F1MWM0 · ABCA4_BOVIN
- ProteinRetinal-specific phospholipid-transporting ATPase ABCA4
- GeneABCA4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2281 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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:10075733, PubMed:10767284, PubMed:20552428, PubMed:22735453, PubMed:24707049).
Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (PubMed:10767284).
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 (PubMed:15471866, PubMed:20552428, PubMed:22735453).
Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (PubMed:10767284).
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 (PubMed:15471866, PubMed:20552428, PubMed:22735453).
Catalytic activity
- ATP + H2O + N-all-trans-retinylidenephosphatidylethanolamine(out) = ADP + H+ + N-all-trans-retinylidenephosphatidylethanolamine(in) + phosphateThis reaction proceeds in the forward direction.
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) = ADP + H+ + N-11-cis-retinylidenephosphatidylethanolamine(in) + phosphateThis reaction proceeds in the forward direction.
Activity regulation
All-trans-retinal transport activity is reduced by EDTA chelation of Mg2+ (PubMed:22735453).
All-trans-retinal transport activity is inhibited by N-ethylmaleimide (NEM) (PubMed:22735453).
Phosphatidylethanolamine transport is strongly inhibited by beryllium fluoride and NEM (PubMed:22735453).
All-trans-retinal transport activity is inhibited by N-ethylmaleimide (NEM) (PubMed:22735453).
Phosphatidylethanolamine transport is strongly inhibited by beryllium fluoride and NEM (PubMed:22735453).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
278 μM | ATP (with a purified ABCA4) | |||||
33 μM | ATP | with ABCA4 reconstituted into brain lipid membrane | ||||
725 μM | ATP | reconstituted into brain lipid membrane, plus 80 uM all-trans-retinal | ||||
18 μM | ATP (with amiodarone) | |||||
400 μM | ATP | with all-trans-retinal | ||||
666 μM | ATP | with all-trans-retinal plus amiodarone | ||||
75 μM | ATP (with CHAPS-solubilized ABCA4) | |||||
32 μM | ATP | with ABCA4 reconstituted into soybean phospholipid | ||||
20 μM | ATP | with ABCA4 reconstituted into brain polar lipid | ||||
25 μM | ATP | with ABCA4 reconstituted into ROS phospholipid | ||||
112 μM | ATP | with CHAPS-solubilized ABCA4 60 uM all-trans-retinal | ||||
56 μM | ATP | with ABCA4 reconstituted into soybean phospholipid 60 uM all-trans-retinal | ||||
106 μM | ATP | with ABCA4 reconstituted into brain polar lipid 60 uM all-trans-retinal | ||||
75 μM | ATP | with ABCA4 reconstituted into ROS phospholipid 60 uM all-trans-retinal | ||||
0.02 mM | ATP | in the presence of 40 uM retinal |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
27 nmol/min/mg | (for ATP hydrolysis and with a purified ABCA4) | ||||
1.3 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into brain lipid membrane) | ||||
29 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into brain lipid membrane, plus 80 uM all-trans-retinal) | ||||
2 nmol/min/mg | (for ATP hydrolysis and with amiodarone as substrate) | ||||
20 nmol/min/mg | (for ATP hydrolysis and with all-trans-retinal as substrate) | ||||
50 nmol/min/mg | (for ATP hydrolysis and with all-trans-retinal and amiodarone as substrates) | ||||
190 nmol/min/mg | (for ATP hydrolysis and with CHAPS-solubilized ABCA4) | ||||
50 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into soybean phospholipid) | ||||
29 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into brain polar lipid) | ||||
202 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into ROS phospholipid) | ||||
402 nmol/min/mg | (for ATP hydrolysis and with CHAPS-solubilized ABCA4 and 60 uM all-trans-retinal) | ||||
110 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into soybean phospholipid and 60 uM all-trans-retinal) | ||||
171 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into brain polar lipid and 60 uM all-trans-retinal) | ||||
673 nmol/min/mg | (for ATP hydrolysis and with ABCA4 reconstituted into ROS phospholipid and 60 uM all-trans-retinal) | ||||
35.5 pmol/min/ug | toward all-trans-retinal (in liposome) | ||||
4.9 nmol/min/mg | towards all-trans-retinal (in rod outer segments) |
pH Dependence
Optimum pH is 8.
