Reviewed, UniProtKB/Swiss-Prot P78363 (ABCA4_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in photoresponse. Retinoids, and most likely retinal, are the natural substrates for transport by abcr in rod outer segments. May act in the visual cycle to flip PE-all-trans-retinal adducts from the lumenal to the cytosolic face of the disk membrane, move free all-trans-retinal from the lipid phase of the disk membrane to a juxtamembrane location, or possibly reorient all-trans-retinal in the bilayer.
Subcellular location	Membrane; Multi-pass membrane protein.
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	Defects in ABCA4 are the cause of Stargardt disease type 1 (STGD1) [MIM:248200]. STGD is one of the most frequent causes of macular degeneration in childhood. It is characterized by macular dystrophy with juvenile-onset, rapidly progressive course, alterations of the peripheral retina, and subretinal deposition of lipofuscin-like material. STGD1 inheritance is autosomal recessive. Ref.1 Ref.3 Ref.4 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.25 Ref.26 Ref.27 Defects in ABCA4 are the cause of fundus flavimaculatus (FFM) [MIM:248200]. FFM is an autosomal recessive retinal disorder very similar to Stargardt disease. In contrast to Stargardt disease, FFM is characterized by later onset and slowly progressive course. Ref.7 Ref.9 Ref.25 Ref.24 Defects in ABCA4 may be a cause of age-related macular degeneration type 2 (ARMD2) [MIM:153800]. ARMD is 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 (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Ref.7 Ref.8 Defects in ABCA4 are the cause of cone-rod dystrophy type 3 (CORD3) [MIM:604116]. CORDs are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are 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. Ref.7 Ref.25 Ref.27 Ref.16 Defects in ABCA4 are the cause of retinitis pigmentosa type 19 (RP19) [MIM:601718]. RP leads to degeneration of retinal photoreceptor cells. 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. Inheritance is autosomal recessive. Ref.7
Sequence similarities	Belongs to the ABC transporter superfamily. ABCA family. Contains 2 ABC transporter domains.

Ontologies

Keywords
Biological process	Sensory transduction Transport Vision
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Age-related macular degeneration Cone-rod dystrophy Disease mutation Retinitis pigmentosa Stargardt disease
Domain	Repeat Transmembrane
Ligand	ATP-binding Nucleotide-binding
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phototransduction, visible light Ref.2 Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Inferred from electronic annotation. Source: InterPro membrane fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Ref.1 Traceable author statement. Source: ProtInc ATPase activity, coupled to transmembrane movement of substances Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2273	2273	Retinal-specific ATP-binding cassette transporter		PRO_0000093301
Regions
	Transmembrane	22 – 42	21	Potential
	Topological domain	43 – 546	504	Extracellular By similarity
	Transmembrane	547 – 567	21	Potential
