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UniProtKB - P78363 (ABCA4_HUMAN)

Protein

Retinal-specific ATP-binding cassette transporter

Gene

ABCA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi963 – 970ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi1972 – 1979ATP 2PROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processSensory transduction, Transport, Vision
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-382556 ABC-family proteins mediated transport

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.1.211.2 the atp-binding cassette (abc) superfamily

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000347

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ABCA4
Synonyms:ABCR
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000198691.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:34 ABCA4

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601691 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P78363

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 21CytoplasmicAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei22 – 42HelicalSequence analysisAdd BLAST21
Topological domaini43 – 646ExtracellularAdd BLAST604
Transmembranei647 – 667HelicalSequence analysisAdd BLAST21
Transmembranei700 – 720HelicalSequence analysisAdd BLAST21
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Transmembranei760 – 780HelicalSequence analysisAdd BLAST21
Transmembranei836 – 856HelicalSequence analysisAdd BLAST21
Topological domaini857 – 1376CytoplasmicAdd BLAST520
Transmembranei1377 – 1397HelicalSequence analysisAdd BLAST21
Topological domaini1398 – 1727ExtracellularAdd BLAST330
Transmembranei1728 – 1748HelicalSequence analysisAdd BLAST21
Transmembranei1760 – 1780HelicalSequence analysisAdd BLAST21
Transmembranei1793 – 1813HelicalSequence analysisAdd BLAST21
Transmembranei1832 – 1852HelicalSequence analysisAdd BLAST21
Transmembranei1874 – 1894HelicalSequence analysisAdd BLAST21
Topological domaini1895 – 2273CytoplasmicAdd BLAST379

