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UniProtKB - O35600 (ABCA4_MOUSE)

Entry version 159 (25 May 2022)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
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Protein

Retinal-specific phospholipid-transporting ATPase ABCA4

Gene

Abca4

Organism
Mus musculus (Mouse)
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

Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid (PubMed:10852960, PubMed:10412977, PubMed:22735453).

Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (By similarity).

Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (By similarity).

By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATPase activity is decreased by cholesterol and ceramide. ATPase activity is stimulated by phosphatidylethanolamine. Phospholipids translocase activity is highly reduced by berylium fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid translocase activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1054ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 – 970ATPPROSITE-ProRule annotationBy similarity8
Nucleotide bindingi1971 – 1979ATPPROSITE-ProRule annotationBy similarity9
Nucleotide bindingi2072 – 2073ATPBy similarity2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-2453902, The canonical retinoid cycle in rods (twilight vision)
R-MMU-382556, ABC-family proteins mediated transport

<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%5Fand%5Ftaxonomy%5Fsection">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 phospholipid-transporting ATPase ABCA4By similarity (EC:7.6.2.1By similarity)
Alternative name(s):
ATP-binding cassette sub-family A member 4
RIM ABC transporter
Short name:
RIM protein1 Publication
Short name:
RmP1 Publication
Retinal-specific ATP-binding cassette transporter
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Abca4Imported
Synonyms:Abcr
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:109424, Abca4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000028125

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 21CytoplasmicCuratedAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 646ExtracellularBy similarityAdd BLAST604
Transmembranei647 – 667HelicalSequence analysisAdd BLAST21
Topological domaini668 – 699CytoplasmicCuratedAdd BLAST32
Transmembranei700 – 720HelicalSequence analysisAdd BLAST21
Topological domaini721 – 730ExtracellularCurated10
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Topological domaini752 – 759CytoplasmicCurated8
Transmembranei760 – 780HelicalSequence analysisAdd BLAST21
Topological domaini781 – 835ExtracellularCuratedAdd BLAST55
Transmembranei836 – 856HelicalSequence analysisAdd BLAST21
Topological domaini857 – 1375CytoplasmicCuratedAdd BLAST519
Transmembranei1376 – 1396HelicalSequence analysisAdd BLAST21
Topological domaini1397 – 1726ExtracellularBy similarityAdd BLAST330
Transmembranei1727 – 1747HelicalSequence analysisAdd BLAST21
Topological domaini1748 – 1758CytoplasmicCuratedAdd BLAST11
Transmembranei1759 – 1779HelicalSequence analysisAdd BLAST21
Topological domaini1780 – 1791ExtracellularCuratedAdd BLAST12
Transmembranei1792 – 1812HelicalSequence analysisAdd BLAST21
Topological domaini1813 – 1830CytoplasmicCuratedAdd BLAST18
Transmembranei1831 – 1851HelicalSequence analysisAdd BLAST21
Topological domaini1852 – 1872ExtracellularCuratedAdd BLAST21
Transmembranei1873 – 1893HelicalSequence analysisAdd BLAST21
Topological domaini1894 – 2310CytoplasmicCuratedAdd BLAST417

Keywords - Cellular componenti

Cell projection, Endoplasmic reticulum, 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Delayed dark adaptation but normal final rod threshold.1 Publication

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000933021 – 2310Retinal-specific phospholipid-transporting ATPase ABCA4Add BLAST2310

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 bondi54 ↔ 81By similarity
Disulfide bondi75 ↔ 324By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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...) asparagineSequence analysis1
Disulfide bondi370 ↔ 519By similarity
Glycosylationi415N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi504N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi641 ↔ 1489InterchainBy similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei901PhosphothreonineBy similarity1
Modified residuei1185PhosphoserineBy similarity1
Disulfide bondi1443 ↔ 1454By similarity
Glycosylationi1468N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1487 ↔ 1501By similarity
Glycosylationi1528N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1587N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1661N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.By similarity
Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal fragment and a 115-kDa C-terminal fragment that are linked through disulfide bonds.By similarity
Phosphorylation is independent of light exposure and modulates ATPase activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1309Cleavage; by trypsinBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		O35600