	Transmembrane	647 – 667	21	Potential
	Transmembrane	700 – 720	21	Potential
	Transmembrane	731 – 751	21	Potential
	Transmembrane	760 – 780	21	Potential
	Transmembrane	836 – 856	21	Potential
	Transmembrane	1072 – 1092	21	Potential
	Transmembrane	1377 – 1397	21	Potential
	Topological domain	1398 – 1559	162	Extracellular By similarity
	Transmembrane	1560 – 1580	21	Potential
	Transmembrane	1682 – 1702	21	Potential
	Transmembrane	1728 – 1748	21	Potential
	Transmembrane	1760 – 1780	21	Potential
	Transmembrane	1793 – 1813	21	Potential
	Transmembrane	1832 – 1852	21	Potential
	Transmembrane	1874 – 1894	21	Potential
	Domain	929 – 1160	232	ABC transporter 1
	Domain	1938 – 2170	233	ABC transporter 2
	Nucleotide binding	963 – 970	8	ATP 1 Potential
	Nucleotide binding	1972 – 1979	8	ATP 2 Potential
Amino acid modifications
	Glycosylation	14	1	N-linked (GlcNAc...) Potential
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	415	1	N-linked (GlcNAc...) Potential
	Glycosylation	444	1	N-linked (GlcNAc...) Potential
	Glycosylation	504	1	N-linked (GlcNAc...) Potential
	Glycosylation	950	1	N-linked (GlcNAc...) Potential
	Glycosylation	1469	1	N-linked (GlcNAc...) Potential
	Glycosylation	1529	1	N-linked (GlcNAc...) Potential
	Glycosylation	1588	1	N-linked (GlcNAc...) Potential
	Glycosylation	1662	1	N-linked (GlcNAc...) Potential
	Glycosylation	1707	1	N-linked (GlcNAc...) Potential
	Glycosylation	1819	1	N-linked (GlcNAc...) Potential
	Glycosylation	1933	1	N-linked (GlcNAc...) Potential
	Glycosylation	2006	1	N-linked (GlcNAc...) Potential
	Glycosylation	2052	1	N-linked (GlcNAc...) Potential
	Disulfide bond	75 ↔ 324		By similarity
	Disulfide bond	1488 ↔ 1502		By similarity
Natural variations
	Natural variant	11	1	L → P in FFM. Ref.9		VAR_012493
	Natural variant	13 – 15	3	Missing in STGD1.		VAR_012494
	Natural variant	18	1	R → W in STGD1. Ref.3 Ref.9		VAR_008398
	Natural variant	24	1	R → H in STGD1.		VAR_008399
	Natural variant	54	1	C → Y in STGD1. Ref.12 Ref.27		VAR_008400
	Natural variant	58	1	N → K in STGD1. Ref.27		VAR_012495
	Natural variant	60	1	A → E in STGD1. Ref.15		VAR_012496
	Natural variant	60	1	A → T in STGD1. Ref.15		VAR_012497
	Natural variant	60	1	A → V in STGD1. Ref.13 Ref.27		VAR_008492
	Natural variant	65	1	G → E in STGD1 and CORD3. Ref.15 Ref.27 Ref.16		VAR_008401
	Natural variant	68	1	P → L in STGD1. Ref.15		VAR_012498
	Natural variant	68	1	P → R in STGD1.		VAR_012499
	Natural variant	72	1	G → R in STGD1. Ref.15		VAR_012500
	Natural variant	75	1	C → G in STGD1.		VAR_008402
	Natural variant	77	1	V → E in STGD1. Ref.27		VAR_012501
	Natural variant	96	1	N → D in STGD1.		VAR_008403
	Natural variant	96	1	N → H in STGD1.		VAR_008404
	Natural variant	100	1	S → P in STGD1.		VAR_012502
	Natural variant	152	1	R → Q		VAR_012503
	Natural variant	156	1	I → V in STGD1.		VAR_012504
	Natural variant	190	1	Q → H in STGD1. Ref.27		VAR_012505
	Natural variant	192	1	A → T in STGD1.		VAR_008405
	Natural variant	206	1	S → R in STGD1; reduced basal and retinal-stimulated ATP-hydrolysis. Ref.13		VAR_012506
