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Chloride intracellular channel protein

 A0A0B8RY47_BOIIR        Unreviewed;       241 AA.
A0A0B8RY47;
01-APR-2015, integrated into UniProtKB/TrEMBL.
01-APR-2015, sequence version 1.
31-JAN-2018, entry version 12.
RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
Boiga irregularis (Brown tree snake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Colubridae; Colubrinae; Boiga.
NCBI_TaxID=92519 {ECO:0000313|EMBL:JAG68347.1};
[1] {ECO:0000313|EMBL:JAG68347.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Venom gland {ECO:0000313|EMBL:JAG68347.1};
PubMed=25476704; DOI=10.1186/1471-2164-15-1061;
McGivern J.J., Wray K.P., Margres M.J., Couch M.E., Mackessy S.P.,
Rokyta D.R.;
"RNA-seq and high-definition mass spectrometry reveal the complex and
divergent venoms of two rear-fanged colubrid snakes.";
BMC Genomics 15:1061-1061(2014).
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362009};
Single-pass membrane protein {ECO:0000256|RuleBase:RU362009}.
Cytoplasm {ECO:0000256|RuleBase:RU362009}.
-!- DOMAIN: Members of this family may change from a globular, soluble
state to a state where the N-terminal domain is inserted into the
membrane and functions as chloride channel. A conformation change
of the N-terminal domain is thought to expose hydrophobic surfaces
that trigger membrane insertion. {ECO:0000256|RuleBase:RU362009}.
-!- SIMILARITY: Belongs to the chloride channel CLIC family.
{ECO:0000256|RuleBase:RU362009}.
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EMBL; GBSH01000678; JAG68347.1; -; Transcribed_RNA.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
InterPro; IPR002946; CLIC.
InterPro; IPR030259; CLIC-1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR43920:SF2; PTHR43920:SF2; 1.
Pfam; PF13417; GST_N_3; 1.
PRINTS; PR01263; INTCLCHANNEL.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00862; O-ClC; 1.
PROSITE; PS50405; GST_CTER; 1.
3: Inferred from homology;
Chloride {ECO:0000256|RuleBase:RU362009};
Chloride channel {ECO:0000256|RuleBase:RU362009};
Cytoplasm {ECO:0000256|RuleBase:RU362009};
Ion channel {ECO:0000256|RuleBase:RU362009};
Ion transport {ECO:0000256|RuleBase:RU362009};
Transport {ECO:0000256|RuleBase:RU362009};
Voltage-gated channel {ECO:0000256|RuleBase:RU362009}.
DOMAIN 70 235 GST C-terminal.
{ECO:0000259|PROSITE:PS50405}.
UNSURE 141 141 D or N. {ECO:0000313|EMBL:JAG68347.1}.
SEQUENCE 241 AA; 27130 MW; F6EC71C08FCDE0D8 CRC64;
MAEEKPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTEAVQKLCP
GGQLPFLMYG TEVHTDTNKV EEFLEEVLCP PKYPKLAANN PESNTAGLDV FAKFSAYIKN
SNPSLNANLE KGLLKALKVL DVYLMTPQPE EVDENSAEDE GQSNRKFLDG NELTLADCNL
LPKLHIVKVV CKKYRDFTIP EEFRGIHRYL KNAYAREEFS STCPDDEEIE LAYELVAKAL
K


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