ID   BEST1_PIG               Reviewed;         428 AA.
AC   Q8WMR7;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Bestrophin-1;
DE   AltName: Full=Vitelliform macular dystrophy protein 2 homolog;
DE   Flags: Fragment;
GN   Name=BEST1; Synonyms=VMD2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPP2CB AND PPP2R1B,
RP   PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12058047; DOI=10.1074/jbc.m204269200;
RA   Marmorstein L.Y., McLaughlin P.J., Stanton J.B., Yan L., Crabb J.W.,
RA   Marmorstein A.D.;
RT   "Bestrophin interacts physically and functionally with protein phosphatase
RT   2A.";
RL   J. Biol. Chem. 277:30591-30597(2002).
CC   -!- FUNCTION: Forms calcium-sensitive chloride channels. Permeable to
CC       bicarbonate (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer or pentamers. May interact with PPP2CB and PPP2R1B
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Basolateral cell membrane {ECO:0000250}.
CC   -!- PTM: Phosphorylated (in vitro) by PP2A. {ECO:0000269|PubMed:12058047}.
CC   -!- SIMILARITY: Belongs to the bestrophin family. {ECO:0000305}.
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DR   EMBL; AY064707; AAL40882.1; -; mRNA.
DR   AlphaFoldDB; Q8WMR7; -.
DR   SMR; Q8WMR7; -.
DR   CORUM; Q8WMR7; -.
DR   STRING; 9823.ENSSSCP00000025663; -.
DR   PaxDb; Q8WMR7; -.
DR   PeptideAtlas; Q8WMR7; -.
DR   eggNOG; KOG3547; Eukaryota.
DR   InParanoid; Q8WMR7; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR033041; Best1.
DR   InterPro; IPR000615; Bestrophin.
DR   InterPro; IPR021134; Bestrophin/UPF0187.
DR   PANTHER; PTHR10736; PTHR10736; 1.
DR   PANTHER; PTHR10736:SF4; PTHR10736:SF4; 1.
DR   Pfam; PF01062; Bestrophin; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Chloride; Chloride channel; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           <1..428
FT                   /note="Bestrophin-1"
FT                   /id="PRO_0000143117"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        76..96
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          263..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   428 AA;  48499 MW;  3E6591B2BCDB6383 CRC64;
     PQHLVKAGFM TPSEHKHLEK LSLPHNSFWM PWVWFANLST KAWIGGRIRD PVLLQSLLDE
     MNTLRTQCGH LYAYDWISVP LVYTQVVTVA VYSFFLACLV GRQFLNPAKA YPGHEMDLVV
     PLFTFLQFFF YAGWLKVAEQ LINPFGEDDD DFETNWIVDR SLQVSLSAVD EMHHDLPPME
     RDMYWNDPEP HPPYTAASAQ SRRPSFFGST FNISLGKEDM EFQPEEEEEA HTGILGHFLG
     LQSSDHQPPR TNSKTKLLWP KKEGHFHEGH PKNLRGARLD SSDQEDSKAW REGGFKSAAL
     CGRPGYHSAP QTPLGHTPMV FPPEESAPLG LRRVSGIDEA AKDQSLQPAT PSIKKSFELL
     PESAEASAEP LQGSHVRRKT VEFNLADLSE APEHLKEPNL EPPMGIHAIL KDHRDPYWAL
     ENRDEAHS