Features
Showing features for binding site, site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRetinal-specific phospholipid-transporting ATPase ABCA4
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionF1MWM0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Note: Localized to the rim and incisures of rod outer segments disks.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-24 | Cytoplasmic | ||||
Sequence: MGFARQIKLLLWKNWTLRKRQKIR | ||||||
Transmembrane | 25-45 | Helical | ||||
Sequence: FVVELVWPLSLFLVLIWLRNV | ||||||
Topological domain | 46-646 | Extracellular | ||||
Sequence: NPLYSKHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTAGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWRELRTLSQLMNTLRMHPERIAGRGIRIREVLKDDEMLTLFLVKNIGLSDSVVYLLVNSQVRPEQFARGVPDLMLKDIACSEALLERFLIFPQRRAAQTVRGSLCSLSQGTLQWMEDTLYANVDFFKLFHVFPRLLDSRSQGMNLRSWGRILSDMSPRIQEFIHRPSVQDLLWVTRPLVQTGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDERTTTFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPATRRILKNANSTFEELERVRKLVKVWEEVGPQIWYFFDKSTQMSMIRDTLENPTVKAFWNRQLGEEGITAEAVLNFLYNGPREGQADDVDNFNWRDIFNITDRALRLANQYLECLILDKFESYDDEFQLTQRALSLLEENRFWAGVVFPDMHPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEHGITRSQAQEEVPVGIYLQQMPYPCFVDDS | ||||||
Transmembrane | 647-667 | Helical | ||||
Sequence: FMIILNRCFPIFMVLAWIYSV | ||||||
Topological domain | 668-699 | Cytoplasmic | ||||
Sequence: SMTVKSIVLEKELRLKETLKNQGVSNRVIWCT | ||||||
Transmembrane | 700-720 | Helical | ||||
Sequence: WFLDSFSIMSMSICLLTIFIM | ||||||
Topological domain | 721-730 | Extracellular | ||||
Sequence: HGRILHYSNP | ||||||
Transmembrane | 731-751 | Helical | ||||
Sequence: FILFLFLLAFSIATIMQCFLL | ||||||
Topological domain | 752-759 | Cytoplasmic | ||||
Sequence: STFFSRAS | ||||||
Transmembrane | 760-780 | Helical | ||||
Sequence: LAAACSGVIYFTLYLPHILCF | ||||||
Topological domain | 781-835 | Extracellular | ||||
Sequence: AWQDRITADMKMAVSLLSPVAFGFGTEYLARFEEQGVGLQWSNIGNSPMEGDEFS | ||||||
Transmembrane | 836-856 | Helical | ||||
Sequence: FLMSMKMMLLDAALYGLLAWY | ||||||
Topological domain | 857-1374 | Cytoplasmic | ||||
Sequence: LDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPITEEMEDPEYPEGINDCFFERELPGLVPGVCVKNLVKIFEPYGRPAVDRLNITFYESQITAFLGHNGAGKTTTLSIMTGLLPPTSGTVLVGGKDIETNLDAIRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWDKAQLEMEAMLEDTGLHHKRNEEAQDLSGGVQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADILGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRRMKTIQSQGRGREATCSCASKGFSVRCPACAEAITPEQVLDGDVNELTDMVHHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDLDSGHLFAGGTQQKRENINLRHPCSGPSEKAGQTPQGSSSHPREPAAHPEGQPPPEREGHSRLNSGARLIVQHVQALLVKRFQHTIRSHKDFLAQ | ||||||
Transmembrane | 1375-1395 | Helical | ||||
Sequence: IVLPATFVFLALMLSLIIPPF | ||||||
Topological domain | 1396-1679 | Extracellular | ||||
Sequence: GEYPALTLHPWMYGQQYTFFSMDQLDSEWLSALADVLVNKPGFGNRCLKEEWLPEFPCGNSSPWKTPSVSPDVTHLLQQQKWTADQPSPSCRCSTREKLTMLPECPEGAGGLPPPQRIQRSTEILQDLTDRNVSDFLVKTYPALIRSSLKSKFWVNEQRYGGISVGGKLPAPPFTGEALVGFLSDLGQLMNVSGGPMTREAAKEMPAFLKQLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLHKDKNPEEYGITVISQPLNLTKEQLSEITVLTTSVDAV | ||||||
Transmembrane | 1680-1700 | Helical | ||||
Sequence: VAICVIFAMSFVPASFVLYLI | ||||||
Topological domain | 1701-1725 | Cytoplasmic | ||||
Sequence: QERVNKAKHLQFVSGVSPTTYWLTN | ||||||
Transmembrane | 1726-1746 | Helical | ||||
Sequence: FLWDIMNYTVSAALVVGIFIG | ||||||
Topological domain | 1747-1757 | Extracellular | ||||
Sequence: FQKKAYTSSEN | ||||||
Transmembrane | 1758-1778 | Helical | ||||
Sequence: LPALVALLMLYGWAVIPMMYP | ||||||
Topological domain | 1779-1790 | Cytoplasmic | ||||
Sequence: ASFLFDIPSTAY | ||||||
Transmembrane | 1791-1811 | Helical | ||||
Sequence: VALSCANLFIGINSSAITFVL | ||||||
Topological domain | 1812-1829 | Extracellular | ||||
Sequence: ELFENNRTLLRINAMLRK | ||||||
Transmembrane | 1830-1850 | Helical | ||||
Sequence: LLIIFPHFCLGRGLIDLALSQ | ||||||
Topological domain | 1851-1879 | Cytoplasmic | ||||
Sequence: AVTDVYARFGEEHSSNPFQWDLIGKNLAA | ||||||
Transmembrane | 1880-1900 | Helical | ||||
Sequence: MAVEGVVYFLLTLLIQYQFFF | ||||||
Topological domain | 1901-2281 | Extracellular | ||||
Sequence: SRWTTEPAKEPITDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTAVTSGDATVAGKSILTNISDVHQSMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIERVTNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIMGIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIRSPKDDLLPDLGPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFRLLVSHKDSLLIEEYSVTQTTLDQVFVNFAKQQNETYDLPLHPRAAGASRQAKEVDKGNSAPQG |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 901 | Decreases expression level. Affects subcellular location. | ||||
Sequence: T → A | ||||||
Mutagenesis | 1185 | Does not affect subcellular location. Does not affect expression level. Does not affect ATPase activity. Reduces the stimulating effect of all-trans-retinal on ATP hydrolysis. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1313 | Does not affect subcellular location. Does not affect expression level. Does not affect ATPase activity. Reduces the stimulating effect of all-trans-retinal on ATP hydrolysis. | ||||
Sequence: T → A | ||||||
Mutagenesis | 1317 | Does not affect subcellular location. Does not affect expression level. Affects both the basal and stimulated ATPase activity. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 255 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453425 | 1-2281 | Retinal-specific phospholipid-transporting ATPase ABCA4 | |||
Sequence: MGFARQIKLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNVNPLYSKHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTAGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWRELRTLSQLMNTLRMHPERIAGRGIRIREVLKDDEMLTLFLVKNIGLSDSVVYLLVNSQVRPEQFARGVPDLMLKDIACSEALLERFLIFPQRRAAQTVRGSLCSLSQGTLQWMEDTLYANVDFFKLFHVFPRLLDSRSQGMNLRSWGRILSDMSPRIQEFIHRPSVQDLLWVTRPLVQTGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDERTTTFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPATRRILKNANSTFEELERVRKLVKVWEEVGPQIWYFFDKSTQMSMIRDTLENPTVKAFWNRQLGEEGITAEAVLNFLYNGPREGQADDVDNFNWRDIFNITDRALRLANQYLECLILDKFESYDDEFQLTQRALSLLEENRFWAGVVFPDMHPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEHGITRSQAQEEVPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNRVIWCTWFLDSFSIMSMSICLLTIFIMHGRILHYSNPFILFLFLLAFSIATIMQCFLLSTFFSRASLAAACSGVIYFTLYLPHILCFAWQDRITADMKMAVSLLSPVAFGFGTEYLARFEEQGVGLQWSNIGNSPMEGDEFSFLMSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPITEEMEDPEYPEGINDCFFERELPGLVPGVCVKNLVKIFEPYGRPAVDRLNITFYESQITAFLGHNGAGKTTTLSIMTGLLPPTSGTVLVGGKDIETNLDAIRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWDKAQLEMEAMLEDTGLHHKRNEEAQDLSGGVQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADILGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRRMKTIQSQGRGREATCSCASKGFSVRCPACAEAITPEQVLDGDVNELTDMVHHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDLDSGHLFAGGTQQKRENINLRHPCSGPSEKAGQTPQGSSSHPREPAAHPEGQPPPEREGHSRLNSGARLIVQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSLIIPPFGEYPALTLHPWMYGQQYTFFSMDQLDSEWLSALADVLVNKPGFGNRCLKEEWLPEFPCGNSSPWKTPSVSPDVTHLLQQQKWTADQPSPSCRCSTREKLTMLPECPEGAGGLPPPQRIQRSTEILQDLTDRNVSDFLVKTYPALIRSSLKSKFWVNEQRYGGISVGGKLPAPPFTGEALVGFLSDLGQLMNVSGGPMTREAAKEMPAFLKQLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLHKDKNPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFVSGVSPTTYWLTNFLWDIMNYTVSAALVVGIFIGFQKKAYTSSENLPALVALLMLYGWAVIPMMYPASFLFDIPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRINAMLRKLLIIFPHFCLGRGLIDLALSQAVTDVYARFGEEHSSNPFQWDLIGKNLAAMAVEGVVYFLLTLLIQYQFFFSRWTTEPAKEPITDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTAVTSGDATVAGKSILTNISDVHQSMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIERVTNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIMGIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIRSPKDDLLPDLGPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFRLLVSHKDSLLIEEYSVTQTTLDQVFVNFAKQQNETYDLPLHPRAAGASRQAKEVDKGNSAPQG | ||||||
Disulfide bond | 54↔81 | |||||
Sequence: CHFPNKAMPSAGMLPWLQGIFCNVNNPC | ||||||
Disulfide bond | 75↔324 | |||||
Sequence: CNVNNPCFQSPTAGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWRELRTLSQLMNTLRMHPERIAGRGIRIREVLKDDEMLTLFLVKNIGLSDSVVYLLVNSQVRPEQFARGVPDLMLKDIACSEALLERFLIFPQRRAAQTVRGSLCSLSQGTLQWMEDTLYANVDFFKLFHVFPRLLDSRSQGMNLRSWGRILSDMSPRIQEFIHRPSVQDLLWVTRPLVQTGGPETFTQLMGILSDLLC | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 370↔519 | |||||
Sequence: CNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPATRRILKNANSTFEELERVRKLVKVWEEVGPQIWYFFDKSTQMSMIRDTLENPTVKAFWNRQLGEEGITAEAVLNFLYNGPREGQADDVDNFNWRDIFNITDRALRLANQYLEC | ||||||
Glycosylation | 415 | N-linked (Hex...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 504 | N-linked (Hex...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 641↔1488 | Interchain | ||||
Sequence: CFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNRVIWCTWFLDSFSIMSMSICLLTIFIMHGRILHYSNPFILFLFLLAFSIATIMQCFLLSTFFSRASLAAACSGVIYFTLYLPHILCFAWQDRITADMKMAVSLLSPVAFGFGTEYLARFEEQGVGLQWSNIGNSPMEGDEFSFLMSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPITEEMEDPEYPEGINDCFFERELPGLVPGVCVKNLVKIFEPYGRPAVDRLNITFYESQITAFLGHNGAGKTTTLSIMTGLLPPTSGTVLVGGKDIETNLDAIRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWDKAQLEMEAMLEDTGLHHKRNEEAQDLSGGVQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADILGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRRMKTIQSQGRGREATCSCASKGFSVRCPACAEAITPEQVLDGDVNELTDMVHHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDLDSGHLFAGGTQQKRENINLRHPCSGPSEKAGQTPQGSSSHPREPAAHPEGQPPPEREGHSRLNSGARLIVQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSLIIPPFGEYPALTLHPWMYGQQYTFFSMDQLDSEWLSALADVLVNKPGFGNRCLKEEWLPEFPCGNSSPWKTPSVSPDVTHLLQQQKWTADQPSPSCRC | ||||||
Modified residue | 901 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1185 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1313 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1317 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1319 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 1442↔1453 | |||||
Sequence: CLKEEWLPEFPC | ||||||