Keywords - Cellular componenti

Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Stargardt disease 1 (STGD1)18 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:248200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01249413 – 15Missing in STGD1. 1 Publication3
Natural variantiVAR_00839818R → W in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs121909205EnsemblClinVar.1
Natural variantiVAR_00839924R → H in STGD1. Corresponds to variant dbSNP:rs62645958EnsemblClinVar.1
Natural variantiVAR_00840054C → Y in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs150774447EnsemblClinVar.1
Natural variantiVAR_01249558N → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748524EnsemblClinVar.1
Natural variantiVAR_01249660A → E in STGD1. 1 Publication1
Natural variantiVAR_01249760A → T in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751411EnsemblClinVar.1
Natural variantiVAR_00849260A → V in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs55732384EnsemblClinVar.1
Natural variantiVAR_01249868P → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62654397EnsemblClinVar.1
Natural variantiVAR_01249968P → R in STGD1. Corresponds to variant dbSNP:rs62654397EnsemblClinVar.1
Natural variantiVAR_01250072G → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751412EnsemblClinVar.1
Natural variantiVAR_00840275C → G in STGD1. Corresponds to variant dbSNP:rs61748526EnsemblClinVar.1
Natural variantiVAR_01250177V → E in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748527EnsemblClinVar.1
Natural variantiVAR_00840396N → D in STGD1. Corresponds to variant dbSNP:rs61748529EnsemblClinVar.1
Natural variantiVAR_00840496N → H in STGD1. Corresponds to variant dbSNP:rs61748529EnsemblClinVar.1
Natural variantiVAR_012502100S → P in STGD1. Corresponds to variant dbSNP:rs61748530EnsemblClinVar.1
Natural variantiVAR_012504156I → V in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62646863EnsemblClinVar.1
Natural variantiVAR_012505190Q → H in STGD1. 1 PublicationCorresponds to variant dbSNP:rs281865397EnsemblClinVar.1
Natural variantiVAR_008405192A → T in STGD1. Corresponds to variant dbSNP:rs61748535EnsemblClinVar.1
Natural variantiVAR_012506206S → R in STGD1; reduced basal and retinal-stimulated ATP-hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs61748536EnsemblClinVar.1
Natural variantiVAR_012508220R → C in STGD1. Corresponds to variant dbSNP:rs61748538EnsemblClinVar.1
Natural variantiVAR_012509230C → S in STGD1. 1 PublicationCorresponds to variant dbSNP:rs1057518767Ensembl.1
Natural variantiVAR_012510244L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62646864EnsemblClinVar.1
Natural variantiVAR_012511247N → S in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62645950EnsemblClinVar.1
Natural variantiVAR_008407249D → G in STGD1. Corresponds to variant dbSNP:rs62646865EnsemblClinVar.1
Natural variantiVAR_008408300T → N in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748544EnsemblClinVar.1
Natural variantiVAR_012512309P → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748545EnsemblClinVar.1
Natural variantiVAR_012513328E → V in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751419EnsemblClinVar.1
Natural variantiVAR_012514333R → W in STGD1. Corresponds to variant dbSNP:rs61748546EnsemblClinVar.1
Natural variantiVAR_008409336S → C in STGD1. Corresponds to variant dbSNP:rs61748547EnsemblClinVar.1
Natural variantiVAR_008410340Y → D in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748548EnsemblClinVar.1
Natural variantiVAR_012516380N → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748549EnsemblClinVar.1
Natural variantiVAR_008412445S → R in STGD1. Corresponds to variant dbSNP:rs61748552EnsemblClinVar.1
Natural variantiVAR_008414523D → E in STGD1. Corresponds to variant dbSNP:rs62646868EnsemblClinVar.1
Natural variantiVAR_012518525F → C in STGD1. 1 Publication1
Natural variantiVAR_012519537R → C in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748556EnsemblClinVar.1
Natural variantiVAR_008415541L → P in STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis. 5 PublicationsCorresponds to variant dbSNP:rs61751392EnsemblClinVar.1
Natural variantiVAR_012520549A → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748557EnsemblClinVar.1
Natural variantiVAR_012521550G → R in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61748558EnsemblClinVar.1
Natural variantiVAR_008416572R → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748559EnsemblClinVar.1
Natural variantiVAR_008417572R → Q in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61748559EnsemblClinVar.1
Natural variantiVAR_012523602R → Q in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749410EnsemblClinVar.1
Natural variantiVAR_008418602R → W in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61749409EnsemblClinVar.1
Natural variantiVAR_012524607G → R in STGD1. 3 PublicationsCorresponds to variant dbSNP:rs61749412EnsemblClinVar.1
Natural variantiVAR_012525607G → W in STGD1. Corresponds to variant dbSNP:rs61749412EnsemblClinVar.1
Natural variantiVAR_008419608F → I in STGD1. Corresponds to variant dbSNP:rs61752398EnsemblClinVar.1
Natural variantiVAR_012526635Q → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749414EnsemblClinVar.1
Natural variantiVAR_012527636Q → H in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752400EnsemblClinVar.1
Natural variantiVAR_012528643V → M in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749417EnsemblClinVar.1
Natural variantiVAR_008421645D → N in STGD1. Corresponds to variant dbSNP:rs61749418EnsemblClinVar.1
Natural variantiVAR_012529653R → C in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61749420EnsemblClinVar.1
Natural variantiVAR_012530686L → S in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752402EnsemblClinVar.1
Natural variantiVAR_012531716T → M in STGD1. Corresponds to variant dbSNP:rs61749426EnsemblClinVar.1
Natural variantiVAR_012532764C → Y in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749428EnsemblClinVar.1
Natural variantiVAR_012534765S → N in STGD1. Corresponds to variant dbSNP:rs61749429EnsemblClinVar.1
Natural variantiVAR_012533765S → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752404EnsemblClinVar.1
Natural variantiVAR_012535767V → D in STGD1. 3 PublicationsCorresponds to variant dbSNP:rs61751395EnsemblClinVar.1
Natural variantiVAR_012536797L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749432EnsemblClinVar.1
Natural variantiVAR_008423821W → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749433EnsemblClinVar.1
Natural variantiVAR_012537824I → T in STGD1. 1 Publication1
Natural variantiVAR_012538849V → A in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749435EnsemblClinVar.1
Natural variantiVAR_008424851G → D in STGD1; highly reduced ATP-binding capacity. Corresponds to variant dbSNP:rs61749436EnsemblClinVar.1
Natural variantiVAR_012539854A → T in STGD1. Corresponds to variant dbSNP:rs61749437EnsemblClinVar.1
Natural variantiVAR_008425863G → A in STGD1, FFM and CORD3; mild alteration probably leading to disease phenotype only in combination with a more severe allele; frequent mutation in northern Europe in linkage disequilibrium with the polymorphic variant Q-943; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis. 5 PublicationsCorresponds to variant dbSNP:rs76157638EnsemblClinVar.1
Natural variantiVAR_012541873F → L in STGD1. Corresponds to variant dbSNP:rs62642570EnsemblClinVar.1
Natural variantiVAR_012542897T → I in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61749440EnsemblClinVar.1
Natural variantiVAR_008427931V → M in STGD1. 1 PublicationCorresponds to variant dbSNP:rs58331765EnsemblClinVar.1
Natural variantiVAR_012544935V → A in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749444EnsemblClinVar.1
Natural variantiVAR_008429957Q → R in STGD1. Corresponds to variant dbSNP:rs61749448EnsemblClinVar.1
Natural variantiVAR_012546959T → I in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752409EnsemblClinVar.1
Natural variantiVAR_008430965N → S in STGD1; reduced retinal-stimulated ATP hydrolysis. 2 PublicationsCorresponds to variant dbSNP:rs201471607EnsemblClinVar.1
Natural variantiVAR_012547971T → N in STGD1; highly reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis. Corresponds to variant dbSNP:rs61749450EnsemblClinVar.1
Natural variantiVAR_012548972T → N in STGD1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs61749451EnsemblClinVar.1
Natural variantiVAR_012549974S → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs281865400EnsemblClinVar.1
Natural variantiVAR_008431978G → C in STGD1. Corresponds to variant dbSNP:rs61749452EnsemblClinVar.1
Natural variantiVAR_012550989V → A in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61749454EnsemblClinVar.1
Natural variantiVAR_0125521014L → R in STGD1. Corresponds to variant dbSNP:rs61749456EnsemblClinVar.1
Natural variantiVAR_0125531019T → A in STGD1. Corresponds to variant dbSNP:rs61749457EnsemblClinVar.1
Natural variantiVAR_0125541019T → M in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs201855602EnsemblClinVar.1
Natural variantiVAR_0125551022E → K in STGD1. Corresponds to variant dbSNP:rs61749459EnsemblClinVar.1
Natural variantiVAR_0125561031K → E in STGD1. Corresponds to variant dbSNP:rs61750060EnsemblClinVar.1
Natural variantiVAR_0084321036E → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750061EnsemblClinVar.1
Natural variantiVAR_0084331038A → V in STGD1, FFM and CORD3; frequent mutation; reduced ATP-binding and retinal-stimulated ATP hydrolysis. 8 PublicationsCorresponds to variant dbSNP:rs61751374EnsemblClinVar.1
Natural variantiVAR_0125571055R → W in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752412EnsemblClinVar.1
Natural variantiVAR_0125581063S → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752413EnsemblClinVar.1
Natural variantiVAR_0084341071S → L in STGD1; reduced ATP-binding capacity. Corresponds to variant dbSNP:rs61750065EnsemblClinVar.1
Natural variantiVAR_0084351072V → A in STGD1. 1
Natural variantiVAR_0125591087E → D in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752416EnsemblClinVar.1
Natural variantiVAR_0084361087E → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751398EnsemblClinVar.1
Natural variantiVAR_0125611097R → C in STGD1. 1 Publication1
Natural variantiVAR_0125631108R → H in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750121EnsemblClinVar.1
Natural variantiVAR_0125641108R → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750121EnsemblClinVar.1
