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Bestrophin homolog

 E1C3A0_CHICK            Unreviewed;       692 AA.
E1C3A0;
02-NOV-2010, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 3.
25-OCT-2017, entry version 50.
RecName: Full=Bestrophin homolog {ECO:0000256|RuleBase:RU363126};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000011669, ECO:0000313|Proteomes:UP000000539};
[1] {ECO:0000313|Ensembl:ENSGALP00000011669}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000011669};
PubMed=15592404; DOI=10.1038/nature03154;
International Chicken Genome Sequencing Consortium;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2] {ECO:0000213|PDB:4RDQ}
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 2-405 IN COMPLEX WITH
CALCIUM, AND DISULFIDE BONDS.
PubMed=25337878; DOI=10.1038/nature13913;
Kane Dickson V., Pedi L., Long S.B.;
"Structure and insights into the function of a Ca(2+)-activated Cl(-)
channel.";
Nature 516:213-218(2014).
[3] {ECO:0000213|PDB:5T5N}
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-405, AND DISULFIDE BONDS.
PubMed=27821745; DOI=10.1073/pnas.1614688113;
Vaisey G., Miller A.N., Long S.B.;
"Distinct regions that control ion selectivity and calcium-dependent
activation in the bestrophin ion channel.";
Proc. Natl. Acad. Sci. U.S.A. 113:E7399-E7408(2016).
[4] {ECO:0000313|Ensembl:ENSGALP00000011669}
IDENTIFICATION.
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000011669};
Ensembl;
Submitted (MAR-2016) to UniProtKB.
-!- FUNCTION: Forms chloride channels.
{ECO:0000256|RuleBase:RU363126}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000256|RuleBase:RU363126}; Multi-pass membrane protein
{ECO:0000256|RuleBase:RU363126}.
-!- SIMILARITY: Belongs to the bestrophin family.
{ECO:0000256|RuleBase:RU363126}.
-!- CAUTION: The sequence shown here is derived from an Ensembl
automatic analysis pipeline and should be considered as
preliminary data. {ECO:0000313|Ensembl:ENSGALP00000011669}.
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EMBL; AADN04000300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PDB; 4RDQ; X-ray; 2.85 A; A/B/C/D/E=2-405.
PDB; 5T5N; X-ray; 3.10 A; A/B/C/D/E=2-405.
PDBsum; 4RDQ; -.
PDBsum; 5T5N; -.
SMR; E1C3A0; -.
DIP; DIP-61344N; -.
TCDB; 1.A.46.1.6; the anion channel-forming bestrophin (bestrophin) family.
Ensembl; ENSGALT00000011683; ENSGALP00000011669; ENSGALG00000007217.
GeneTree; ENSGT00390000002997; -.
InParanoid; E1C3A0; -.
OrthoDB; EOG091G06XO; -.
TreeFam; TF315803; -.
Reactome; R-GGA-2672351; Stimuli-sensing channels.
Proteomes; UP000000539; Chromosome 5.
Bgee; ENSGALG00000007217; -.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
InterPro; IPR033041; Best1.
InterPro; IPR000615; Bestrophin.
InterPro; IPR021134; Bestrophin/UPF0187.
PANTHER; PTHR10736; PTHR10736; 1.
PANTHER; PTHR10736:SF4; PTHR10736:SF4; 1.
Pfam; PF01062; Bestrophin; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:4RDQ, ECO:0000213|PDB:5T5N};
Calcium {ECO:0000213|PDB:4RDQ, ECO:0000213|PDB:5T5N};
Cell membrane {ECO:0000256|RuleBase:RU363126};
Chloride {ECO:0000256|RuleBase:RU363126};
Chloride channel {ECO:0000256|RuleBase:RU363126};
Complete proteome {ECO:0000313|Proteomes:UP000000539};
Ion channel {ECO:0000256|RuleBase:RU363126};
Ion transport {ECO:0000256|RuleBase:RU363126};
Membrane {ECO:0000256|RuleBase:RU363126};
Metal-binding {ECO:0000213|PDB:4RDQ, ECO:0000213|PDB:5T5N};
Reference proteome {ECO:0000313|Proteomes:UP000000539};
Transmembrane {ECO:0000256|RuleBase:RU363126};
Transmembrane helix {ECO:0000256|RuleBase:RU363126};
Transport {ECO:0000256|RuleBase:RU363126}.
TRANSMEM 31 54 Helical. {ECO:0000256|RuleBase:RU363126}.
TRANSMEM 75 95 Helical. {ECO:0000256|RuleBase:RU363126}.
TRANSMEM 235 257 Helical. {ECO:0000256|RuleBase:RU363126}.
METAL 10 10 Calcium 1; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 10 10 Calcium 2; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 293 293 Calcium 1; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ}.
METAL 293 293 Calcium 2; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ}.
METAL 296 296 Calcium 1; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 296 296 Calcium 2; via carbonyl oxygen.
{ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 301 301 Calcium 1. {ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 301 301 Calcium 2. {ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 304 304 Calcium 1. {ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
METAL 304 304 Calcium 2. {ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
DISULFID 135 185 {ECO:0000213|PDB:4RDQ,
ECO:0000213|PDB:5T5N}.
SEQUENCE 692 AA; 78428 MW; 829A3613D361DA04 CRC64;
MTVTYTNRVA DARLGTFSQL LLQWKGSIYK LLYSEFLIFI SLYFAISLVY RLILSESQRL
MFEKLALYCN SYAELIPVSF VLGFYVSLVV SRWWAQYESI PWPDRIMNLV SCNVDGEDEY
GRLLRRTLMR YSNLCSVLIL RSVSTAVYKR FPSMEHVVRA GLMTPEEHKK FESLNSPHNK
FWIPCVWFSN LAVKARNEGR IRDSVLLQGI LNELNTLRSQ CGRLYGYDWI SIPLVYTQVV
TVAVYSFFLA CLIGRQFLDP EKAYPGHELD LFVPVFTFLQ FFFYAGWLKV AEQLINPFGE
DDDDFETNWL IDRNLQVSLM AVDEMHQDLP ILEKDLYWNE PDPQPPYTAA TAEYKRPSFL
GSTFDISMQK EEMEFQPLEQ IKENEEANHS TPLLGHLGRL LGVQSPSFSR SSSRMNLLRR
RGEPTSPFSH YTYQDMGKSG NISHPRGDTN SQEKLREFDA FISTPFYERP GFYSAPQTPI
SSIPMIFPSR RQGRKKPPAL SSIAACSNSL KDSSLGSGAK ETFIWPTERN KGPDSLVVMV
EEEKSNSSSK KSPDHEQQGS FKSLKSLKGS HPPWLTLENA ATTTSNCEQS SAFPQPGNIP
PSSSTSFCFS FTPVASPVLE RSPIGNREVS RSGRDTASRS SNAPPTRETR RAESPSTNDS
GISLAEGDYV GLMEVIMEAS ESVCEEQMDQ CS


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