	Natural variant	212	1	R → C in STGD1 and CORD3; common mutation in southern Europe; reduced ATP-binding capacity. Ref.3 Ref.9 Ref.15 Ref.19 Ref.25 Ref.16		VAR_008406
	Natural variant	212	1	R → H: dbSNP rs6657239. Ref.15 Ref.19 Ref.27 Ref.24 Ref.22		VAR_012507
	Natural variant	220	1	R → C in STGD1.		VAR_012508
	Natural variant	224	1	T → M in a breast cancer sample; somatic mutation. Ref.29		VAR_035736
	Natural variant	230	1	C → S in STGD1. Ref.15		VAR_012509
	Natural variant	244	1	L → P in STGD1. Ref.27		VAR_012510
	Natural variant	247	1	N → S in STGD1. Ref.15		VAR_012511
	Natural variant	249	1	D → G in STGD1.		VAR_008407
	Natural variant	300	1	T → N in STGD1. Ref.13		VAR_008408
	Natural variant	309	1	P → R in STGD1. Ref.27		VAR_012512
	Natural variant	328	1	E → V in STGD1. Ref.15		VAR_012513
	Natural variant	333	1	R → W in STGD1.		VAR_012514
	Natural variant	336	1	S → C in STGD1.		VAR_008409
	Natural variant	339	1	W → G in FFM. Ref.24		VAR_012515
	Natural variant	340	1	Y → D in STGD1. Ref.17		VAR_008410
	Natural variant	380	1	N → K in STGD1.		VAR_012516
	Natural variant	407	1	A → V in STGD1 and CORD3.		VAR_008411
	Natural variant	423	1	H → R: dbSNP rs3112831. Ref.15 Ref.27 Ref.24 Ref.22 Ref.28		VAR_012517
	Natural variant	445	1	S → R in STGD1.		VAR_008412
	Natural variant	471	1	E → K in ARMD2 and STGD1; ATP-binding capacity and retinal stimulation as in wild-type. dbSNP rs1800548. Ref.15		VAR_008413
	Natural variant	523	1	D → E in STGD1.		VAR_008414
	Natural variant	525	1	F → C in STGD1. Ref.27		VAR_012518
	Natural variant	537	1	R → C in STGD1. Ref.27		VAR_012519
	Natural variant	541	1	L → P in STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis. Ref.9 Ref.13 Ref.15 Ref.27 Ref.16		VAR_008415
	Natural variant	549	1	A → P in STGD1. Ref.27		VAR_012520
	Natural variant	550	1	G → R in STGD1. Ref.27		VAR_012521
	Natural variant	552	1	V → I		VAR_012522
	Natural variant	572	1	R → P in STGD1.		VAR_008416
	Natural variant	572	1	R → Q in STGD1. Ref.15 Ref.17		VAR_008417
	Natural variant	602	1	R → Q in STGD1. Ref.27		VAR_012523
	Natural variant	602	1	R → W in STGD1.		VAR_008418
	Natural variant	607	1	G → R in STGD1. Ref.15 Ref.27		VAR_012524
	Natural variant	607	1	G → W in STGD1.		VAR_012525
	Natural variant	608	1	F → I in STGD1.		VAR_008419
	Natural variant	635	1	Q → K in STGD1. Ref.15		VAR_012526
	Natural variant	636	1	Q → H in STGD1. Ref.9		VAR_012527
	Natural variant	643	1	V → G		VAR_008420
	Natural variant	643	1	V → M in STGD1. Ref.27		VAR_012528
	Natural variant	645	1	D → N in STGD1.		VAR_008421
	Natural variant	653	1	R → C in STGD1. Ref.15		VAR_012529
	Natural variant	686	1	L → S in STGD1. Ref.25		VAR_012530
	Natural variant	716	1	T → M in STGD1.		VAR_012531
	Natural variant	752	1	S → I: dbSNP rs1801369.		VAR_014703
	Natural variant	764	1	C → Y in STGD1. Ref.15		VAR_012532
	Natural variant	765	1	S → N in STGD1.		VAR_012534
	Natural variant	765	1	S → R in STGD1. Ref.15		VAR_012533
	Natural variant	767	1	V → D in STGD1. Ref.19 Ref.27		VAR_012535
	Natural variant	797	1	L → P in STGD1. Ref.27		VAR_012536
	Natural variant	818	1	G → E in ARMD2 and STGD1; reduced ATP-binding capacity.		VAR_008422
	Natural variant	821	1	W → R in STGD1. Ref.27		VAR_008423
	Natural variant	824	1	I → T in STGD1. Ref.27		VAR_012537
	Natural variant	846	1	D → H		VAR_008493
	Natural variant	849	1	V → A in STGD1. Ref.13		VAR_012538
	Natural variant	851	1	G → D in STGD1; highly reduced ATP-binding capacity.		VAR_008424
	Natural variant	854	1	A → T in STGD1.		VAR_012539
	Natural variant	863	1	G → 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.12 Ref.17 Ref.27 Ref.24 Ref.16		VAR_008425
	Natural variant	863	1	Missing in STGD1 and CORD3; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis.		VAR_012540
	Natural variant	873	1	F → L in STGD1.		VAR_012541
	Natural variant	897	1	T → I in STGD1. Ref.19		VAR_012542
	Natural variant	901	1	T → A		VAR_008426
	Natural variant	914	1	H → R		VAR_012543
	Natural variant	931	1	V → M in STGD1.		VAR_008427
	Natural variant	935	1	V → A in STGD1. Ref.27		VAR_012544
	Natural variant	943	1	R → Q in linkage disequilibrium with A-863 in the European population. dbSNP rs1801581. Ref.1 Ref.15 Ref.17 Ref.21 Ref.25 Ref.27 Ref.24 Ref.5		VAR_008428
	Natural variant	943	1	R → W in STGD1 and FFM. Ref.27 Ref.24		VAR_012545
	Natural variant	957	1	Q → R in STGD1.		VAR_008429
	Natural variant	959	1	T → I in STGD1. Ref.15		VAR_012546
	Natural variant	965	1	N → S in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.17		VAR_008430
	Natural variant	971	1	T → N in STGD1; highly reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis.		VAR_012547
	Natural variant	972	1	T → N in STGD1; could be a rare polymorphism. Ref.21		VAR_012548
	Natural variant	974	1	S → P in STGD1. Ref.13		VAR_012549
	Natural variant	978	1	G → C in STGD1.		VAR_008431
	Natural variant	989	1	V → A in STGD1. Ref.27		VAR_012550
	Natural variant	991	1	G → R in FFM. Ref.24		VAR_012551
	Natural variant	1014	1	L → R in STGD1.		VAR_012552
	Natural variant	1019	1	T → A in STGD1.		VAR_012553
	Natural variant	1019	1	T → M in STGD1. Ref.9		VAR_012554
	Natural variant	1022	1	E → K in STGD1.		VAR_012555
	Natural variant	1031	1	K → E in STGD1.		VAR_012556
	Natural variant	1036	1	E → K in STGD1. Ref.15		VAR_008432
	Natural variant	1038	1	A → V in STGD1, FFM and CORD3; frequent mutation; reduced ATP-binding and retinal-stimulated ATP hydrolysis. Ref.9 Ref.13 Ref.15 Ref.17 Ref.19 Ref.27 Ref.24 Ref.16		VAR_008433
	Natural variant	1055	1	R → W in STGD1. Ref.25		VAR_012557
	Natural variant	1063	1	S → P in STGD1. Ref.15		VAR_012558
	Natural variant	1071	1	S → L in STGD1; reduced ATP-binding capacity.		VAR_008434
	Natural variant	1072	1	V → A in STGD1.		VAR_008435
	Natural variant	1087	1	E → D in STGD1. Ref.15		VAR_012559
	Natural variant	1087	1	E → K in STGD1. Ref.19		VAR_008436
	Natural variant	1091	1	G → E in FFM. Ref.9		VAR_012560
	Natural variant	1097	1	R → C in STGD1. Ref.15		VAR_012561
	Natural variant	1108	1	R → C in STGD1 and FFM; reduced ATP-binding capacity. Ref.9 Ref.13 Ref.15 Ref.27 Ref.24		VAR_012562
	Natural variant	1108	1	R → H in STGD1.		VAR_012563
	Natural variant	1108	1	R → L in STGD1. Ref.27		VAR_012564
	Natural variant	1112	1	T → N in STGD1.		VAR_008437
	Natural variant	1122	1	E → K in STGD1 and CORD3. Ref.27 Ref.16		VAR_008438
