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P78363 (ABCA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Retinal-specific ATP-binding cassette transporter
Alternative name(s):
ATP-binding cassette sub-family A member 4
RIM ABC transporter
Short name=RIM protein
Short name=RmP
Stargardt disease protein
Gene names
Name:ABCA4
Synonyms:ABCR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans-retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery. Ref.8

Subcellular location

Membrane; Multi-pass membrane protein. Note: Localized to outer segment disk edges of rods and cones, with around one million copies/photoreceptor. Ref.8

Tissue specificity

Retinal-specific. Seems to be exclusively found in the rims of rod photoreceptor cells.

Polymorphism

The variant Ala-863 is present in the general population at a frequency of approximately 3% and 1% in Northern Europe and United States, respectively. It is a mild alteration probably leading to STGD phenotype only in combination with a more severe allele. The variant Glu-1961 is found with high frequency in healthy individuals of Somali ancestry.

Involvement in disease

Stargardt disease 1 (STGD1) [MIM:248200]: A common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.3 Ref.4 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.28 Ref.29 Ref.30 Ref.34

Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal recessive retinal disorder very similar to Stargardt disease. In contrast to Stargardt disease, FFM is characterized by later onset and slowly progressive course.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.12 Ref.27 Ref.28

Macular degeneration, age-related, 2 (ARMD2) [MIM:153800]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9 Ref.11 Ref.33

Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.19 Ref.28 Ref.30

Retinitis pigmentosa 19 (RP19) [MIM:601718]: 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. RP19 is characterized by choroidal atrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the ABC transporter superfamily. ABCA family.

Contains 2 ABC transporter domains.

Sequence caution

The sequence BAE06122.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processSensory transduction
Transport
Vision
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseAge-related macular degeneration
Cone-rod dystrophy
Disease mutation
Retinitis pigmentosa
Stargardt disease
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphospholipid transfer to membrane

Inferred from electronic annotation. Source: Ensembl

photoreceptor cell maintenance

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

retinoid metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

visual perception

Traceable author statement PubMed 9425888. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

membrane

Traceable author statement Ref.1. Source: ProtInc

photoreceptor disc membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

ATPase activity, coupled to transmembrane movement of substances

Traceable author statement Ref.1. Source: ProtInc

phospholipid-translocating ATPase activity

Inferred from electronic annotation. Source: Ensembl

transporter activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22732273Retinal-specific ATP-binding cassette transporter
PRO_0000093301

Regions

Topological domain1 – 2121Cytoplasmic Ref.10
Transmembrane22 – 4221Helical; Potential
Topological domain43 – 646604Extracellular Ref.10
Transmembrane647 – 66721Helical; Potential
Transmembrane700 – 72021Helical; Potential
Transmembrane731 – 75121Helical; Potential
Transmembrane760 – 78021Helical; Potential
Transmembrane836 – 85621Helical; Potential
Topological domain857 – 1376520Cytoplasmic Ref.10
Transmembrane1377 – 139721Helical; Potential
Topological domain1398 – 1727330Extracellular Ref.10
Transmembrane1728 – 174821Helical; Potential
Transmembrane1760 – 178021Helical; Potential
Transmembrane1793 – 181321Helical; Potential
Transmembrane1832 – 185221Helical; Potential
Transmembrane1874 – 189421Helical; Potential
Topological domain1895 – 2273379Cytoplasmic Ref.10
Domain929 – 1160232ABC transporter 1
Domain1938 – 2170233ABC transporter 2
Nucleotide binding963 – 9708ATP 1 Potential
Nucleotide binding1972 – 19798ATP 2 Potential

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Ref.10
Glycosylation4151N-linked (GlcNAc...) Ref.10
Glycosylation4441N-linked (GlcNAc...) Ref.10
Glycosylation5041N-linked (GlcNAc...) Ref.10
Glycosylation14691N-linked (GlcNAc...) Ref.10
Glycosylation15291N-linked (GlcNAc...) Ref.10
Glycosylation15881N-linked (GlcNAc...) Ref.10
Glycosylation16621N-linked (GlcNAc...) Ref.10
Disulfide bond75 ↔ 324 By similarity
Disulfide bond1488 ↔ 1502 By similarity

