte J.G., Urushidani T.;
RT "Molecular cloning and characterization of a novel chloride intracellular
RT channel-related protein, parchorin, expressed in water-secreting cells.";
RL J. Biol. Chem. 275:11164-11173(2000).
CC -!- FUNCTION: May insert into membranes and form chloride ion channels. May
CC play a critical role in water-secreting cells, possibly through the
CC regulation of chloride ion transport.
CC -!- SUBUNIT: Interacts with dopamine receptors DRD2, DRD3 and DRD4.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}. Note=Predominantly cytoplasmic.
CC Upon chloride ion efflux from the cell, it is translocated to the
CC plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in brain, chorioretinal, lacrimal glands,
CC submandibular glands, airway epithelium, kidney and gastric mucosa,
CC where it is preferentially expressed in cells that secrete or transport
CC water. In brain, it is highly expressed in choroid plexus. Not detected
CC in pancreas, adrenal glands, heart, skeletal muscle, ileal mucosa,
CC liver and lung.
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 -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10753923}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AB035520; BAA94345.1; -; mRNA.
DR RefSeq; NP_001075473.1; NM_001082004.1.
DR AlphaFoldDB; Q9N2G5; -.
DR SMR; Q9N2G5; -.
DR PRIDE; Q9N2G5; -.
DR GeneID; 100008620; -.
DR KEGG; ocu:100008620; -.
DR CTD; 54102; -.
DR InParanoid; Q9N2G5; -.
DR OrthoDB; 974249at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; 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: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; 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 1: Evidence at protein level;
KW Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..637
FT /note="Chloride intracellular channel protein 6"
FT /id="PRO_0000144219"
FT TRANSMEM 422..442
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT REPEAT 155..160
FT /note="1"
FT REPEAT 161..166
FT /note="2"
FT REPEAT 167..172
FT /note="3"
FT REPEAT 173..178
FT /note="4"
FT REPEAT 179..184
FT /note="5"
FT REPEAT 185..190
FT /note="6"
FT REPEAT 191..196
FT /note="7"
FT REPEAT 197..202
FT /note="8"
FT REPEAT 203..208
FT /note="9"
FT REPEAT 209..214
FT /note="10"
FT REPEAT 215..220
FT /note="11"
FT REPEAT 221..226
FT /note="12"
FT REPEAT 227..232
FT /note="13"
FT REPEAT 233..238
FT /note="14"
FT REPEAT 239..244
FT /note="15"
FT DOMAIN 489..637
FT /note="GST C-terminal"
FT REGION 1..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..244
FT /note="15 X 6 AA tandem repeat of [GEA]-[DGR]-[SN]-[VIM]-D-
FT [AT]"
FT COMPBIAS 284..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q2"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q2"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q2"
SQ SEQUENCE 637 AA; 64919 MW; ECF59FCAFAB2C2AD CRC64;
MAETAEPEGG APSPQGPPEG SALLEERPGE PDPAGPEASE GAAKAPSGEG AGAAAKAGAT
EEASGGRDGE GAGEQAPDAG TESGGETPDA KGAQIEAEGA PEGTKAPQLG EEGSGGKQVE
ESGPDCELRG EAAREAEGQA AAPAAPGAQE EAVPGDSVDA EGSIDAGGSV DAAGSVDAGG
SIDAGGSMDA GGSVDAGGSI DTGGSVDAAG SVDAGGSIDT GRNVDAGGSI DAGGSVDAGG
SMDAEGPAGG AHGAGGEPQD LGAGSPQPRS EAVEVAAAEN EGHSPGESVE DAAAEEAAGT
REPEGSEDAA GEDGDQGRPQ EETEQQAERQ EPGPETQSEE EERPPDRSPD GEAAASTRAA
QPEAELSNHL AAEEGGQRGE GPANGRGEDG EASEEGDPGQ EHDITLFVKA GYDGESIGNC
PFSQRLFMIL WLKGVIFNVT TVDLKRKPAD LQNLAPGTNP PFMTFDGDVK TDVNKIEEFL
EEKLAPPRYP KLATQHPESN SAGNDVFAKF SAFIKNTKKD ANEIYEKSLL KALKKLDAYL
NSPLPDEVDA YSTEDVAVSG RKFLDGDDLT LADCNLLPKL HIIKIVAKKY RDFEFPPEMT
GIWRYLNNAY ARDEFINTCP ADQEIEHAYS DVAKRMK