	Natural variant	1129	1	R → C in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.22		VAR_012565
	Natural variant	1129	1	R → L in ARMD2, STGD1 and FFM; reduced ATP-binding capacity. dbSNP rs1801269.		VAR_008439
	Natural variant	1148	1	K → T		VAR_012566
	Natural variant	1201	1	L → R in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.27 Ref.22		VAR_008440
	Natural variant	1204	1	D → N in STGD1.		VAR_008441
	Natural variant	1250	1	L → P in STGD1.		VAR_012567
	Natural variant	1253	1	T → M in FFM; could be a rare polymorphism. Ref.25		VAR_012568
	Natural variant	1300	1	R → Q in STGD1. Ref.27		VAR_012569
	Natural variant	1314	1	P → T		VAR_008442
	Natural variant	1380	1	P → L in STGD1; reduced ATP-binding capacity. Ref.15 Ref.27		VAR_008443
	Natural variant	1388	1	L → P in STGD1. Ref.27		VAR_012570
	Natural variant	1399	1	E → K in STGD1. Ref.15 Ref.19		VAR_012571
	Natural variant	1406	1	H → Y in STGD1.		VAR_008444
	Natural variant	1408	1	W → L in STGD1. Ref.13		VAR_008445
	Natural variant	1408	1	W → R in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.27		VAR_008446
	Natural variant	1428	1	T → M in ARMD2. dbSNP rs1800549.		VAR_008447
	Natural variant	1429	1	V → A in STGD1.		VAR_008448
	Natural variant	1430	1	L → P in STGD1. Ref.15		VAR_012572
	Natural variant	1433	1	V → I in STGD1.		VAR_008449
	Natural variant	1439	1	G → D in STGD1.		VAR_008450
	Natural variant	1440	1	F → S in STGD1.		VAR_008451
	Natural variant	1440	1	F → V in STGD1. Ref.15		VAR_012573
	Natural variant	1443	1	R → H in STGD1. Ref.15		VAR_012574
	Natural variant	1486	1	P → L in STGD1. Ref.15 Ref.27		VAR_008452
	Natural variant	1488	1	C → F in STGD1.		VAR_012575
	Natural variant	1488	1	C → R in STGD1 and FFM; reduced retinal-stimulated ATP hydrolysis. Ref.13 Ref.27 Ref.24		VAR_008453
	Natural variant	1488	1	C → Y in STGD1. Ref.15		VAR_012576
	Natural variant	1490	1	C → Y in STGD1 and CORD3; reduced retinal-stimulated ATP hydrolysis. Ref.27 Ref.16		VAR_008454
	Natural variant	1508	1	G → C in FFM. Ref.9		VAR_012577
	Natural variant	1513	1	Q → R in STGD1.		VAR_012578
	Natural variant	1517	1	R → S in ARMD2. dbSNP rs1800550.		VAR_008455
	Natural variant	1525	1	L → P in STGD1.		VAR_012579
	Natural variant	1526	1	T → M in STGD1; reduced retinal-stimulated ATP hydrolysis. Ref.27		VAR_008456
	Natural variant	1532	1	D → N in STGD1. Ref.27		VAR_008457
	Natural variant	1537	1	T → M in STGD1. Ref.15		VAR_012580
	Natural variant	1562	1	I → T in STGD1, FFM, ARMD2 and CORD3. dbSNP rs1762111. Ref.15 Ref.27 Ref.24		VAR_008458
	Natural variant	1578	1	G → R in ARMD2. dbSNP rs1800551.		VAR_008459
	Natural variant	1598	1	A → D in CORD3. Ref.16		VAR_012581
	Natural variant	1631	1	L → P in STGD1.		VAR_008460
	Natural variant	1637	1	A → T Rare polymorphism. Ref.27		VAR_012582
	Natural variant	1640	1	R → Q in STGD1, FFM and CORD3. Ref.19 Ref.27 Ref.24		VAR_012583
	Natural variant	1640	1	R → W in STGD1 and CORD3. Ref.9 Ref.27		VAR_008461
	Natural variant	1652	1	Y → D in STGD1. Ref.13		VAR_008462
	Natural variant	1681 – 1685	5	Missing in STGD1; highly reduced ATP-binding capacity.		VAR_012584
	Natural variant	1689	1	S → P in STGD1. Ref.15		VAR_012585