Natural variations

Natural variant111L → P in FFM. Ref.12
VAR_012493
Natural variant13 – 153Missing in STGD1.
VAR_012494
Natural variant181R → W in STGD1. Ref.3 Ref.12
Corresponds to variant rs121909205 [ dbSNP | Ensembl ].
VAR_008398
Natural variant241R → H in STGD1.
VAR_008399
Natural variant541C → Y in STGD1. Ref.15 Ref.30
VAR_008400
Natural variant581N → K in STGD1. Ref.30
VAR_012495
Natural variant601A → E in STGD1. Ref.18
VAR_012496
Natural variant601A → T in STGD1. Ref.18
VAR_012497
Natural variant601A → V in STGD1. Ref.16 Ref.30
VAR_008492
Natural variant651G → E in STGD1 and CORD3. Ref.18 Ref.19 Ref.30
VAR_008401
Natural variant681P → L in STGD1. Ref.18
VAR_012498
Natural variant681P → R in STGD1.
VAR_012499
Natural variant721G → R in STGD1. Ref.18
VAR_012500
Natural variant751C → G in STGD1.
VAR_008402
Natural variant771V → E in STGD1. Ref.30
VAR_012501
Natural variant961N → D in STGD1.
VAR_008403
Natural variant961N → H in STGD1.
VAR_008404
Natural variant1001S → P in STGD1.
VAR_012502
Natural variant1521R → Q. Ref.18
Corresponds to variant rs62646862 [ dbSNP | Ensembl ].
VAR_012503
Natural variant1561I → V in STGD1. Ref.34
Corresponds to variant rs62646863 [ dbSNP | Ensembl ].
VAR_012504
Natural variant1901Q → H in STGD1. Ref.30
VAR_012505
Natural variant1921A → T in STGD1.
VAR_008405
Natural variant2061S → R in STGD1; reduced basal and retinal-stimulated ATP-hydrolysis. Ref.16
Corresponds to variant rs61748536 [ dbSNP | Ensembl ].
VAR_012506
Natural variant2121R → C in STGD1 and CORD3; common mutation in southern Europe; reduced ATP-binding capacity. Ref.3 Ref.12 Ref.18 Ref.19 Ref.22 Ref.28 Ref.34
VAR_008406
Natural variant2121R → H. Ref.18 Ref.22 Ref.25 Ref.27 Ref.30
Corresponds to variant rs6657239 [ dbSNP | Ensembl ].
VAR_012507
Natural variant2201R → C in STGD1.
VAR_012508
Natural variant2241T → M in a breast cancer sample; somatic mutation. Ref.32
VAR_035736
Natural variant2301C → S in STGD1. Ref.18
VAR_012509
Natural variant2441L → P in STGD1. Ref.30
VAR_012510
Natural variant2471N → S in STGD1. Ref.18
VAR_012511
Natural variant2491D → G in STGD1.
VAR_008407
Natural variant3001T → N in STGD1. Ref.16
VAR_008408
Natural variant3091P → R in STGD1. Ref.30
VAR_012512
Natural variant3281E → V in STGD1. Ref.18
VAR_012513
Natural variant3331R → W in STGD1.
VAR_012514
Natural variant3361S → C in STGD1.
VAR_008409
Natural variant3391W → G in FFM. Ref.27
VAR_012515
Natural variant3401Y → D in STGD1. Ref.20
VAR_008410
Natural variant3801N → K in STGD1. Ref.34
VAR_012516
Natural variant4071A → V in STGD1 and CORD3.
VAR_008411
Natural variant4231H → R. Ref.18 Ref.25 Ref.27 Ref.30 Ref.31
Corresponds to variant rs3112831 [ dbSNP | Ensembl ].
VAR_012517
Natural variant4451S → R in STGD1.
VAR_008412
Natural variant4711E → K in ARMD2 and STGD1; ATP-binding capacity and retinal stimulation as in wild-type. Ref.18
Corresponds to variant rs1800548 [ dbSNP | Ensembl ].
VAR_008413
Natural variant5231D → E in STGD1.
VAR_008414
Natural variant5251F → C in STGD1. Ref.30
VAR_012518
Natural variant5371R → C in STGD1. Ref.30
VAR_012519
Natural variant5411L → P in STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis. Ref.12 Ref.16 Ref.18 Ref.19 Ref.30
VAR_008415
Natural variant5491A → P in STGD1. Ref.30
VAR_012520
Natural variant5501G → R in STGD1. Ref.30 Ref.34
VAR_012521
Natural variant5521V → I. Ref.18 Ref.33
VAR_012522
Natural variant5721R → P in STGD1. Ref.34
VAR_008416
Natural variant5721R → Q in STGD1. Ref.18 Ref.20
VAR_008417
Natural variant6021R → Q in STGD1. Ref.30
VAR_012523
Natural variant6021R → W in STGD1. Ref.34
VAR_008418
Natural variant6071G → R in STGD1. Ref.18 Ref.30 Ref.34
VAR_012524
Natural variant6071G → W in STGD1.
VAR_012525
Natural variant6081F → I in STGD1.
VAR_008419
Natural variant6351Q → K in STGD1. Ref.18
VAR_012526
Natural variant6361Q → H in STGD1. Ref.12
VAR_012527
Natural variant6431V → G.
Corresponds to variant rs114572202 [ dbSNP | Ensembl ].
VAR_008420
Natural variant6431V → M in STGD1. Ref.30
Corresponds to variant rs143548435 [ dbSNP | Ensembl ].
VAR_012528
Natural variant6451D → N in STGD1.
VAR_008421
Natural variant6531R → C in STGD1. Ref.18 Ref.34
VAR_012529
Natural variant6861L → S in STGD1. Ref.28
VAR_012530
Natural variant7161T → M in STGD1.
VAR_012531
Natural variant7521S → I.
Corresponds to variant rs1801369 [ dbSNP | Ensembl ].
VAR_014703
Natural variant7621A → E in ARMD2. Ref.33
VAR_067427
Natural variant7641C → Y in STGD1. Ref.18
VAR_012532
Natural variant7651S → N in STGD1.
VAR_012534
Natural variant7651S → R in STGD1. Ref.18
VAR_012533
Natural variant7671V → D in STGD1. Ref.22 Ref.30 Ref.34
VAR_012535
Natural variant7971L → P in STGD1. Ref.30
VAR_012536
Natural variant8181G → E in ARMD2 and STGD1; reduced ATP-binding capacity.
VAR_008422
Natural variant8211W → R in STGD1. Ref.30
VAR_008423
Natural variant8241I → T in STGD1. Ref.30
VAR_012537
Natural variant8461D → H. Ref.1
VAR_008493
Natural variant8491V → A in STGD1. Ref.16
Corresponds to variant rs61749435 [ dbSNP | Ensembl ].
VAR_012538
Natural variant8511G → D in STGD1; highly reduced ATP-binding capacity.
VAR_008424
Natural variant8541A → T in STGD1.
VAR_012539
Natural variant8631G → A in STGD1, FFM and CORD3; frequent mutation in northern Europe in linkage disequilibrium with the polymorphic variant Q-943; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis. Ref.15 Ref.19 Ref.20 Ref.27 Ref.30
Corresponds to variant rs76157638 [ dbSNP | Ensembl ].
VAR_008425
Natural variant8631Missing in STGD1 and CORD3; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis. Ref.19
VAR_012540
Natural variant8731F → L in STGD1.
VAR_012541
Natural variant8971T → I in STGD1. Ref.22 Ref.34
