BEST2_MOUSE
ID BEST2_MOUSE Reviewed; 508 AA.
AC Q8BGM5; Q6H1U9; Q8VCM0;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Bestrophin-2;
DE AltName: Full=Vitelliform macular dystrophy 2-like protein 1;
GN Name=Best2; Synonyms=Vmd2l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=15218265; DOI=10.1159/000078016;
RA Kraemer F., Stoehr H., Weber B.H.F.;
RT "Cloning and characterization of the murine Vmd2 RFP-TM gene family.";
RL Cytogenet. Genome Res. 105:107-114(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=18400985; DOI=10.1152/ajpcell.00398.2007;
RA Qu Z., Hartzell H.C.;
RT "Bestrophin Cl- channels are highly permeable to HCO3-.";
RL Am. J. Physiol. 294:C1371-C1377(2008).
CC -!- FUNCTION: Forms calcium-sensitive chloride channels. Permeable to
CC bicarbonate. {ECO:0000269|PubMed:18400985}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Mainly confined to the retinal pigment epithelium
CC and colon.
CC -!- SIMILARITY: Belongs to the bestrophin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH31186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH36157.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH36163.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY450428; AAS09923.1; -; mRNA.
DR EMBL; BC019528; AAH19528.1; ALT_INIT; mRNA.
DR EMBL; BC031186; AAH31186.1; ALT_INIT; mRNA.
DR EMBL; BC036157; AAH36157.2; ALT_INIT; mRNA.
DR EMBL; BC036163; AAH36163.2; ALT_INIT; mRNA.
DR CCDS; CCDS52621.1; -.
DR RefSeq; NP_001123666.1; NM_001130194.1.
DR RefSeq; XP_006530883.1; XM_006530820.1.
DR AlphaFoldDB; Q8BGM5; -.
DR SMR; Q8BGM5; -.
DR STRING; 10090.ENSMUSP00000053408; -.
DR PhosphoSitePlus; Q8BGM5; -.
DR PaxDb; Q8BGM5; -.
DR PRIDE; Q8BGM5; -.
DR ProteomicsDB; 273556; -.
DR DNASU; 212989; -.
DR GeneID; 212989; -.
DR KEGG; mmu:212989; -.
DR UCSC; uc009mov.1; mouse.
DR CTD; 54831; -.
DR MGI; MGI:2387588; Best2.
DR eggNOG; KOG3547; Eukaryota.
DR InParanoid; Q8BGM5; -.
DR OrthoDB; 279144at2759; -.
DR PhylomeDB; Q8BGM5; -.
DR TreeFam; TF315803; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 212989; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Best2; mouse.
DR PRO; PR:Q8BGM5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BGM5; protein.
DR GO; GO:0034707; C:chloride channel complex; IDA:BHF-UCL.
DR GO; GO:0005929; C:cilium; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IDA:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0006821; P:chloride transport; IDA:MGI.
DR GO; GO:0051899; P:membrane depolarization; IDA:HGNC-UCL.
DR GO; GO:0007608; P:sensory perception of smell; IEP:HGNC-UCL.
DR InterPro; IPR000615; Bestrophin.
DR InterPro; IPR021134; Bestrophin/UPF0187.
DR PANTHER; PTHR10736; PTHR10736; 1.
DR Pfam; PF01062; Bestrophin; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="Bestrophin-2"
FT /id="PRO_0000143119"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 229..249
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 455..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 462
FT /note="P -> S (in Ref. 1; AAS09923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 57023 MW; 8730B806F0576B3D CRC64;
MTVTYTARVA NARFGGFSQL LLLWRGSIYK LLWRELLCFL GLYMALSAAY RFLLAEEQKR
YFEKLVIYCD QYASLIPVSF VLGFYVTLVV HRWWNQYLCM PLPDALMCIV AGTVHGRDDR
GRLYRRTLMR YAGLSAVLIL RSVSTAVFKR FPTIDHVVEA GFMTREERKK FENLNSSYNK
YWVPCVWFSS LAAQARREGR IRDNSALKLL LEELNVFRSK CGMLFHYDWI SIPLVYTQVV
TIAVYSYFLA CLIGRQFLDP AQGYKDHTLD LCVPIFTLLQ FFFYAGWLKV AEQLINPFGE
DDDDFETNFL IDRNFQVSML AVDEMYDDLA MLEKDLYWDA AEARAPYTAA TAFLLQQPSF
QGSTFDIALA KEDMQFQRLD GVDGPLGEVH GDFLQRLLPA GAGSVGPLGR RLSLLRRKNS
CVSEASTAAS CGCAGAADGG GVECGCGDPL LDPSLREPEL EPPACPEPPA PIPGPTPEPF
TTVSIPGPRA PAPPWLPSPI GEEEESPA