	Natural variant	1693	1	V → I in STGD1.		VAR_012586
	Natural variant	1696	1	S → N in STGD1.		VAR_008463
	Natural variant	1703	1	Q → K in STGD1.		VAR_008464
	Natural variant	1705	1	R → L in STGD1. Ref.15		VAR_012587
	Natural variant	1729	1	L → P in STGD1. Ref.13		VAR_008465
	Natural variant	1733	1	M → T in STGD1. Ref.15		VAR_012588
	Natural variant	1736	1	S → P in STGD1.		VAR_012589
	Natural variant	1748	1	G → R in STGD1. Ref.15		VAR_012590
	Natural variant	1761 – 1763	3	Missing in STGD1; highly reduced ATP-binding capacity.		VAR_012591
	Natural variant	1763	1	L → P in STGD1. Ref.15		VAR_012592
	Natural variant	1776	1	P → L in STGD1. Ref.27		VAR_012593
	Natural variant	1780	1	P → A in STGD1. Ref.17		VAR_012594
	Natural variant	1794	1	A → D in STGD1.		VAR_008466
	Natural variant	1799	1	N → D in STGD1. Ref.25		VAR_012595
	Natural variant	1805	1	N → D in STGD1. Ref.25		VAR_012596
	Natural variant	1817	1	E → D		VAR_012597
	Natural variant	1820	1	R → P in STGD1.		VAR_008467
	Natural variant	1838	1	H → Y in STGD1.		VAR_008468
	Natural variant	1843	1	R → W in STGD1.		VAR_008469
	Natural variant	1846	1	I → T		VAR_008494
	Natural variant	1868	1	N → I Slightly reduced retinal-stimulated ATP hydrolysis. dbSNP rs1801466. Ref.15 Ref.21 Ref.27 Ref.24 Ref.22		VAR_008470
	Natural variant	1884	1	V → E in STGD1.		VAR_012598
	Natural variant	1885	1	E → K in STGD1. Ref.15		VAR_012599
	Natural variant	1886	1	G → E in STGD1; highly reduced ATP-binding capacity.		VAR_008471
	Natural variant	1890	1	Missing in STGD1.		VAR_008472
	Natural variant	1896	1	V → D in STGD1.		VAR_012600
	Natural variant	1898	1	R → H in STGD1 and ARMD2. dbSNP rs1800552. Ref.15 Ref.17		VAR_008473
	Natural variant	1921	1	V → M		VAR_012601
	Natural variant	1940	1	L → P in STGD1 and FFM. Ref.25		VAR_012602
	Natural variant	1948	1	P → L		VAR_008474
	Natural variant	1961	1	G → E in STGD1 and FFM; frequent mutation; may be associated with ARMD2; inhibition of ATP hydrolysis by retinal. dbSNP rs1800553. Ref.13 Ref.15 Ref.19 Ref.27 Ref.14 Ref.23		VAR_008475
	Natural variant	1970	1	L → F in ARMD2 and FFM. dbSNP rs1800554. Ref.9 Ref.15		VAR_008476
	Natural variant	1971	1	L → R in FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis. Ref.9		VAR_012603
	Natural variant	1975	1	G → R in STGD1. Ref.15		VAR_012604
	Natural variant	1977	1	G → S in STGD1; highly reduced ATP-binding capacity; inhibition of ATP hydrolysis by retinal. Ref.9 Ref.15 Ref.27		VAR_008477
	Natural variant	2027	1	L → F in STGD1 and FFM; highly reduced ATP-binding capacity. Ref.27 Ref.24		VAR_008478
	Natural variant	2030	1	R → Q in STGD1 and FFM. Ref.27 Ref.24		VAR_008480
	Natural variant	2035	1	L → P in STGD1. Ref.27		VAR_012605
	Natural variant	2038	1	R → W in STGD1; highly reduced ATP-binding capacity. Ref.13		VAR_008495
	Natural variant	2050	1	V → L in STGD1. Ref.27		VAR_008481
	Natural variant	2059	1	G → A		VAR_012606
	Natural variant	2060	1	L → R in CORD3. Ref.25		VAR_012607
	Natural variant	2071	1	Y → F in STGD1.		VAR_012608
	Natural variant	2077	1	R → G in STGD1. Ref.15		VAR_012609
	Natural variant	2077	1	R → W in STGD1; highly reduced ATP-binding capacity. Ref.13 Ref.15		VAR_008482
