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BEST3_MOUSE
ID   BEST3_MOUSE             Reviewed;         669 AA.
AC   Q6H1V1;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Bestrophin-3;
DE   AltName: Full=Vitelliform macular dystrophy 2-like protein 3;
GN   Name=Best3; Synonyms=Vmd2l3;
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=Heart;
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).
CC   -!- FUNCTION: Forms calcium-sensitive chloride channels. Permeable to
CC       bicarbonate (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the bestrophin family. {ECO:0000305}.
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DR   EMBL; AY450426; AAS09921.1; -; mRNA.
DR   CCDS; CCDS24188.1; -.
DR   RefSeq; NP_001007584.1; NM_001007583.1.
DR   AlphaFoldDB; Q6H1V1; -.
DR   SMR; Q6H1V1; -.
DR   STRING; 10090.ENSMUSP00000020378; -.
DR   TCDB; 1.A.46.1.4; the anion channel-forming bestrophin (bestrophin) family.
DR   PhosphoSitePlus; Q6H1V1; -.
DR   PaxDb; Q6H1V1; -.
DR   PRIDE; Q6H1V1; -.
DR   ProteomicsDB; 265208; -.
DR   Antibodypedia; 29432; 303 antibodies from 26 providers.
DR   DNASU; 382427; -.
DR   Ensembl; ENSMUST00000020378; ENSMUSP00000020378; ENSMUSG00000020169.
DR   GeneID; 382427; -.
DR   KEGG; mmu:382427; -.
DR   UCSC; uc007hcp.1; mouse.
DR   CTD; 144453; -.
DR   MGI; MGI:3580298; Best3.
DR   VEuPathDB; HostDB:ENSMUSG00000020169; -.
DR   eggNOG; KOG3547; Eukaryota.
DR   GeneTree; ENSGT00940000157777; -.
DR   HOGENOM; CLU_018069_5_1_1; -.
DR   InParanoid; Q6H1V1; -.
DR   OMA; DWLWNYE; -.
DR   OrthoDB; 279144at2759; -.
DR   PhylomeDB; Q6H1V1; -.
DR   TreeFam; TF315803; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 382427; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Best3; mouse.
DR   PRO; PR:Q6H1V1; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q6H1V1; protein.
DR   Bgee; ENSMUSG00000020169; Expressed in hindlimb stylopod muscle and 27 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; IDA:MGI.
DR   GO; GO:0015698; P:inorganic anion transport; IDA:MGI.
DR   GO; GO:0043271; P:negative regulation of ion transport; IDA:MGI.
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..669
FT                   /note="Bestrophin-3"
FT                   /id="PRO_0000143122"
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..669
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          399..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  76431 MW;  83E66FD62BA492A9 CRC64;
     MTVTYSSKVA NATFFGFHRL LLKWRGSIYK LLYREFIVFA VLYTAISLVY RLLLTGAQKR
     YFEKLSIYCD RYAEQIPVTF VLGFYVTLVV NRWWNQFVNL PWPDRLMLLI SSSVHGSDQH
     GRLLRRTLMR YVNLTSLLIF RSVSTAVYKR FPTMDHVVEA GFMTADERKL FDHLKSPHLK
     YWVPFIWFGN LATKARNEGR IRDSVDLQSL MTEMNRYRSW CSLLFGYDWV GIPLVYTQVV
     TLAVYTFFFA CLIGRQFLDP TKGYVGHDLD LYVPIFTLLQ FFFYAGWLKV AEQLINPFGE
     DDDDFETNWC IDRNLQVSLL AVDEMHMSLP KMKKDIYWDD SAARPPYTLA AADYCIPSFL
     GSTIQMGLSG SNFPAEDWLW NYEKHGNRHS VMRRVKRFLS THEHPGSPRR RRSFGRQASD
     SSMFLPPSPA RDLLDVPSRN PHRGSPTRKQ SRSQEGSPKL HSSMGELSTI RETSRTSTLQ
     SLSPQSSVRS SPTKMPQVPE VLITAAEAPA FSADSHQHDS TTSILSLEFT GVQPSGTEQQ
     VEPSGTPPGD PNPQTTSAST ERDLFKFEED LEDDRFPKRW SLPEFLESRH TSLGNLGPDP
     VSPRDALLLP DTETPSETNG IHPGAGSALA PDILYLMESL DKETDILEFN NEHTGESPKG
     TPQRPRTWF
 
 
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