Natural variantiVAR_0084371112T → N in STGD1. Corresponds to variant dbSNP:rs61750122EnsemblClinVar.1
Natural variantiVAR_0125651129R → C in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. 1 PublicationCorresponds to variant dbSNP:rs779426136EnsemblClinVar.1
Natural variantiVAR_0084401201L → R in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. 2 PublicationsCorresponds to variant dbSNP:rs61750126EnsemblClinVar.1
Natural variantiVAR_0084411204D → N in STGD1. Corresponds to variant dbSNP:rs61750127EnsemblClinVar.1
Natural variantiVAR_0125671250L → P in STGD1. Corresponds to variant dbSNP:rs61750128EnsemblClinVar.1
Natural variantiVAR_0125691300R → Q in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750129EnsemblClinVar.1
Natural variantiVAR_0084431380P → L in STGD1; reduced ATP-binding capacity. 3 PublicationsCorresponds to variant dbSNP:rs61750130EnsemblClinVar.1
Natural variantiVAR_0125701388L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750131EnsemblClinVar.1
Natural variantiVAR_0125711399E → K in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs62642573EnsemblClinVar.1
Natural variantiVAR_0084441406H → Y in STGD1. Corresponds to variant dbSNP:rs61750133EnsemblClinVar.1
Natural variantiVAR_0084451408W → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750134EnsemblClinVar.1
Natural variantiVAR_0084461408W → R in STGD1; reduced retinal-stimulated ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs61750135EnsemblClinVar.1
Natural variantiVAR_0084481429V → A in STGD1. Corresponds to variant dbSNP:rs61752432EnsemblClinVar.1
Natural variantiVAR_0125721430L → P in STGD1. 1 Publication1
Natural variantiVAR_0084491433V → I in STGD1. 1 PublicationCorresponds to variant dbSNP:rs56357060EnsemblClinVar.1
Natural variantiVAR_0084501439G → D in STGD1. Corresponds to variant dbSNP:rs61750140EnsemblClinVar.1
Natural variantiVAR_0084511440F → S in STGD1. Corresponds to variant dbSNP:rs61750141EnsemblClinVar.1
Natural variantiVAR_0125731440F → V in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61752433EnsemblClinVar.1
Natural variantiVAR_0125741443R → H in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750142EnsemblClinVar.1
Natural variantiVAR_0084521486P → L in STGD1. 3 PublicationsCorresponds to variant dbSNP:rs61750145EnsemblClinVar.1
Natural variantiVAR_0125751488C → F in STGD1. Corresponds to variant dbSNP:rs61750147EnsemblClinVar.1
Natural variantiVAR_0125761488C → Y in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750147EnsemblClinVar.1
Natural variantiVAR_0125781513Q → R in STGD1. Corresponds to variant dbSNP:rs281865402EnsemblClinVar.1
Natural variantiVAR_0125791525L → P in STGD1. Corresponds to variant dbSNP:rs61750151EnsemblClinVar.1
Natural variantiVAR_0084561526T → M in STGD1; reduced retinal-stimulated ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs61750152EnsemblClinVar.1
Natural variantiVAR_0084571532D → N in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62642574EnsemblClinVar.1
Natural variantiVAR_0125801537T → M in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62642575EnsemblClinVar.1
Natural variantiVAR_0084581562I → T in STGD1, FFM, ARMD2 and CORD3. 3 PublicationsCorresponds to variant dbSNP:rs1762111EnsemblClinVar.1
Natural variantiVAR_0084601631L → P in STGD1. Corresponds to variant dbSNP:rs61750158EnsemblClinVar.1
Natural variantiVAR_0125831640R → Q in STGD1, FFM and CORD3. 4 PublicationsCorresponds to variant dbSNP:rs61751403EnsemblClinVar.1
Natural variantiVAR_0084621652Y → D in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750560EnsemblClinVar.1
Natural variantiVAR_0125841681 – 1685Missing in STGD1; highly reduced ATP-binding capacity. 5
Natural variantiVAR_0125851689S → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61753020EnsemblClinVar.1
Natural variantiVAR_0125861693V → I in STGD1. Corresponds to variant dbSNP:rs61750563EnsemblClinVar.1
Natural variantiVAR_0084631696S → N in STGD1. Corresponds to variant dbSNP:rs61750564EnsemblClinVar.1
Natural variantiVAR_0084641703Q → K in STGD1. 1
Natural variantiVAR_0125871705R → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61753021EnsemblClinVar.1
Natural variantiVAR_0084651729L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750567EnsemblClinVar.1
Natural variantiVAR_0125881733M → T in STGD1. 1 PublicationCorresponds to variant dbSNP:rs765563320Ensembl.1
Natural variantiVAR_0125891736S → P in STGD1. Corresponds to variant dbSNP:rs61750568EnsemblClinVar.1
Natural variantiVAR_0125901748G → R in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61753025EnsemblClinVar.1
Natural variantiVAR_0125911761 – 1763Missing in STGD1; highly reduced ATP-binding capacity. 3
Natural variantiVAR_0125921763L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61753028EnsemblClinVar.1
Natural variantiVAR_0125931776P → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs281865404EnsemblClinVar.1
Natural variantiVAR_0125941780P → A in STGD1. 1 PublicationCorresponds to variant dbSNP:rs121909207EnsemblClinVar.1
Natural variantiVAR_0084661794A → D in STGD1. Corresponds to variant dbSNP:rs61751406EnsemblClinVar.1
Natural variantiVAR_0125951799N → D in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61750574EnsemblClinVar.1
Natural variantiVAR_0125961805N → D in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61753029EnsemblClinVar.1