	Natural variant	2096	1	E → K in STGD1; inhibition of ATP hydrolysis by retinal.		VAR_008483
	Natural variant	2106	1	R → C in STGD1 and FFM; reduced ATP-binding capacity. Ref.24		VAR_008484
	Natural variant	2107	1	R → C in STGD1. Ref.27		VAR_012610
	Natural variant	2107	1	R → H in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. Ref.9 Ref.13 Ref.25 Ref.27 Ref.22		VAR_008485
	Natural variant	2128	1	H → R in STGD1. Ref.13		VAR_008486
	Natural variant	2131	1	E → K in STGD1.		VAR_008487
	Natural variant	2139	1	R → W in STGD1. Ref.27		VAR_008488
	Natural variant	2146	1	G → D in CORD3. Ref.27		VAR_012611
	Natural variant	2149	1	R → L in STGD1.		VAR_012612
	Natural variant	2150	1	C → R in STGD1. Ref.27		VAR_012613
	Natural variant	2150	1	C → Y in STGD1 and CORD3. Ref.13 Ref.27		VAR_008489
	Natural variant	2160	1	K → R in STGD1.		VAR_008490
	Natural variant	2177	1	D → N May be associated with ARMD2; increased retinal-stimulated ATP hydrolysis. dbSNP rs1800555. Ref.15 Ref.14 Ref.23		VAR_008491
	Natural variant	2216	1	A → V		VAR_012614
	Natural variant	2229	1	L → P in STGD1.		VAR_012615
	Natural variant	2241	1	L → V in STGD1. Ref.15		VAR_012616
	Natural variant	2255	1	S → I: dbSNP rs6666652. Ref.25 Ref.24 Ref.22		VAR_009157
	Natural variant	2263	1	R → L in STGD1.		VAR_012617
Experimental info
	Mutagenesis	966	1	G → D: Abolishes basal and retinal-stimulated ATP hydrolysis. Ref.20
	Mutagenesis	969	1	K → M: Abolishes basal and retinal-stimulated ATP hydrolysis. Ref.20
	Mutagenesis	1975	1	G → D: Inhibition of retinal-stimulated ATP hydrolysis. Ref.20
	Mutagenesis	1978	1	K → M: Inhibition of retinal-stimulated ATP hydrolysis. Ref.20
	Sequence conflict	722	1	G → V in AAC23915. Ref.2
	Sequence conflict	849	1	V → C in AAC51144. Ref.1
	Sequence conflict	882	1	G → S Ref.1
	Sequence conflict	882	1	G → S Ref.3
	Sequence conflict	941	1	C → S in AAC23915. Ref.2
	Sequence conflict	1116	1	S → P in AAC51144. Ref.1
	Sequence conflict	1125 – 1126	2	LL → HQ in AAC51144. Ref.1
	Sequence conflict	1395	1	P → L Ref.1
	Sequence conflict	1395	1	P → L Ref.3
	Sequence conflict	1465	1	S → C in AAC05632. Ref.4
	Sequence conflict	1518	1	S → T in AAC05632. Ref.4
	Sequence conflict	1733	1	M → V in AAC23915. Ref.2
	Sequence conflict	1989	1	T → N in AAC23915. Ref.2
	Sequence conflict	2119	1	E → K in AAC51144. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P78363-1 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: 6E7012D3041CD043	FASTA	2,273	255,944
	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

References

	« Hide 'large scale' referencesShow '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: 9054934] [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: 9202155] [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: 9503029] [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: 9490294] [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]	"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: 10075733] [Abstract] Cited for: CHARACTERIZATION.
[7]	"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: 9466990] [Abstract] Cited for: DISEASE.