Corresponds to variant rs61749440 [ dbSNP | Ensembl ].
VAR_012542
Natural variant9011T → A. Ref.18 Ref.34
Corresponds to variant rs61754030 [ dbSNP | Ensembl ].
VAR_008426
Natural variant9141H → R. Ref.18
VAR_012543
Natural variant9311V → M in STGD1. Ref.34
Corresponds to variant rs58331765 [ dbSNP | Ensembl ].
VAR_008427
Natural variant9351V → A in STGD1. Ref.30
VAR_012544
Natural variant9431R → Q in linkage disequilibrium with A-863 in the European population. Ref.1 Ref.5 Ref.18 Ref.20 Ref.24 Ref.27 Ref.28 Ref.30
Corresponds to variant rs1801581 [ dbSNP | Ensembl ].
VAR_008428
Natural variant9431R → W in STGD1 and FFM. Ref.27 Ref.30
Corresponds to variant rs61749446 [ dbSNP | Ensembl ].
VAR_012545
Natural variant9571Q → R in STGD1.
VAR_008429
Natural variant9591T → I in STGD1. Ref.18
VAR_012546
Natural variant9651N → S in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.20 Ref.34
VAR_008430
Natural variant9711T → N in STGD1; highly reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis.
VAR_012547
Natural variant9721T → N in STGD1; unknown pathological significance. Ref.24
VAR_012548
Natural variant9741S → P in STGD1. Ref.16
VAR_012549
Natural variant9781G → C in STGD1.
VAR_008431
Natural variant9891V → A in STGD1. Ref.30
Corresponds to variant rs139296587 [ dbSNP | Ensembl ].
VAR_012550
Natural variant9911G → R in FFM. Ref.27
Corresponds to variant rs147484266 [ dbSNP | Ensembl ].
VAR_012551
Natural variant10141L → R in STGD1.
VAR_012552
Natural variant10191T → A in STGD1.
VAR_012553
Natural variant10191T → M in STGD1. Ref.12 Ref.34
VAR_012554
Natural variant10221E → K in STGD1.
VAR_012555
Natural variant10311K → E in STGD1.
VAR_012556
Natural variant10361E → K in STGD1. Ref.18
VAR_008432
Natural variant10381A → V in STGD1, FFM and CORD3; frequent mutation; reduced ATP-binding and retinal-stimulated ATP hydrolysis. Ref.12 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.27 Ref.30
Corresponds to variant rs61751374 [ dbSNP | Ensembl ].
VAR_008433
Natural variant10551R → W in STGD1. Ref.28
VAR_012557
Natural variant10631S → P in STGD1. Ref.18
VAR_012558
Natural variant10711S → L in STGD1; reduced ATP-binding capacity.
VAR_008434
Natural variant10721V → A in STGD1.
VAR_008435
Natural variant10871E → D in STGD1. Ref.18
VAR_012559
Natural variant10871E → K in STGD1. Ref.22
VAR_008436
Natural variant10911G → E in FFM. Ref.12
VAR_012560
Natural variant10971R → C in STGD1. Ref.18
VAR_012561
Natural variant11081R → C in STGD1 and FFM; reduced ATP-binding capacity. Ref.12 Ref.16 Ref.18 Ref.27 Ref.30
Corresponds to variant rs61750120 [ dbSNP | Ensembl ].
VAR_012562
Natural variant11081R → H in STGD1. Ref.34
VAR_012563
Natural variant11081R → L in STGD1. Ref.30
VAR_012564
Natural variant11121T → N in STGD1.
VAR_008437
Natural variant11221E → K in STGD1 and CORD3. Ref.19 Ref.30
VAR_008438
Natural variant11291R → C in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.25
VAR_012565
Natural variant11291R → L in ARMD2 and STGD1; also found in patients with fundus flavimaculatus; reduced ATP-binding capacity. Ref.33 Ref.34
Corresponds to variant rs1801269 [ dbSNP | Ensembl ].
VAR_008439
Natural variant11481K → T. Ref.27
VAR_012566
Natural variant12011L → R in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.25 Ref.30
Corresponds to variant rs61750126 [ dbSNP | Ensembl ].
VAR_008440
Natural variant12041D → N in STGD1.
VAR_008441
Natural variant12501L → P in STGD1.
VAR_012567
Natural variant12531T → M in FFM; unknown pathological significance. Ref.28
VAR_012568
Natural variant13001R → Q in STGD1. Ref.30
Corresponds to variant rs61750129 [ dbSNP | Ensembl ].
VAR_012569
Natural variant13141P → T.
VAR_008442
Natural variant13801P → L in STGD1; reduced ATP-binding capacity. Ref.18 Ref.30 Ref.34
VAR_008443
Natural variant13881L → P in STGD1. Ref.30
VAR_012570
Natural variant13991E → K in STGD1. Ref.18 Ref.22
VAR_012571
Natural variant14061H → Y in STGD1.
VAR_008444
Natural variant14081W → L in STGD1. Ref.16
VAR_008445
Natural variant14081W → R in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.30
VAR_008446
Natural variant14281T → M in ARMD2.
Corresponds to variant rs1800549 [ dbSNP | Ensembl ].
VAR_008447
Natural variant14291V → A in STGD1.
VAR_008448
Natural variant14301L → P in STGD1. Ref.18
VAR_012572
Natural variant14331V → I in STGD1. Ref.34
Corresponds to variant rs56357060 [ dbSNP | Ensembl ].
VAR_008449
Natural variant14391G → D in STGD1.
VAR_008450
Natural variant14401F → S in STGD1.
VAR_008451
Natural variant14401F → V in STGD1. Ref.18
VAR_012573
Natural variant14431R → H in STGD1. Ref.18
VAR_012574
Natural variant14861P → L in STGD1. Ref.18 Ref.30 Ref.34
VAR_008452
Natural variant14881C → F in STGD1.
VAR_012575
Natural variant14881C → R in STGD1 and FFM; reduced retinal-stimulated ATP hydrolysis. Ref.16 Ref.27 Ref.30
VAR_008453
Natural variant14881C → Y in STGD1. Ref.18
VAR_012576
Natural variant14901C → Y in STGD1 and CORD3; reduced retinal-stimulated ATP hydrolysis. Ref.19 Ref.30 Ref.34
VAR_008454
Natural variant15081G → C in FFM. Ref.12
VAR_012577
Natural variant15131Q → R in STGD1.
VAR_012578
Natural variant15171R → S in ARMD2.
Corresponds to variant rs1800550 [ dbSNP | Ensembl ].
VAR_008455
Natural variant15251L → P in STGD1.
VAR_012579
Natural variant15261T → M in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.30
VAR_008456
Natural variant15321D → N in STGD1. Ref.30
VAR_008457
Natural variant15371T → M in STGD1. Ref.18
VAR_012580
Natural variant15621I → T in STGD1, FFM, ARMD2 and CORD3. Ref.18 Ref.27 Ref.30
Corresponds to variant rs1762111 [ dbSNP | Ensembl ].
VAR_008458
Natural variant15781G → R in ARMD2.
Corresponds to variant rs1800551 [ dbSNP | Ensembl ].
VAR_008459
Natural variant15981A → D in CORD3. Ref.19
VAR_012581
Natural variant16311L → P in STGD1.
VAR_008460
Natural variant16371A → T Rare polymorphism. Ref.30
VAR_012582
Natural variant16401R → Q in STGD1, FFM and CORD3. Ref.22 Ref.27 Ref.30 Ref.34
VAR_012583
Natural variant16401R → W in STGD1 and CORD3. Ref.12 Ref.30 Ref.34
VAR_008461
Natural variant16521Y → D in STGD1. Ref.16
VAR_008462
Natural variant1681 – 16855Missing in STGD1; highly reduced ATP-binding capacity.
VAR_012584
Natural variant16891S → P in STGD1. Ref.18
VAR_012585
Natural variant16931V → I in STGD1.
Corresponds to variant rs61750563 [ dbSNP | Ensembl ].
VAR_012586
Natural variant16961S → N in STGD1.
VAR_008463
Natural variant17031Q → K in STGD1.
VAR_008464
Natural variant17051R → L in STGD1. Ref.18
VAR_012587
Natural variant17241W → C in ARMD2. Ref.33
VAR_067428
Natural variant17291L → P in STGD1. Ref.16
VAR_008465
Natural variant17331M → T in STGD1. Ref.18
VAR_012588
Natural variant17361S → P in STGD1.
VAR_012589
Natural variant17481G → R in STGD1. Ref.18 Ref.34
VAR_012590
Natural variant1761 – 17633Missing in STGD1; highly reduced ATP-binding capacity.
VAR_012591
Natural variant17631L → P in STGD1. Ref.18
VAR_012592
Natural variant17761P → L in STGD1. Ref.30
VAR_012593
Natural variant17801P → A in STGD1. Ref.20
VAR_012594
Natural variant17941A → D in STGD1.
VAR_008466
Natural variant17991N → D in STGD1. Ref.28 Ref.34
VAR_012595
Natural variant18051N → D in STGD1. Ref.28
VAR_012596
Natural variant18171E → D. Ref.1 Ref.3
VAR_012597
Natural variant18201R → P in STGD1.
VAR_008467
Natural variant18381H → Y in STGD1.
VAR_008468
Natural variant18431R → W in STGD1.
VAR_008469
Natural variant18461I → T. Ref.30
VAR_008494
Natural variant18681N → I Slightly reduced retinal-stimulated ATP hydrolysis. Ref.18 Ref.24 Ref.25 Ref.27 Ref.30
Corresponds to variant rs1801466 [ dbSNP | Ensembl ].
VAR_008470
Natural variant18841V → E in STGD1.
VAR_012598
Natural variant18851E → K in STGD1. Ref.18
VAR_012599
Natural variant18861G → E in STGD1; highly reduced ATP-binding capacity.
VAR_008471
Natural variant18901Missing in STGD1.
VAR_008472
Natural variant18961V → D in STGD1.
VAR_012600
Natural variant18981R → H in STGD1 and ARMD2. Ref.18 Ref.20
Corresponds to variant rs1800552 [ dbSNP | Ensembl ].
VAR_008473
Natural variant19211V → M. Ref.18
Corresponds to variant rs61753032 [ dbSNP | Ensembl ].
VAR_012601
Natural variant19401L → P in STGD1 and FFM. Ref.28 Ref.34
VAR_012602
Natural variant19481P → L. Ref.18 Ref.24 Ref.28 Ref.30
Corresponds to variant rs56142141 [ dbSNP | Ensembl ].
VAR_008474
Natural variant19611G → E in STGD1 and FFM; frequent mutation; may be associated with ARMD2; inhibition of ATP hydrolysis by retinal. Ref.16 Ref.17 Ref.18 Ref.22 Ref.26 Ref.30 Ref.34
Corresponds to variant rs1800553 [ dbSNP | Ensembl ].
VAR_008475
Natural variant19701L → F in ARMD2 and FFM. Ref.12 Ref.18
Corresponds to variant rs1800554 [ dbSNP | Ensembl ].
VAR_008476
Natural variant19711L → R in FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis. Ref.12
VAR_012603
Natural variant19751G → R in STGD1. Ref.18
VAR_012604
Natural variant19771G → S in STGD1 and ARMD2; highly reduced ATP-binding capacity; inhibition of ATP hydrolysis by retinal. Ref.12 Ref.18 Ref.30 Ref.33 Ref.34
VAR_008477
Natural variant20271L → F in STGD1 and FFM; highly reduced ATP-binding capacity. Ref.27 Ref.30 Ref.34
Corresponds to variant rs61751408 [ dbSNP | Ensembl ].
VAR_008478
Natural variant20301R → Q in STGD1 and FFM. Ref.27 Ref.30
Corresponds to variant rs61750641 [ dbSNP | Ensembl ].
VAR_008480
Natural variant20351L → P in STGD1. Ref.30
VAR_012605
Natural variant20381R → W in STGD1; highly reduced ATP-binding capacity. Ref.16
VAR_008495
Natural variant20471I → N in ARMD2. Ref.33
VAR_067429
Natural variant20501V → L in STGD1. Ref.30
Corresponds to variant rs41292677 [ dbSNP | Ensembl ].
VAR_008481
Natural variant20591G → A. Ref.18
VAR_012606
Natural variant20601L → R in CORD3. Ref.28 Ref.34
VAR_012607
Natural variant20711Y → F in STGD1.
VAR_012608
Natural variant20771R → G in STGD1. Ref.18
VAR_012609
Natural variant20771R → W in STGD1; highly reduced ATP-binding capacity. Ref.16 Ref.18
VAR_008482
Natural variant20961E → K in STGD1; inhibition of ATP hydrolysis by retinal.
VAR_008483
Natural variant21061R → C in STGD1 and FFM; reduced ATP-binding capacity. Ref.27
VAR_008484
Natural variant21071R → C in STGD1. Ref.30
Corresponds to variant rs2297669 [ dbSNP | Ensembl ].
VAR_012610
Natural variant21071R → H in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.12 Ref.16 Ref.25 Ref.28 Ref.30 Ref.34
Corresponds to variant rs62642564 [ dbSNP | Ensembl ].
VAR_008485
Natural variant21281H → R in STGD1. Ref.16
VAR_008486
Natural variant21311E → K in STGD1.
VAR_008487
Natural variant21371C → Y in ARMD2. Ref.33
VAR_067430
Natural variant21391R → W in STGD1. Ref.30
VAR_008488
Natural variant21461G → D in CORD3. Ref.30
VAR_012611
Natural variant21491R → L in STGD1.
VAR_012612
Natural variant21501C → R in STGD1. Ref.30
VAR_012613
Natural variant21501C → Y in STGD1 and CORD3. Ref.16 Ref.30 Ref.34
VAR_008489
Natural variant21601K → R in STGD1.
VAR_008490
Natural variant21771D → N May be associated with ARMD2; increased retinal-stimulated ATP hydrolysis. Ref.17 Ref.18 Ref.26
Corresponds to variant rs1800555 [ dbSNP | Ensembl ].
VAR_008491
Natural variant22161A → V. Ref.18
VAR_012614
Natural variant22291L → P in STGD1.
VAR_012615
Natural variant22411L → V in STGD1. Ref.18 Ref.34
Corresponds to variant rs61748521 [ dbSNP | Ensembl ].
VAR_012616
Natural variant22551S → I. Ref.25 Ref.27 Ref.28
Corresponds to variant rs6666652 [ dbSNP | Ensembl ].
VAR_009157
Natural variant22631R → L in STGD1.
VAR_012617