Natural variantiVAR_0084671820R → P in STGD1. Corresponds to variant dbSNP:rs62646875EnsemblClinVar.1
Natural variantiVAR_0084681838H → Y in STGD1. Corresponds to variant dbSNP:rs62642562EnsemblClinVar.1
Natural variantiVAR_0084691843R → W in STGD1. Corresponds to variant dbSNP:rs62642576EnsemblClinVar.1
Natural variantiVAR_0125981884V → E in STGD1. Corresponds to variant dbSNP:rs62642578EnsemblClinVar.1
Natural variantiVAR_0125991885E → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62642563EnsemblClinVar.1
Natural variantiVAR_0084711886G → E in STGD1; highly reduced ATP-binding capacity. Corresponds to variant dbSNP:rs62642579EnsemblClinVar.1
Natural variantiVAR_0084721890Missing in STGD1. 1
Natural variantiVAR_0126001896V → D in STGD1. Corresponds to variant dbSNP:rs61750636EnsemblClinVar.1
Natural variantiVAR_0126041975G → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61753036EnsemblClinVar.1
Natural variantiVAR_0126052035L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750642EnsemblClinVar.1
Natural variantiVAR_0084952038R → W in STGD1; highly reduced ATP-binding capacity. 1 PublicationCorresponds to variant dbSNP:rs61750643EnsemblClinVar.1
Natural variantiVAR_0084812050V → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs41292677EnsemblClinVar.1
Natural variantiVAR_0126082071Y → F in STGD1. 1
Natural variantiVAR_0126092077R → G in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750645EnsemblClinVar.1
Natural variantiVAR_0084822077R → W in STGD1; highly reduced ATP-binding capacity. 2 PublicationsCorresponds to variant dbSNP:rs61750645EnsemblClinVar.1
Natural variantiVAR_0084832096E → K in STGD1; inhibition of ATP hydrolysis by retinal. Corresponds to variant dbSNP:rs61750646EnsemblClinVar.1
Natural variantiVAR_0126102107R → C in STGD1. 1 PublicationCorresponds to variant dbSNP:rs2297669Ensembl.1
Natural variantiVAR_0084852107R → H in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine. 6 PublicationsCorresponds to variant dbSNP:rs62642564EnsemblClinVar.1
Natural variantiVAR_0084862128H → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750651EnsemblClinVar.1
Natural variantiVAR_0084872131E → K in STGD1. Corresponds to variant dbSNP:rs61750652EnsemblClinVar.1
Natural variantiVAR_0084882139R → W in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750653EnsemblClinVar.1
Natural variantiVAR_0126122149R → L in STGD1. Corresponds to variant dbSNP:rs61750655EnsemblClinVar.1
Natural variantiVAR_0126132150C → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61750656EnsemblClinVar.1
Natural variantiVAR_0084902160K → R in STGD1. Corresponds to variant dbSNP:rs281865405EnsemblClinVar.1
Natural variantiVAR_0126152229L → P in STGD1. Corresponds to variant dbSNP:rs61750659EnsemblClinVar.1
Natural variantiVAR_0126162241L → V in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61748521EnsemblClinVar.1
Natural variantiVAR_0126172263R → L in STGD1. Corresponds to variant dbSNP:rs281865407EnsemblClinVar.1
Fundus flavimaculatus (FFM)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive retinal disorder very similar to Stargardt disease. In contrast to Stargardt disease, FFM is characterized by later onset and slowly progressive course.
See also OMIM:248200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01249311L → P in FFM. 1 PublicationCorresponds to variant dbSNP:rs62645946EnsemblClinVar.1
Natural variantiVAR_012515339W → G in FFM. 1 PublicationCorresponds to variant dbSNP:rs61751420EnsemblClinVar.1
Natural variantiVAR_012551991G → R in FFM. 1 PublicationCorresponds to variant dbSNP:rs61749455EnsemblClinVar.1
Natural variantiVAR_0125601091G → E in FFM. 1 PublicationCorresponds to variant dbSNP:rs61752417EnsemblClinVar.1
Natural variantiVAR_0125681253T → M in FFM; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs61752424EnsemblClinVar.1
Natural variantiVAR_0125771508G → C in FFM. 1 Publication1
Natural variantiVAR_0126031971L → R in FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs61753034EnsemblClinVar.1
Macular degeneration, age-related, 2 (ARMD2)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:153800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067427762A → E in ARMD2. 1 Publication1
Natural variantiVAR_0084471428T → M in ARMD2. Corresponds to variant dbSNP:rs1800549EnsemblClinVar.1
Natural variantiVAR_0084551517R → S in ARMD2. Corresponds to variant dbSNP:rs1800550EnsemblClinVar.1
Natural variantiVAR_0084591578G → R in ARMD2. Corresponds to variant dbSNP:rs1800551EnsemblClinVar.1
Natural variantiVAR_0674281724W → C in ARMD2. 1 Publication1
Natural variantiVAR_0674292047I → N in ARMD2. 1 Publication1
Natural variantiVAR_0674302137C → Y in ARMD2. 1 Publication1
Cone-rod dystrophy 3 (CORD3)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors.
See also OMIM:604116
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0125811598A → D in CORD3. 1 PublicationCorresponds to variant dbSNP:rs61750155EnsemblClinVar.1
Natural variantiVAR_0126072060L → R in CORD3. 2 PublicationsCorresponds to variant dbSNP:rs61753039EnsemblClinVar.1
Natural variantiVAR_0126112146G → D in CORD3. 1 PublicationCorresponds to variant dbSNP:rs61753044EnsemblClinVar.1
Retinitis pigmentosa 19 (RP19)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:601718