[8]	"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: 9295268] [Abstract] Cited for: VARIANTS ARMD2, VARIANTS.
[9]	"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: 9781034] [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.
[10]	"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: 9973280] [Abstract] Cited for: VARIANTS STGD1.
[11]	"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: 10090887] [Abstract] Cited for: VARIANTS STGD1, VARIANTS.
[12]	"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: 10612508] [Abstract] Cited for: VARIANT STGD1 TYR-54, VARIANT ALA-863.
[13]	"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: 10206579] [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.
[14]	"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. , 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: 10880298] [Abstract] Cited for: VARIANTS GLU-1961 AND ASN-2177.
[15]	"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: 10958763] [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.
[16]	"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: 10958761] [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.
[17]	"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: 10746567] [Abstract] Cited for: VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 AND HIS-1898, VARIANT GLN-943.
[18]	"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: 10634594] [Abstract] Cited for: VARIANTS STGD1.
[19]	"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: 10711710] [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.
[20]	"Biochemical defects in ABCR protein variants associated with human retinopathies." Sun H., Smallwood P.M., Nathans J. Nat. Genet. 26:242-246(2000) [PubMed: 11017087] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS, MUTAGENESIS OF GLY-966; LYS-969; GLY-1975 AND LYS-1978.
[21]	"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: 11594993] [Abstract] Cited for: VARIANT STGD1 ASN-972, VARIANTS GLN-943; ILE-1868 AND LEU-1948.
[22]	"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: 11384574] [Abstract] Cited for: VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, VARIANTS HIS-212; ARG-423; ILE-1868 AND ILE-2255.
[23]	"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: 11346402] [Abstract] Cited for: VARIANTS GLU-1961 AND ASN-2177.
[24]	"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: 11379881] [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.
[25]	"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: 11385708] [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.
[26]	"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: 11328725] [Abstract] Cited for: VARIANTS STGD1, VARIANTS.
[27]	"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: 11527935] [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.
[28]	"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: 12111378] [Abstract] Cited for: VARIANT ARG-423.
[29]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-224.
+	Additional computationally mapped references.

Web resources

Mutations of the ABCA4 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	U88667 mRNA. Translation: AAC51144.1. AF000148 mRNA. Translation: AAC23915.1. Y15635 , 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.
IPI	IPI00297763.
RefSeq	NP_000341.2.
UniGene	Hs.416707
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P78363.
Protein family/group databases
TCDB	3.A.1.211.2. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	P78363.
Proteomic databases
PRIDE	P78363.
Genome annotation databases
Ensembl	ENST00000370225; ENSP00000359245; ENSG00000198691; Homo sapiens. [Genome view]
GeneID	24.
KEGG	hsa:24.
UCSC	uc001dqh.1. human.
Organism-specific databases
CTD	24.
GeneCards	GC01M094230.
H-InvDB	HIX0028510.
HGNC	HGNC:34. ABCA4.
MIM	153800. phenotype. 248200. phenotype. 601691. gene. 601718. phenotype. 604116. phenotype.
Orphanet	1872. Cone rod dystrophy. 279. Macular degeneration, age-related. 791. Retinitis pigmentosa. 827. Stargardt disease.
PharmGKB	PA24379.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P78363.
OMA	RRMLWNT
OrthoDB	EOG954CJP
Gene expression databases
ArrayExpress	P78363.
Bgee	P78363.
CleanEx	HS_ABCA4.
Genevestigator	P78363.
GermOnline	ENSG00000198691. Homo sapiens.
Family and domain databases
InterPro	IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR003593. ATPase_AAA+_core. IPR005951. Rim_ABC_transpt. [Graphical view]
Pfam	PF00005. ABC_tran. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. [Graphical view]
TIGRFAMs	TIGR01257. rim_protein. 1 hit.
PROSITE	PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	75.
SOURCE	Search...

Entry information

Entry name

ABCA4_HUMAN

Accession

Primary (citable) accession number: P78363
Secondary accession number(s): O15112 , O60438, O60915, Q4LE31

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 24, 2009
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.