Glycosylation | 1455 | N-linked (Hex...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1486↔1500 | |||||
Sequence: CRCSTREKLTMLPEC | ||||||
Glycosylation | 1527 | N-linked (Hex...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1586 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1660 | N-linked (Hex...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1817 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1931 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2004 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2050 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2251 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
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.
Phosphorylation is independent of light exposure and modulates ATPase activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in retina namely in the periphery and incisures of the rod outer segments (ROS).
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | F1MWM0 | CNGB1 Q28181 | 3 | EBI-7079806, EBI-6979031 |
Protein-protein interaction databases
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 929-1160 | ABC transporter 1 | ||||
Sequence: VCVKNLVKIFEPYGRPAVDRLNITFYESQITAFLGHNGAGKTTTLSIMTGLLPPTSGTVLVGGKDIETNLDAIRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWDKAQLEMEAMLEDTGLHHKRNEEAQDLSGGVQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADILGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLV | ||||||
Region | 1295-1340 | Disordered | ||||
Sequence: ENINLRHPCSGPSEKAGQTPQGSSSHPREPAAHPEGQPPPEREGHS | ||||||
Domain | 1936-2168 | ABC transporter 2 | ||||
Sequence: LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTAVTSGDATVAGKSILTNISDVHQSMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIERVTNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIMGIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMK | ||||||
Region | 2242-2247 | Essential for ATP binding and ATPase activity | ||||
Sequence: VFVNFA | ||||||
Region | 2262-2281 | Disordered | ||||
Sequence: AAGASRQAKEVDKGNSAPQG |
Domain
The second extracellular domain (ECD2, aa 1395-1680) undergoes conformational change in response to its specific interaction with its substrate all-trans-retinal. Nucleotide binding domain 1 (NBD1, aa 854-1375) binds preferentially and with high affinity with the 11-cis retinal.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,281
- Mass (Da)257,376
- Last updated2011-11-16 v2
- Checksum26C8C84FB3CB243F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1LRB6 | A0A3Q1LRB6_BOVIN | ABCA4 | 2273 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1037 | in Ref. 1; AAC48716 | ||||
Sequence: K → E | ||||||
Sequence conflict | 1060 | in Ref. 1; AAC48716 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 1322 | in Ref. 1; AAC48716 | ||||
Sequence: R → G | ||||||
Sequence conflict | 1420 | in Ref. 1; AAC48716 | ||||
Sequence: L → P | ||||||
Sequence conflict | 1858-1862 | in Ref. 1; AAC48716 | ||||
Sequence: RFGEE → QFGEA | ||||||
Sequence conflict | 2118 | in Ref. 1; AAC48716 | ||||
Sequence: G → E | ||||||
Sequence conflict | 2203 | in Ref. 1; AAC48716 | ||||
Sequence: M → T | ||||||
Sequence conflict | 2262 | in Ref. 1; AAC48716 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90126 EMBL· GenBank· DDBJ | AAC48716.1 EMBL· GenBank· DDBJ | mRNA | ||
DAAA02007872 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |