BEST1
entrez
7439
canonical
uniprot
O76090
canonical
ensembl
ENSG00000167995
resolver
ensp
ENSP00000367282
resolver
ensp
ENSP00000399709
resolver
ensp
ENSP00000432681
resolver
ensp
ENSP00000677353
resolver
ensp
ENSP00000786951
resolver
enst
ENST00000524926
resolver
genesymbol
BEST1
resolver
genesymbol_syn
VMD2
resolver
hgnc
HGNC:12703
resolver
uniprot
A0A0C4DGE9
resolver
uniprot
A0A0S2Z4M4
resolver
uniprot
A0A0S2Z579
resolver
uniprot
A8K0W6
resolver
uniprot
B7Z375
resolver
uniprot
B7Z3J8
resolver
uniprot
B7Z736
resolver
uniprot
E9PDT5
resolver
uniprot
O75904
resolver
uniprot
Q53YQ9
resolver
uniprot
Q8IUR9
resolver
uniprot
Q8IZ80
resolver
uniprot_entry
A0A0C4DGE9_HUMAN
resolver
uniprot_entry
A0A0S2Z4M4_HUMAN
resolver
uniprot_entry
A0A0S2Z579_HUMAN
resolver
uniprot_entry
B7Z375_HUMAN
resolver
uniprot_entry
BEST1_HUMAN
resolver
uniprot_sec
A8K0W6
resolver
uniprot_sec
B7Z3J8
resolver
uniprot_sec
B7Z736
resolver
uniprot_sec
E9PDT5
resolver
uniprot_sec
O75904
resolver
uniprot_sec
Q53YQ9
resolver
uniprot_sec
Q8IUR9
resolver
uniprot_sec
Q8IZ80
resolver
activity_regulation
ACTIVITY REGULATION: Inactivated by sulfhydryl-reactive agents. {ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679}.
uniprot
proteins
amino_acid_sequence
MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS
uniprot
proteins
disease_involvement
DISEASE: Macular dystrophy, vitelliform, 2 (VMD2) [MIM:153700]: An autosomal dominant form of macular degeneration that usually begins in childhood or adolescence. VMD2 is characterized by typical 'egg-yolk' macular lesions due to abnormal accumulation of lipofuscin within and beneath the retinal pigment epithelium cells. Progression of the disease leads to destruction of the retinal pigment epithelium and vision loss. {ECO:0000269|PubMed:10331951, ECO:0000269|PubMed:10394929, ECO:0000269|PubMed:10453731, ECO:0000269|PubMed:10682987, ECO:0000269|PubMed:10798642, ECO:0000269|PubMed:10854112, ECO:0000269|PubMed:11241846, ECO:0000269|PubMed:11449320, ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12187431, ECO:0000269|PubMed:12324875, ECO:0000269|PubMed:13129869, ECO:0000269|PubMed:14517959, ECO:0000269|PubMed:15176385, ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:18400985, ECO:0000269|PubMed:18766995, ECO:0000269|PubMed:19357557, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:9662395, ECO:0000269|PubMed:9700209}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 50 (RP50) [MIM:613194]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:19853238}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bestrophinopathy, autosomal recessive (ARB) [MIM:611809]: A retinopathy characterized by loss of central vision, an absent electro-oculogram light rise, and electroretinogram anomalies. {ECO:0000269|PubMed:18179881, ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502, ECO:0000269|PubMed:26720466}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Vitreoretinochoroidopathy (VRCP) [MIM:193220]: An autosomal dominant ocular disorder characterized by vitreoretinochoroidal dystrophy. The clinical presentation is variable. VRCP may be associated with cataract, nanophthalmos, microcornea, shallow anterior chamber, and glaucoma. {ECO:0000269|PubMed:15452077}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Allows the movement of chloride and hydrogencarbonate (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Found in a partially open conformation leading to significantly smaller chloride movement (PubMed:35789156). Upon F2R/PAR-1 activation, the sequestered calcium is released into the cytosol of astrocytes, leading to the (Ca2+)-dependent release of L-glutamate into the synaptic cleft that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). Upon activation of the norepinephrine-alpha-1 adrenergic receptor signaling pathway, transports as well D-serine than L-glutamate in a (Ca2+)-dependent manner, leading to activation of adjacent NMDAR receptors and therefore regulates the heterosynaptic long-term depression and metaplasticity during initial memory acquisition (By similarity). Releases the 4-aminobutanoate neurotransmitter in a (Ca2+)-dependent manner, and participates in its tonic release from cerebellar glial cells (By similarity). {ECO:0000250|UniProtKB:O88870, ECO:0000269|PubMed:11904445, ECO:0000269|PubMed:12907679, ECO:0000269|PubMed:18179881, ECO:0000269|PubMed:18400985, ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502, ECO:0000269|PubMed:26720466, ECO:0000269|PubMed:35789156}.
uniprot
proteins
mass_dalton
67684
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="C->A: Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-42; A-69; A-221 and A-251."; /evidence="ECO:0000269|PubMed:11904445"; MUTAGEN 42; /note="C->A: Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-23; A-69; A-221 and A-251."; /evidence="ECO:0000269|PubMed:11904445"; MUTAGEN 69; /note="C->A: Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-23; A-42; A-221 and A-251."; /evidence="ECO:0000269|PubMed:11904445"; MUTAGEN 221; /note="C->A: Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-23; A-42; A-69 and A-251."; /evidence="ECO:0000269|PubMed:11904445"; MUTAGEN 251; /note="C->A: Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-23; A-42; A-69 and A-221."; /evidence="ECO:0000269|PubMed:11904445
uniprot
proteins
protein_family
Anion channel-forming bestrophin (TC 1.A.46) family
uniprot
proteins
protein_family
Calcium-sensitive chloride channel subfamily
uniprot
proteins
pubmed
10331951
uniprot
proteins
pubmed
10394929
uniprot
proteins
pubmed
10453731
uniprot
proteins
pubmed
10682987
uniprot
proteins
pubmed
10766140
uniprot
proteins
pubmed
10798642
uniprot
proteins
pubmed
10854112
uniprot
proteins
pubmed
11241846
uniprot
proteins
pubmed
11449320
uniprot
proteins
pubmed
11904445
uniprot
proteins
pubmed
12187431
uniprot
proteins
pubmed
12324875
uniprot
proteins
pubmed
12907679
uniprot
proteins
pubmed
13129869
uniprot
proteins
pubmed
14517959
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15176385
uniprot
proteins
pubmed
15452077
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17110374
uniprot
proteins
pubmed
18179881
uniprot
proteins
pubmed
18400985
uniprot
proteins
pubmed
18766995
uniprot
proteins
pubmed
19357557
uniprot
proteins
pubmed
19853238
uniprot
proteins
pubmed
21330666
uniprot
proteins
pubmed
26200502
uniprot
proteins
pubmed
26720466
uniprot
proteins
pubmed
29121962
uniprot
proteins
pubmed
35789156
uniprot
proteins
pubmed
9662395
uniprot
proteins
pubmed
9700209
uniprot
proteins
sequence_length
585
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Basolateral cell membrane {ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Note=Localized at the surface membrane of microdomains adjacent to glutamatergic synapses. {ECO:0000250|UniProtKB:O88870}.
uniprot
proteins
transmembrane_region
TRANSMEM 32..51; /note="Helical"; /evidence="ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156"; TRANSMEM 61..82; /note="Helical"; /evidence="ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156"; TRANSMEM 238..255; /note="Helical"; /evidence="ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156"; TRANSMEM 275..288; /note="Helical"; /evidence="ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156
uniprot
proteins