Abca4
entrez
11304
canonical
uniprot
O35600
canonical
ensembl
ENSMUSG00000028125
resolver
ensp
ENSMUSP00000013995
resolver
ensp
ENSMUSP00000143560
resolver
enst
ENSMUST00000013995
resolver
genesymbol
Abca4
resolver
genesymbol_syn
Abcr
resolver
uniprot_entry
ABCA4_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and ceramide. Phospholipids translocase activity is highly reduced by berylium fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid translocase activity. {ECO:0000250|UniProtKB:P78363}.
uniprot
proteins
amino_acid_sequence
MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGLLPWLQGIFCNMNNPCFQNPTPGESPGTVSNYNNSILARVYRDFQELFMDTPEVQHLGQVWAELRTLSQFMDTLRTHPERFAGRGLQIRDILKDEEALTLFLMRNIGLSDSVAHLLVNSQVRVEQFAYGVPDLELTDIACSEALLQRFIIFSQRRGAQTVRDALCPLSQVTLQWIEDTLYADVDFFKLFHVLPTLLDSSSQGINLRFWGGILSDLSPRMQKFIHRPSVQDLLWVSRPLLQNGGPETFTQLMSILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPAYSYDKRTTSFCNSLIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRIMKNANSTFEELDRVRKLVKAWEEVGPQIWYFFEKSTQMTVIRDTLQHPTVKDFINRQLGEEGITTEAVLNFFSNGPQEKQADDMTSFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPGMYPWASSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGIVKSQMQAEPPIGVYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKGIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMALSIFLLTLFIMHGRILHYSDPFILFLFLLAFATATIMQSFLLSTLFSKASLAAACSGVIYFTLYLPHVLCFAWQDRMTADLKTTVSLLSSVAFGFGTEYLVRFEEQGLGLQWSNIGKSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGMNDSFFERELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGVCSCTSKGFSTRCPTRVDEITEEQVLDGDVQELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDAGAGSMFVGGAQQKREQAGLRHPCSAPTEKLRQYAQAPHTCSPGQVDPPKGQPSPEPEDPGVPFNTGARLILQHVQALLVKRFHHTIRSRKDFVAQIVLPATFVFLALMLSIIVPPFGEFPALTLHPWMYGHQYTFFSMDEPNNEHLEVLADVLLNRPGFGNRCLKEEWLPEYPCINATSWKTPSVSPNITHLFQKQKWTAAHPSPSCKCSTREKLTMLPECPEGAGGLPPPQRTQRSTEVLQDLTNRNISDYLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPISGEALVGFLSGLGQMMNVSGGPVTREASKEMLDFLKHLETTDNIKVWFNNKGWHALVSFLNVAHNAILRASLPRDRDPEEYGITVISQPLNLTKEQLSDITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVTKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPDNLPALVSLLMLYGWAVIPMMYPASFLFEVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEYSANPFQWDLIGKNLVAMAIEGVVYFLLTLLIQHHFFLTRWIAEPAREPVFDEDDDVAEERQRVMSGGNKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHHSMLQFQVPSSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDLPLHPRAAGASWQAKLEEKSGRLQTQEPLPAGSEQLANGSNPTAAEDKHTRSPQ
uniprot
proteins
ec_number
7.6.2.1
uniprot
proteins
function
FUNCTION: Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid (PubMed:10412977, PubMed:10852960, PubMed:22735453). Displays ATPase activity in vitro in absence of retinal substrate (By similarity). May display GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (By similarity). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (By similarity). {ECO:0000250|UniProtKB:F1MWM0, ECO:0000250|UniProtKB:P78363, ECO:0000269|PubMed:10412977, ECO:0000269|PubMed:10852960, ECO:0000269|PubMed:22735453}.
uniprot
proteins
mass_dalton
260209
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:F1MWM0}.; PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal fragment and a 115-kDa C-terminal fragment that are linked through disulfide bonds. {ECO:0000250|UniProtKB:F1MWM0}.; PTM: Phosphorylation is independent of light exposure and modulates ATPase activity. {ECO:0000250|UniProtKB:F1MWM0}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCA family
uniprot
proteins
pubmed
10412977
uniprot
proteins
pubmed
10852960
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22735453
uniprot
proteins
pubmed
9202155
uniprot
proteins
sequence_length
2310
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P78363}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9202155}. Note=Localized to the rim and incisures of rod outer segments disks. {ECO:0000269|PubMed:9202155}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 647..667; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 700..720; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 731..751; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 760..780; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 836..856; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1376..1396; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1727..1747; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1759..1779; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1792..1812; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1831..1851; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1873..1893; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins