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Database: UniProt
Entry: H3B2P3_LATCH
LinkDB: H3B2P3_LATCH
Original site: H3B2P3_LATCH 
ID   H3B2P3_LATCH            Unreviewed;       251 AA.
AC   H3B2P3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
GN   Name=CLIC5 {ECO:0000313|Ensembl:ENSLACP00000016164.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016164.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000016164.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362009}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362009}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU362009}.
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. {ECO:0000256|RuleBase:RU362009}.
CC   -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC       {ECO:0000256|ARBA:ARBA00007655, ECO:0000256|RuleBase:RU362009}.
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DR   EMBL; AFYH01096713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01096722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005998876.1; XM_005998814.2.
DR   AlphaFoldDB; H3B2P3; -.
DR   Ensembl; ENSLACT00000016276.1; ENSLACP00000016164.1; ENSLACG00000014238.2.
DR   GeneID; 102350369; -.
DR   KEGG; lcm:102350369; -.
DR   CTD; 53405; -.
DR   GeneTree; ENSGT00940000156406; -.
DR   OrthoDB; 103277at2759; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000014238; Expressed in muscle tissue and 5 other cell types or tissues.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   CDD; cd03061; GST_N_CLIC; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002946; CLIC.
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   NCBIfam; TIGR00862; O-ClC; 1.
DR   PANTHER; PTHR45476:SF4; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 5; 1.
DR   PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PRINTS; PR01263; INTCLCHANNEL.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU362009};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173,
KW   ECO:0000256|RuleBase:RU362009}; Cytoplasm {ECO:0000256|RuleBase:RU362009};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU362009};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362009}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU362009};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU362009}.
FT   DOMAIN          78..244
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   251 AA;  28180 MW;  1565EC98D2B5AC05 CRC64;
     MTDSAPTNGN EKDPEIELFV KAGIDGESIG NCPFSQRLFM ILWLKGVVFN VTTVDLKRKP
     ADLHNLAPGT HPPFLTFNGE VKTDINKIEE FLEEILSPPK YPKLAAKHHE SNTAGNDIFA
     KFSAYIKNTK PEANGSLEKG LLKTLKKLDD YLNSPLPEEI DADSAEDEKV SKRKFLDGDE
     LTLADCNLLP KLHIVKIVAK KYRNFEMPSE MTGVWRYLKN AYARDEFTNT CAADKEIEQA
     YADVAKRLSK S
//
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