Experimental info

Mutagenesis9661G → D: Abolishes basal and retinal-stimulated ATP hydrolysis. Ref.23
Mutagenesis9691K → M: Abolishes basal and retinal-stimulated ATP hydrolysis. Ref.23
Mutagenesis19751G → D: Inhibition of retinal-stimulated ATP hydrolysis. Ref.23
Mutagenesis19781K → M: Inhibition of retinal-stimulated ATP hydrolysis. Ref.23
Sequence conflict7221G → V in AAC23915. Ref.2
Sequence conflict8491V → C in AAC51144. Ref.1
Sequence conflict8821G → S in AAC51144. Ref.1
Sequence conflict8821G → S in CAA75729. Ref.3
Sequence conflict9411C → S in AAC23915. Ref.2
Sequence conflict11161S → P in AAC51144. Ref.1
Sequence conflict1125 – 11262LL → HQ in AAC51144. Ref.1
Sequence conflict13951P → L in AAC51144. Ref.1
Sequence conflict13951P → L in CAA75729. Ref.3
Sequence conflict14651S → C in AAC05632. Ref.4
Sequence conflict15181S → T in AAC05632. Ref.4
Sequence conflict17331M → V in AAC23915. Ref.2
Sequence conflict19891T → N in AAC23915. Ref.2
Sequence conflict21191E → K in AAC51144. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78363 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: 6E7012D3041CD043

FASTA2,273255,944
        10         20         30         40         50         60 
MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS HHECHFPNKA 

        70         80         90        100        110        120 
MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS ILARVYRDFQ ELLMNAPESQ 

       130        140        150        160        170        180 
HLGRIWTELH ILSQFMDTLR THPERIAGRG IRIRDILKDE ETLTLFLIKN IGLSDSVVYL 

       190        200        210        220        230        240 
LINSQVRPEQ FAHGVPDLAL KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI 

       250        260        270        280        290        300 
EDTLYANVDF FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT 

       310        320        330        340        350        360 
RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG IDSTRKDPIY 

       370        380        390        400        410        420 
SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY TPDSPAARRI LKNANSTFEE 

       430        440        450        460        470        480 
LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM IRDTLGNPTV KDFLNRQLGE EGITAEAILN 

       490        500        510        520        530        540 
FLYKGPRESQ ADDMANFDWR DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS 

       550        560        570        580        590        600 
LLEENMFWAG VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED 

       610        620        630        640        650        660 
FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV 

       670        680        690        700        710        720 
LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM 

       730        740        750        760        770        780 
HGRILHYSDP FILFLFLLAF STATIMLCFL LSTFFSKASL AAACSGVIYF TLYLPHILCF 

       790        800        810        820        830        840 
AWQDRMTAEL KKAVSLLSPV AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM 

       850        860        870        880        890        900 
QMMLLDAAVY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL 

       910        920        930        940        950        960 
TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN ITFYENQITA 

       970        980        990       1000       1010       1020 
FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA VRQSLGMCPQ HNILFHHLTV 

      1030       1040       1050       1060       1070       1080 
AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA 

      1090       1100       1110       1120       1130       1140 
KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC 

      1150       1160       1170       1180       1190       1200 
SGTPLFLKNC FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV 

      1210       1220       1230       1240       1250       1260 
LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL EETLADLGLS 

      1270       1280       1290       1300       1310       1320 
SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR HPCLGPREKA GQTPQDSNVC 

      1330       1340       1350       1360       1370       1380 
SPGAPAAHPE GQPPPEPECP GPQLNTGTQL VLQHVQALLV KRFQHTIRSH KDFLAQIVLP 

      1390       1400       1410       1420       1430       1440 
ATFVFLALML SIVIPPFGEY PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF 

      1450       1460       1470       1480       1490       1500 
GNRCLKEGWL PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP 

      1510       1520       1530       1540       1550       1560 
ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF WVNEQRYGGI 

      1570       1580       1590       1600       1610       1620 
SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK EIPDFLKHLE TEDNIKVWFN 

      1630       1640       1650       1660       1670       1680 
NKGWHALVSF LNVAHNAILR ASLPKDRSPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA 

      1690       1700       1710       1720       1730       1740 
VVAICVIFSM SFVPASFVLY LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG 

      1750       1760       1770       1780       1790       1800 
LVVGIFIGFQ KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL 

      1810       1820       1830       1840       1850       1860 
FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL SQAVTDVYAR 

      1870       1880       1890       1900       1910       1920 
FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF FLSQWIAEPT KEPIVDEDDD 

      1930       1940       1950       1960       1970       1980 
VAEERQRIIT GGNKTDILRL HELTKIYPGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT 

      1990       2000       2010       2020       2030       2040 
TFKMLTGDTT VTSGDATVAG KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR 

      2050       2060       2070       2080       2090       2100 
GVPAEEIEKV ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG 

      2110       2120       2130       2140       2150       2160 
MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC MGTIQHLKSK 

      2170       2180       2190       2200       2210       2220 
FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFQ 

      2230       2240       2250       2260       2270 
LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK QQTESHDLPL HPRAAGASRQ AQD 

« Hide

References

« Hide 'large scale' references
[1]"A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy."
Allikmets R., Singh N., Sun H., Shroyer N.F., Hutchinson A., Chidambaram A., Gerrard B., Baird L., Stauffer D., Peiffer A., Rattner A., Smallwood P.M., Li Y., Anderson K.L., Lewis R.A., Nathans J., Leppert M., Dean M., Lupski J.R.
Nat. Genet. 15:236-246(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1, VARIANTS HIS-846; GLN-943 AND ASP-1817.
[2]"The photoreceptor rim protein is an ABC transporter encoded by the gene for recessive Stargardt's disease (ABCR)."
Azarian S.M., Travis G.H.
FEBS Lett. 409:247-252(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete exon-intron structure of the retina-specific ATP binding transporter gene (ABCR) allows the identification of novel mutations underlying Stargardt disease."
Gerber S., Rozet J.-M., van de Pol T.J.R., Hoyng C.B., Munnich A., Blankenagel A., Kaplan J., Cremers F.P.M.
Genomics 48:139-142(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STGD1 TRP-18 AND CYS-212, VARIANT ASP-1817.
[4]"Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and identification of novel mutations in Stargardt's disease."
Nasonkin I., Illing M., Koehler M.R., Schmid M., Molday R.S., Weber B.H.F.
Hum. Genet. 102:21-26(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1.
[5]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-943.
Tissue: Brain.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Mapping of transcription start sites of human retina expressed genes."
Roni V., Carpio R., Wissinger B.
BMC Genomics 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-29.
Tissue: Retina.
[8]"Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease."
Sun H., Molday R.S., Nathans J.
J. Biol. Chem. 274:8269-8281(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Autosomal recessive retinitis pigmentosa and cone-rod dystrophy caused by splice site mutations in the Stargardt's disease gene ABCR."
Cremers F.P.M., van de Pol D.J.R., van Driel M.A., den Hollander A.I., van Haren F.J.J., Knoers N.V.A.M., Tijmes N., Bergen A.A.B., Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Deutman A.F., Hoyng C.B.
Hum. Mol. Genet. 7:355-362(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[10]"Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites."
Bungert S., Molday L.L., Molday R.S.
J. Biol. Chem. 276:23539-23546(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MEMBRANE TOPOLOGY, GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; ASN-504; ASN-1469; ASN-1529; ASN-1588 AND ASN-1662.
[11]"Mutation of the Stargardt disease gene (ABCR) in age-related macular degeneration."
Allikmets R., Shroyer N.F., Singh N., Seddon J.M., Lewis R.A., Bernstein P.S., Peiffer A., Zabriskie N.A., Li Y., Hutchinson A., Dean M., Lupski J.R., Leppert M.
Science 277:1805-1807(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARMD2, VARIANTS.
[12]"Spectrum of ABCR gene mutations in autosomal recessive macular dystrophies."
Rozet J.-M., Gerber S., Souied E., Perrault I., Chatelin S., Ghazi I., Leowski C., Dufier J.-L., Munnich A., Kaplan J.
Eur. J. Hum. Genet. 6:291-295(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108; TRP-1640; SER-1977 AND HIS-2107, VARIANTS FFM PRO-11; PRO-541; VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971.
[13]"Genotype/phenotype analysis of a photoreceptor-specific ATP-binding cassette transporter gene, ABCR, in Stargardt disease."
Lewis R.A., Shroyer N.F., Singh N., Allikmets R., Hutchinson A., Li Y., Lupski J.R., Leppert M., Dean M.
Am. J. Hum. Genet. 64:422-434(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1.
[14]"The 2588G-->C mutation in the ABCR gene is a mild frequent founder mutation in the western European population and allows the classification of ABCR Mutations in patients with Stargardt disease."
Maugeri A., van Driel M.A., van de Pol D.J.R., Klevering B.J., van Haren F.J.J., Tijmes N., Bergen A.A.B., Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Dahl N., Brunner H.G., Deutman A.F., Hoyng C.B., Cremers F.P.M.
Am. J. Hum. Genet. 64:1024-1035(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1, VARIANTS.
[15]"A novel mutation in the ABCR gene in four patients with autosomal recessive Stargardt disease."
Zhang K., Garibaldi D.C., Kniazeva M., Albini T., Chiang M.F., Kerrigan M., Sunness J.S., Han M., Allikmets R.
Am. J. Ophthalmol. 128:720-724(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STGD1 TYR-54, VARIANT ALA-863.
[16]"Variation of clinical expression in patients with Stargardt dystrophy and sequence variations in the ABCR gene."
Fishman G.A., Stone E.M., Grover S., Derlacki D.J., Haines H.L., Hockey R.R.
Arch. Ophthalmol. 117:504-510(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 VAL-60; ARG-206; ASN-300; PRO-541; ALA-849; PRO-974; VAL-1038; CYS-1108; LEU-1408; ARG-1488; ASP-1652; PRO-1729; GLU-1961; TRP-2038; TRP-2077; HIS-2107; ARG-2128 AND TYR-2150.
[17]"Further evidence for an association of ABCR alleles with age-related macular degeneration."
Allikmets R., Tammur J., Hutchinson A., Lewis R.A., Shroyer N.F., Dalakishvili K., Lupski J.R., Steiner K., Pauleikhoff D., Holz F.G., Weber B.H.F., Dean M., Atkinson A., Gail M.H., Bernstein P.S., Singh N., Peiffer A., Zabriskie N.A. expand/collapse author list , Leppert M., Seddon J.M., Zhang K., Sunness J.S., Udar N.S., Yelchits S., Silva-Garcia R., Small K.W., Simonelli F., Testa F., D'Urso M., Brancato R., Rinaldi E., Ingvast S., Taube A., Wadelius C., Souied E., Ducroq D., Kaplan J., Assink J.J.M., ten Brink J.B., de Jong P.T.V.M., Bergen A.A.B., Maugeri A., van Driel M.A., Hoyng C.B., Cremers F.P.M., Paloma E., Coco R., Balcells S., Gonzalez-Duarte R., Kermani S., Stanga P., Bhattacharya S.S., Bird A.C.
Am. J. Hum. Genet. 67:487-491(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-1961 AND ASN-2177.
[18]"A comprehensive survey of sequence variation in the ABCA4 (ABCR) gene in Stargardt disease and age-related macular degeneration."
Rivera A., White K., Stoehr H., Steiner K., Hemmrich N., Grimm T., Jurklies B., Lorenz B., Scholl H.P.N., Apfelstedt-Sylla E., Weber B.H.F.
Am. J. Hum. Genet. 67:800-813(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 GLU-60; THR-60; GLU-65; LEU-68; ARG-72; CYS-212; SER-230; SER-247; VAL-328; LYS-471; PRO-541; GLN-572; ARG-607; LYS-635; CYS-653; TYR-764; ARG-765; ALA-901; ILE-959; LYS-1036; VAL-1038; PRO-1063; ASP-1087; CYS-1097; CYS-1108; LEU-1380; LYS-1399; PRO-1430; VAL-1440; HIS-1443; LEU-1486; TYR-1488; MET-1537; PRO-1689; LEU-1705; THR-1733; ARG-1748; PRO-1763; LYS-1885; HIS-1898; GLU-1961; ARG-1975; SER-1977; GLY-2077; TRP-2077 AND VAL-2241, VARIANTS GLN-152; HIS-212; ARG-423; ILE-552; ARG-914; GLN-943; THR-1562; ILE-1868; MET-1921; LEU-1948; PHE-1970; ALA-2059; ASN-2177 AND VAL-2216.
[19]"Mutations in the ABCA4 (ABCR) gene are the major cause of autosomal recessive cone-rod dystrophy."
Maugeri A., Klevering B.J., Rohrschneider K., Blankenagel A., Brunner H.G., Deutman A.F., Hoyng C.B., Cremers F.P.M.
Am. J. Hum. Genet. 67:960-966(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CORD3 GLU-65; CYS-212; PRO-541; ALA-863; GLY-863 DEL; VAL-1038; LYS-1122; TYR-1490 AND ASP-1598.
[20]"Complex inheritance of ABCR mutations in Stargardt disease: linkage disequilibrium, complex alleles, and pseudodominance."
Shroyer N.F., Lewis R.A., Lupski J.R.
Hum. Genet. 106:244-248(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 AND HIS-1898, VARIANT GLN-943.
[21]"An analysis of ABCR mutations in British patients with recessive retinal dystrophies."
Papaioannou M., Ocaka L., Bessant D., Lois N., Bird A.C., Payne A., Bhattacharya S.S.
Invest. Ophthalmol. Vis. Sci. 41:16-19(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1.
[22]"New ABCR mutations and clinical phenotype in Italian patients with Stargardt disease."
Simonelli F., Testa F., de Crecchio G., Rinaldi E., Hutchinson A., Atkinson A., Dean M., D'Urso M., Allikmets R.
Invest. Ophthalmol. Vis. Sci. 41:892-897(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 CYS-212; ASP-767; ILE-897; VAL-1038; LYS-1087; LYS-1399; GLN-1640 AND GLU-1961, VARIANT HIS-212.
[23]"Biochemical defects in ABCR protein variants associated with human retinopathies."
Sun H., Smallwood P.M., Nathans J.
Nat. Genet. 26:242-246(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS, MUTAGENESIS OF GLY-966; LYS-969; GLY-1975 AND LYS-1978.
[24]"Different clinical expressions in two families with Stargardt's macular dystrophy (STGD1)."
Eksandh L., Ekstroem U., Abrahamson M., Bauer B., Andreasson S.
Acta Ophthalmol. Scand. 79:524-530(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STGD1 ASN-972, VARIANTS GLN-943; ILE-1868 AND LEU-1948.
[25]"Analysis of the ABCR (ABCA4) gene in 4-aminoquinoline retinopathy: is retinal toxicity by chloroquine and hydroxychloroquine related to Stargardt disease?"
Shroyer N.F., Lewis R.A., Lupski J.R.
Am. J. Ophthalmol. 131:761-766(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, VARIANTS HIS-212; ARG-423; ILE-1868 AND ILE-2255.
[26]"Variation of codons 1961 and 2177 of the Stargardt disease gene is not associated with age-related macular degeneration."
Guymer R.H., Heon E., Lotery A.J., Munier F.L., Schorderet D.F., Baird P.N., McNeil R.J., Haines H.L., Sheffield V.C., Stone E.M.
Arch. Ophthalmol. 119:745-751(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-1961 AND ASN-2177.
[27]"Late-onset Stargardt disease is associated with missense mutations that map outside known functional regions of ABCR (ABCA4)."
Yatsenko A.N., Shroyer N.F., Lewis R.A., Lupski J.R.
Hum. Genet. 108:346-355(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FFM GLY-339; ALA-863; TRP-943; ARG-991; VAL-1038; CYS-1108; ARG-1488; THR-1562; GLN-1640; PHE-2027; GLN-2030 AND CYS-2106, VARIANTS HIS-212; ARG-423; GLN-943; THR-1148; ILE-1868 AND ILE-2255.
[28]"Spectrum of ABCA4 (ABCR) gene mutations in Spanish patients with autosomal recessive macular dystrophies."
Paloma E., Martinez-Mir A., Vilageliu L., Gonzalez-Duarte R., Balcells S.
Hum. Mutat. 17:504-510(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 SER-686; TRP-1055; ASP-1799; ASP-1805; PRO-1940 AND HIS-2107, VARIANTS FFM MET-1253 AND PRO-1940, VARIANTS CORD3 CYS-212 AND ARG-2060, VARIANTS GLN-943; LEU-1948 AND ILE-2255.
[29]"An analysis of allelic variation in the ABCA4 gene."
Webster A.R., Heon E., Lotery A.J., Vandenburgh K., Casavant T.L., Oh K.T., Beck G., Fishman G.A., Lam B.L., Levin A., Heckenlively J.R., Jacobson S.G., Weleber R.G., Sheffield V.C., Stone E.M.
Invest. Ophthalmol. Vis. Sci. 42:1179-1189(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1, VARIANTS.
[30]"Mutations in ABCR (ABCA4) in patients with Stargardt macular degeneration or cone-rod degeneration."
Briggs C.E., Rucinski D., Rosenfeld P.J., Hirose T., Berson E.L., Dryja T.P.
Invest. Ophthalmol. Vis. Sci. 42:2229-2236(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 13-LYS--TRP-15 DEL; TYR-54; LYS-58; VAL-60; GLU-65; GLU-77; HIS-190; PRO-244; ARG-309; CYS-525; CYS-537; PRO-541; PRO-549; ARG-550; GLN-602; ARG-607; MET-643; ASP-767; PRO-797; ARG-821; THR-824; ALA-863; ALA-935; TRP-943; ALA-989; VAL-1038; CYS-1108; LEU-1108; LYS-1122; ARG-1201; GLN-1300; LEU-1380; PRO-1388; ARG-1408; LEU-1486; ARG-1488; TYR-1490; MET-1526; ASN-1532; THR-1562; TRP-1640; LEU-1776; THR-1846; GLU-1961; SER-1977; PHE-2027; GLN-2030; PRO-2035; LEU-2050; CYS-2107; HIS-2107; TRP-2139; ARG-2150 AND TYR-2150, VARIANTS CORD3 GLN-1640 AND ASP-2146, VARIANTS HIS-212; ARG-423; GLN-943; THR-1637; ILE-1868 AND LEU-1948.
[31]"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8."
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., Harigae S., Osawa S., Nakamura Y.
J. Hum. Genet. 47:285-310(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-423.
[32]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-224.
[33]"Molecular analysis of the ABCA4 gene for reliable detection of allelic variations in Spanish patients: identification of 21 novel variants."
Aguirre-Lamban J., Riveiro-Alvarez R., Maia-Lopes S., Cantalapiedra D., Vallespin E., Avila-Fernandez A., Villaverde-Montero C., Trujillo-Tiebas M.J., Ramos C., Ayuso C.
Br. J. Ophthalmol. 93:614-621(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARMD2 GLU-762; LEU-1129; CYS-1724; SER-1977; ASN-2047 AND TYR-2137, VARIANT ILE-552.
[34]"Frequency of ABCA4 mutations in 278 Spanish controls: an insight into the prevalence of autosomal recessive Stargardt disease."
Riveiro-Alvarez R., Aguirre-Lamban J., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Cantalapiedra D., Vallespin E., Avila-Fernandez A., Ramos C., Ayuso C.
Br. J. Ophthalmol. 93:1359-1364(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602; ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965; MET-1019; HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490; GLN-1640; TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977; PHE-2027; ARG-2060; HIS-2107; TYR-2150 AND VAL-2241.
+Additional computationally mapped references.

Web resources

Mutations of the ABCA4 gene

Retina International's Scientific Newsletter

GeneReviews
ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U88667 mRNA. Translation: AAC51144.1.
AF000148 mRNA. Translation: AAC23915.1.
Y15635 expand/collapse EMBL AC list , Y15636, Y15637, Y15638, Y15639, Y15640, Y15641, Y15642, Y15643, Y15644, Y15645, Y15646, Y15647, Y15648, Y15649, Y15650, Y15651, Y15652, Y15653, Y15654, Y15655, Y15656, Y15657, Y15658, Y15659, Y15660, Y15661, Y15662, Y15663, Y15664, Y15665, Y15666, Y15667, Y15668, Y15669, Y15670, Y15671, Y15672, Y15673, Y15674, Y15675, Y15676, Y15677, Y15678, Y15679, Y15680, Y15681, Y15682, Y15683, Y15684 Genomic DNA. Translation: CAA75729.1.
AF001945 mRNA. Translation: AAC05632.1.
AB210040 mRNA. Translation: BAE06122.1. Different initiation.
AC093579 Genomic DNA. No translation available.
AC105278 Genomic DNA. No translation available.
DQ426859 mRNA. Translation: ABD90529.1.
RefSeqNP_000341.2. NM_000350.2.
UniGeneHs.416707.

3D structure databases

ProteinModelPortalP78363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106542. 1 interaction.
STRING9606.ENSP00000359245.

Protein family/group databases

TCDB3.A.1.211.2. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP78363.

Polymorphism databases

DMDM6707663.

Proteomic databases

PaxDbP78363.
PRIDEP78363.

Protocols and materials databases

DNASU24.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370225; ENSP00000359245; ENSG00000198691.
GeneID24.
KEGGhsa:24.
UCSCuc001dqh.3. human.

Organism-specific databases

CTD24.
GeneCardsGC01M094458.
H-InvDBHIX0028510.
HGNCHGNC:34. ABCA4.
MIM153800. phenotype.
248200. phenotype.
601691. gene.
601718. phenotype.
604116. phenotype.
neXtProtNX_P78363.
Orphanet279. Age-related macular degeneration.
1872. Cone rod dystrophy.
791. Retinitis pigmentosa.
827. Stargardt disease.
PharmGKBPA24379.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1131.
HOGENOMHOG000231547.
HOVERGENHBG050436.
InParanoidP78363.
KOK05644.
OMAIMVKGAF.
OrthoDBEOG78D7J6.
PhylomeDBP78363.
TreeFamTF105191.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP78363.
BgeeP78363.
CleanExHS_ABCA4.
GenevestigatorP78363.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR026082. ABC_A.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
IPR005951. Rim_ABC_transpt.
[Graphical view]
PANTHERPTHR19229. PTHR19229. 1 hit.
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR01257. rim_protein. 1 hit.
PROSITEPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCA4. human.
GeneWikiABCA4.
GenomeRNAi24.
NextBio75.
PROP78363.
SOURCESearch...

Entry information

Entry nameABCA4_HUMAN
AccessionPrimary (citable) accession number: P78363
Secondary accession number(s): O15112 expand/collapse secondary AC list , O60438, O60915, Q0QD48, Q4LE31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM