BST15_CAEEL
ID BST15_CAEEL Reviewed; 525 AA.
AC Q21973;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bestrophin homolog 15;
DE AltName: Full=Bestrophin-1;
DE Short=ceBest1;
GN Name=best-15; ORFNames=R13.3;
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], FUNCTION, AND SUBUNIT.
RX PubMed=11904445; DOI=10.1073/pnas.052692999;
RA Sun H., Tsunenari T., Yau K.-W., Nathans J.;
RT "The vitelliform macular dystrophy protein defines a new family of chloride
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4008-4013(2002).
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).
CC -!- FUNCTION: Forms chloride channels. {ECO:0000269|PubMed:11904445}.
CC -!- SUBUNIT: Forms oligomers. {ECO:0000269|PubMed:11904445}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the bestrophin family. {ECO:0000305}.
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DR EMBL; AY515708; AAR99658.1; -; mRNA.
DR EMBL; Z73105; CAA97442.2; -; Genomic_DNA.
DR PIR; T24210; T24210.
DR RefSeq; NP_502007.2; NM_069606.6.
DR AlphaFoldDB; Q21973; -.
DR SMR; Q21973; -.
DR BioGRID; 43076; 1.
DR STRING; 6239.R13.3; -.
DR TCDB; 1.A.46.1.3; the anion channel-forming bestrophin (bestrophin) family.
DR PaxDb; Q21973; -.
DR PeptideAtlas; Q21973; -.
DR EnsemblMetazoa; R13.3.1; R13.3.1; WBGene00011258.
DR GeneID; 177975; -.
DR KEGG; cel:CELE_R13.3; -.
DR UCSC; R13.3; c. elegans.
DR CTD; 177975; -.
DR WormBase; R13.3; CE32919; WBGene00011258; best-15.
DR eggNOG; KOG3547; Eukaryota.
DR HOGENOM; CLU_018069_7_2_1; -.
DR InParanoid; Q21973; -.
DR OMA; QAPSEIN; -.
DR OrthoDB; 279144at2759; -.
DR PhylomeDB; Q21973; -.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR PRO; PR:Q21973; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011258; Expressed in adult organism and 2 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR InterPro; IPR000615; Bestrophin.
DR InterPro; IPR021134; Bestrophin/UPF0187.
DR PANTHER; PTHR10736; PTHR10736; 1.
DR Pfam; PF01062; Bestrophin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Chloride channel; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..525
FT /note="Bestrophin homolog 15"
FT /id="PRO_0000143123"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 525 AA; 60485 MW; 9E0A90D9523C3229 CRC64;
MTVNYNLDVS SASIFSFLRL QLRWKGSIWK YLLKELFMFI IAFITVSSVY RSNLIIGEKT
RKIWDNFAAL FDQNMDFIPL TFMLGFFVTI IVRRWNDIFA NLGWVENTAI TVANYIRGTD
DRTRMIRRNV IRYMVLAQVL VFRDCSIQVR KRFPTMESIV SAGFMLEHEK EALDNVQCGK
LQKYFVPIQW STGLLVDARA EGKIAADLLM NEIGKHIIEF RKMLALLSNY DWVPIPLAYP
QVVFLAVRSY FFMALIARQS VLLDGKEPEQ PSILYPTVPF VMSILQFIFV VGWMKVAESM
INPLGEDDDD FECNYLLDRN LMIGLCIVDD NYNRTPSVEK DAFWCADVEP LYSVETAMIP
KNPQIGSAAN YDVKVDEEEV MMMPHMDDVD LFDFESTNNL IPRKTFSVIS IQRPFGSRAS
LASRKRSMMF DQLRGRIAKK QHRSNMFQNS VSQASLHYFE SQAPSEINLS TLEMTAPKRK
SSTGKLGSMN VAEEQHKLSA EVLPIVIEED EERSKMLEKD KNKNA