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi966G → D: Abolishes basal and retinal-stimulated ATP hydrolysis. 1 Publication1
Mutagenesisi969K → M: Abolishes basal and retinal-stimulated ATP hydrolysis. 1 Publication1
Mutagenesisi1975G → D: Inhibition of retinal-stimulated ATP hydrolysis. 1 Publication1
Mutagenesisi1978K → M: Inhibition of retinal-stimulated ATP hydrolysis. 1 Publication1

Keywords - Diseasei

Age-related macular degeneration, Cone-rod dystrophy, Disease mutation, Retinitis pigmentosa, Stargardt disease

Organism-specific databases

DisGeNET

More...DisGeNETi		24

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		ABCA4

MalaCards human disease database

More...MalaCardsi		ABCA4
MIMi153800 phenotype
248200 phenotype
601718 phenotype
604116 phenotype

Open Targets

More...OpenTargetsi		ENSG00000198691

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		1872 Cone rod dystrophy
279 NON RARE IN EUROPE: Age-related macular degeneration
791 Retinitis pigmentosa
827 Stargardt disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24379

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ABCA4

Domain mapping of disease mutations (DMDM)

More...DMDMi		6707663

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000933011 – 2273Retinal-specific ATP-binding cassette transporterAdd BLAST2273

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi75 ↔ 324By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi98N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi415N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi444N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi504N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1469N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1488 ↔ 1502By similarity
Glycosylationi1529N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1588N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1662N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P78363

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P78363

PeptideAtlas

More...PeptideAtlasi		P78363

PRoteomics IDEntifications database

More...PRIDEi		P78363

ProteomicsDB human proteome resource

More...ProteomicsDBi		57593

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P78363

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P78363

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000198691 Expressed in 92 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

More...CleanExi		HS_ABCA4

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P78363 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P78363 HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		106542, 1 interactor

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P78363

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000359245

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P78363

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P78363

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini929 – 1160ABC transporter 1PROSITE-ProRule annotationAdd BLAST232
Domaini1938 – 2170ABC transporter 2PROSITE-ProRule annotationAdd BLAST233

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ABC transporter superfamily. ABCA family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0059 Eukaryota
COG1131 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155624

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231547

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG050436

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P78363

KEGG Orthology (KO)

More...KOi		K05644

Identification of Orthologs from Complete Genome Data

More...OMAi		HPWMYGQ

Database of Orthologous Groups

More...OrthoDBi		EOG091G007E

Database for complete collections of gene phylogenies

More...PhylomeDBi		P78363

TreeFam database of animal gene trees

More...TreeFami		TF105191

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593 AAA+_ATPase
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR026082 ABCA
IPR005951 ABCA4/ABCR
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...PANTHERi		PTHR19229 PTHR19229, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00005 ABC_tran, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01257 rim_protein, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P78363-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS 
        60         70         80         90        100
HHECHFPNKA MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS 
       110        120        130        140        150
ILARVYRDFQ ELLMNAPESQ HLGRIWTELH ILSQFMDTLR THPERIAGRG 
       160        170        180        190        200
IRIRDILKDE ETLTLFLIKN IGLSDSVVYL LINSQVRPEQ FAHGVPDLAL 
       210        220        230        240        250
KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI EDTLYANVDF 
       260        270        280        290        300
FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT 
       310        320        330        340        350
RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG 
       360        370        380        390        400
IDSTRKDPIY SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY 
       410        420        430        440        450
TPDSPAARRI LKNANSTFEE LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM 
       460        470        480        490        500
IRDTLGNPTV KDFLNRQLGE EGITAEAILN FLYKGPRESQ ADDMANFDWR 
       510        520        530        540        550
DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS LLEENMFWAG 
       560        570        580        590        600
VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED 
       610        620        630        640        650
FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII 
       660        670        680        690        700
LNRCFPIFMV LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW 
       710        720        730        740        750
FLDSFSIMSM SIFLLTIFIM HGRILHYSDP FILFLFLLAF STATIMLCFL 
       760        770        780        790        800
LSTFFSKASL AAACSGVIYF TLYLPHILCF AWQDRMTAEL KKAVSLLSPV 
       810        820        830        840        850
AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM QMMLLDAAVY 
       860        870        880        890        900
GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL 
       910        920        930        940        950
TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN 
       960        970        980        990       1000
ITFYENQITA FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA 
      1010       1020       1030       1040       1050
VRQSLGMCPQ HNILFHHLTV AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG 
      1060       1070       1080       1090       1100
LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA KVVILDEPTS GVDPYSRRSI 
      1110       1120       1130       1140       1150
WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC SGTPLFLKNC 
      1160       1170       1180       1190       1200
FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV 
      1210       1220       1230       1240       1250
LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL 
      1260       1270       1280       1290       1300
EETLADLGLS SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR 
      1310       1320       1330       1340       1350
HPCLGPREKA GQTPQDSNVC SPGAPAAHPE GQPPPEPECP GPQLNTGTQL 
      1360       1370       1380       1390       1400
VLQHVQALLV KRFQHTIRSH KDFLAQIVLP ATFVFLALML SIVIPPFGEY 
      1410       1420       1430       1440       1450
PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF GNRCLKEGWL 
      1460       1470       1480       1490       1500
PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP 
      1510       1520       1530       1540       1550
ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF 
      1560       1570       1580       1590       1600
WVNEQRYGGI SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK 
      1610       1620       1630       1640       1650
EIPDFLKHLE TEDNIKVWFN NKGWHALVSF LNVAHNAILR ASLPKDRSPE 
      1660       1670       1680       1690       1700
EYGITVISQP LNLTKEQLSE ITVLTTSVDA VVAICVIFSM SFVPASFVLY 
      1710       1720       1730       1740       1750
LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG LVVGIFIGFQ 
      1760       1770       1780       1790       1800
KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL 
      1810       1820       1830       1840       1850
FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL 
      1860       1870       1880       1890       1900
SQAVTDVYAR FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF 
      1910       1920       1930       1940       1950
FLSQWIAEPT KEPIVDEDDD VAEERQRIIT GGNKTDILRL HELTKIYPGT 
      1960       1970       1980       1990       2000
SSPAVDRLCV GVRPGECFGL LGVNGAGKTT TFKMLTGDTT VTSGDATVAG 
      2010       2020       2030       2040       2050
KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR GVPAEEIEKV 
      2060       2070       2080       2090       2100
ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG 
      2110       2120       2130       2140       2150
MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC 
      2160       2170       2180       2190       2200
MGTIQHLKSK FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE 
      2210       2220       2230       2240       2250
RHYNMLQFQV SSSSLARIFQ LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK 
      2260       2270 
QQTESHDLPL HPRAAGASRQ AQD
Length:2,273
Mass (Da):255,944
Last modified:May 30, 2000 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6E7012D3041CD043
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6TT59F6TT59_HUMAN
Retinal-specific ATP-binding casset...
ABCA4
1,065Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti722G → V in AAC23915 (PubMed:9202155).Curated1
Sequence conflicti849V → C in AAC51144 (PubMed:9054934).Curated1
Sequence conflicti882G → S in AAC51144 (PubMed:9054934).Curated1
Sequence conflicti882G → S in CAA75729 (PubMed:9503029).Curated1
Sequence conflicti941C → S in AAC23915 (PubMed:9202155).Curated1
Sequence conflicti1116S → P in AAC51144 (PubMed:9054934).Curated1
Sequence conflicti1125 – 1126LL → HQ in AAC51144 (PubMed:9054934).Curated2
Sequence conflicti1395P → L in AAC51144 (PubMed:9054934).Curated1
Sequence conflicti1395P → L in CAA75729 (PubMed:9503029).Curated1
Sequence conflicti1465S → C in AAC05632 (PubMed:9490294).Curated1
Sequence conflicti1518S → T in AAC05632 (PubMed:9490294).Curated1
Sequence conflicti1733M → V in AAC23915 (PubMed:9202155).Curated1
Sequence conflicti1989T → N in AAC23915 (PubMed:9202155).Curated1
Sequence conflicti2119E → K in AAC51144 (PubMed:9054934).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01249311L → P in FFM. 1 PublicationCorresponds to variant dbSNP:rs62645946EnsemblClinVar.1
Natural variantiVAR_01249413 – 15Missing in STGD1. 1 Publication3
Natural variantiVAR_00839818R → W in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs121909205EnsemblClinVar.1
Natural variantiVAR_00839924R → H in STGD1. Corresponds to variant dbSNP:rs62645958EnsemblClinVar.1
Natural variantiVAR_00840054C → Y in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs150774447EnsemblClinVar.1
Natural variantiVAR_01249558N → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748524EnsemblClinVar.1
Natural variantiVAR_01249660A → E in STGD1. 1 Publication1
Natural variantiVAR_01249760A → T in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751411EnsemblClinVar.1
Natural variantiVAR_00849260A → V in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs55732384EnsemblClinVar.1
Natural variantiVAR_00840165G → E in STGD1 and CORD3. 3 PublicationsCorresponds to variant dbSNP:rs62654395EnsemblClinVar.1
Natural variantiVAR_01249868P → L in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62654397EnsemblClinVar.1
Natural variantiVAR_01249968P → R in STGD1. Corresponds to variant dbSNP:rs62654397EnsemblClinVar.1
Natural variantiVAR_01250072G → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751412EnsemblClinVar.1
Natural variantiVAR_00840275C → G in STGD1. Corresponds to variant dbSNP:rs61748526EnsemblClinVar.1
Natural variantiVAR_01250177V → E in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748527EnsemblClinVar.1
Natural variantiVAR_00840396N → D in STGD1. Corresponds to variant dbSNP:rs61748529EnsemblClinVar.1
Natural variantiVAR_00840496N → H in STGD1. Corresponds to variant dbSNP:rs61748529EnsemblClinVar.1
Natural variantiVAR_012502100S → P in STGD1. Corresponds to variant dbSNP:rs61748530EnsemblClinVar.1
Natural variantiVAR_012503152R → Q1 PublicationCorresponds to variant dbSNP:rs62646862EnsemblClinVar.1
Natural variantiVAR_012504156I → V in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62646863EnsemblClinVar.1
Natural variantiVAR_012505190Q → H in STGD1. 1 PublicationCorresponds to variant dbSNP:rs281865397EnsemblClinVar.1
Natural variantiVAR_008405192A → T in STGD1. Corresponds to variant dbSNP:rs61748535EnsemblClinVar.1
Natural variantiVAR_012506206S → R in STGD1; reduced basal and retinal-stimulated ATP-hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs61748536EnsemblClinVar.1
Natural variantiVAR_008406212R → C in STGD1 and CORD3; common mutation in southern Europe; reduced ATP-binding capacity. 7 PublicationsCorresponds to variant dbSNP:rs61750200EnsemblClinVar.1
Natural variantiVAR_012507212R → H5 PublicationsCorresponds to variant dbSNP:rs6657239EnsemblClinVar.1
Natural variantiVAR_012508220R → C in STGD1. Corresponds to variant dbSNP:rs61748538EnsemblClinVar.1
Natural variantiVAR_035736224T → M in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs373540612Ensembl.1
Natural variantiVAR_012509230C → S in STGD1. 1 PublicationCorresponds to variant dbSNP:rs1057518767Ensembl.1
Natural variantiVAR_012510244L → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62646864EnsemblClinVar.1
Natural variantiVAR_012511247N → S in STGD1. 1 PublicationCorresponds to variant dbSNP:rs62645950EnsemblClinVar.1
Natural variantiVAR_008407249D → G in STGD1. Corresponds to variant dbSNP:rs62646865EnsemblClinVar.1
Natural variantiVAR_008408300T → N in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748544EnsemblClinVar.1
Natural variantiVAR_012512309P → R in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748545EnsemblClinVar.1
Natural variantiVAR_012513328E → V in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61751419EnsemblClinVar.1
Natural variantiVAR_012514333R → W in STGD1. Corresponds to variant dbSNP:rs61748546EnsemblClinVar.1
Natural variantiVAR_008409336S → C in STGD1. Corresponds to variant dbSNP:rs61748547EnsemblClinVar.1
Natural variantiVAR_012515339W → G in FFM. 1 PublicationCorresponds to variant dbSNP:rs61751420EnsemblClinVar.1
Natural variantiVAR_008410340Y → D in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748548EnsemblClinVar.1
Natural variantiVAR_012516380N → K in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748549EnsemblClinVar.1
Natural variantiVAR_008411407A → V in STGD1 and CORD3. Corresponds to variant dbSNP:rs61751264EnsemblClinVar.1
Natural variantiVAR_012517423H → R5 PublicationsCorresponds to variant dbSNP:rs3112831EnsemblClinVar.1
Natural variantiVAR_008412445S → R in STGD1. Corresponds to variant dbSNP:rs61748552EnsemblClinVar.1
Natural variantiVAR_008413471E → K in ARMD2 and STGD1; ATP-binding capacity and retinal stimulation as in wild-type. 1 PublicationCorresponds to variant dbSNP:rs1800548EnsemblClinVar.1
Natural variantiVAR_008414523D → E in STGD1. Corresponds to variant dbSNP:rs62646868EnsemblClinVar.1
Natural variantiVAR_012518525F → C in STGD1. 1 Publication1
Natural variantiVAR_012519537R → C in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748556EnsemblClinVar.1
Natural variantiVAR_008415541L → P in STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis. 5 PublicationsCorresponds to variant dbSNP:rs61751392EnsemblClinVar.1
Natural variantiVAR_012520549A → P in STGD1. 1 PublicationCorresponds to variant dbSNP:rs61748557EnsemblClinVar.1
Natural variantiVAR_012521550G → R in STGD1. 2 PublicationsCorresponds to variant dbSNP:rs61748558EnsemblClinVar.1
Natural variantiVAR_012522552V → I2 PublicationsCorresponds to variant dbSNP:rs145525174EnsemblClinVar.1
Natural variantiVAR_008416572R → P in STGD1. 1 Publication