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

More...PaxDbi		O35600

PRoteomics IDEntifications database

More...PRIDEi		O35600

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		285899

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2683, 3 N-Linked glycans (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O35600, 8 sites, 3 N-linked glycans (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O35600

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

More...PhosphoSitePlusi		O35600

<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 (PubMed:9202155). Seems to be exclusively found in the rims of rod photoreceptor cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000028125, Expressed in retina and 128 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O35600, MM

<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		197901, 2 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000013995

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O35600, protein

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		O35600

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

More...SMRi		O35600

Database of comparative protein structure models

More...ModBasei		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%5Fand%5Fdomains%5Fsection">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
Domaini1937 – 2169ABC transporter 2PROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni891 – 910DisorderedSequence analysisAdd BLAST20
Regioni1311 – 1344DisorderedSequence analysisAdd BLAST34
Regioni2243 – 2248Essential for ATP binding and ATPase activityBy similarity6
Regioni2266 – 2310DisorderedSequence analysisAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2282 – 2310Polar residuesSequence analysisAdd BLAST29

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The second extracellular domain (ECD2, aa 1395-1680) undergoes conformational change in response to its specific interaction with its substrate all-trans-retinal. Nucleotide binding domain 1 (NBD1, aa 854-1375) binds preferentially and with high affinity with the 11-cis retinal.By similarity

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155624

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000604_19_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O35600

Identification of Orthologs from Complete Genome Data

More...OMAi		DPVYSYD

Database of Orthologous Groups

More...OrthoDBi		131191at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O35600

TreeFam database of animal gene trees

More...TreeFami		TF105191

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593, AAA+_ATPase
IPR003439, ABC_transporter-like_ATP-bd
IPR017871, ABC_transporter-like_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

O35600-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGFLRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS 
        60         70         80         90        100
QHECHFPNKA MPSAGLLPWL QGIFCNMNNP CFQNPTPGES PGTVSNYNNS 
       110        120        130        140        150
ILARVYRDFQ ELFMDTPEVQ HLGQVWAELR TLSQFMDTLR THPERFAGRG 
       160        170        180        190        200
LQIRDILKDE EALTLFLMRN IGLSDSVAHL LVNSQVRVEQ FAYGVPDLEL 
       210        220        230        240        250
TDIACSEALL QRFIIFSQRR GAQTVRDALC PLSQVTLQWI EDTLYADVDF 
       260        270        280        290        300
FKLFHVLPTL LDSSSQGINL RFWGGILSDL SPRMQKFIHR PSVQDLLWVS 
       310        320        330        340        350
RPLLQNGGPE TFTQLMSILS DLLCGYPEGG GSRVFSFNWY EDNNYKAFLG 
       360        370        380        390        400
IDSTRKDPAY SYDKRTTSFC NSLIQSLESN PLTKIAWRAA KPLLMGKILF 
       410        420        430        440        450
TPDSPAARRI MKNANSTFEE LDRVRKLVKA WEEVGPQIWY FFEKSTQMTV 
       460        470        480        490        500
IRDTLQHPTV KDFINRQLGE EGITTEAVLN FFSNGPQEKQ ADDMTSFDWR 
       510        520        530        540        550
DIFNITDRFL RLANQYLECL VLDKFESYDD EVQLTQRALS LLEENRFWAG 
       560        570        580        590        600
VVFPGMYPWA SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED 
       610        620        630        640        650
FRYIWGGFAY LQDMVEQGIV KSQMQAEPPI GVYLQQMPYP CFVDDSFMII 
       660        670        680        690        700
LNRCFPIFMV LAWIYSVSMT VKGIVLEKEL RLKETLKNQG VSNAVIWCTW 
       710        720        730        740        750
FLDSFSIMAL SIFLLTLFIM HGRILHYSDP FILFLFLLAF ATATIMQSFL 
       760        770        780        790        800
LSTLFSKASL AAACSGVIYF TLYLPHVLCF AWQDRMTADL KTTVSLLSSV 
       810        820        830        840        850
AFGFGTEYLV RFEEQGLGLQ WSNIGKSPLE GDEFSFLLSM KMMLLDAALY 
       860        870        880        890        900
GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL 
       910        920        930        940        950
TEEMEDPEHP EGMNDSFFER ELPGLVPGVC VKNLVKVFEP SGRPAVDRLN 
       960        970        980        990       1000
ITFYENQITA FLGHNGAGKT TTLSILTGLL PPTSGTVLIG GKDIETNLDV 
      1010       1020       1030       1040       1050
VRQSLGMCPQ HNILFHHLTV AEHILFYAQL KGRSWEEAQL EMEAMLEDTG 
      1060       1070       1080       1090       1100
LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDS KVVVLDEPTS GVDPYSRRSI 
      1110       1120       1130       1140       1150
WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIISQGRLYC SGTPLFLKNC 
      1160       1170       1180       1190       1200
FGTGFYLTLV RKMKNIQSQR GGCEGVCSCT SKGFSTRCPT RVDEITEEQV 
      1210       1220       1230       1240       1250
LDGDVQELMD LVYHHVPEAK LVECIGQELI FLLPNKNFKQ RAYASLFREL 
      1260       1270       1280       1290       1300
EETLADLGLS SFGISDTPLE EIFLKVTEDA GAGSMFVGGA QQKREQAGLR 
      1310       1320       1330       1340       1350
HPCSAPTEKL RQYAQAPHTC SPGQVDPPKG QPSPEPEDPG VPFNTGARLI 
      1360       1370       1380       1390       1400
LQHVQALLVK RFHHTIRSRK DFVAQIVLPA TFVFLALMLS IIVPPFGEFP 
      1410       1420       1430       1440       1450
ALTLHPWMYG HQYTFFSMDE PNNEHLEVLA DVLLNRPGFG NRCLKEEWLP 
      1460       1470       1480       1490       1500
EYPCINATSW KTPSVSPNIT HLFQKQKWTA AHPSPSCKCS TREKLTMLPE 
      1510       1520       1530       1540       1550
CPEGAGGLPP PQRTQRSTEV LQDLTNRNIS DYLVKTYPAL IRSSLKSKFW 
      1560       1570       1580       1590       1600
VNEQRYGGIS IGGKLPAIPI SGEALVGFLS GLGQMMNVSG GPVTREASKE 
      1610       1620       1630       1640       1650
MLDFLKHLET TDNIKVWFNN KGWHALVSFL NVAHNAILRA SLPRDRDPEE 
      1660       1670       1680       1690       1700
YGITVISQPL NLTKEQLSDI TVLTTSVDAV VAICVIFAMS FVPASFVLYL 
      1710       1720       1730       1740       1750
IQERVTKAKH LQFISGVSPT TYWLTNFLWD IMNYAVSAGL VVGIFIGFQK 
      1760       1770       1780       1790       1800
KAYTSPDNLP ALVSLLMLYG WAVIPMMYPA SFLFEVPSTA YVALSCANLF 
      1810       1820       1830       1840       1850
IGINSSAITF VLELFENNRT LLRFNAMLRK LLIVFPHFCL GRGLIDLALS 
      1860       1870       1880       1890       1900
QAVTDVYAQF GEEYSANPFQ WDLIGKNLVA MAIEGVVYFL LTLLIQHHFF 
      1910       1920       1930       1940       1950
LTRWIAEPAR EPVFDEDDDV AEERQRVMSG GNKTDILKLN ELTKVYSGSS 
      1960       1970       1980       1990       2000
SPAVDRLCVG VRPGECFGLL GVNGAGKTTT FKMLTGDTTV TSGDATVAGK 
      2010       2020       2030       2040       2050
SILTSISDVH QNMGYCPQFD AIDDLLTGRE HLYLYARLRG VPSKEIEKVA 
      2060       2070       2080       2090       2100
NWGIQSLGLS LYADRLAGTY SGGNKRKLST AIALTGCPPL LLLDEPTTGM 
      2110       2120       2130       2140       2150
DPQARRMLWN TIVSIIREGR AVVLTSHSME ECEALCTRLA IMVKGTFQCL 
      2160       2170       2180       2190       2200
GTIQHLKYKF GDGYIVTMKI KSPKDDLLPD LNPVEQFFQG NFPGSVQRER 
      2210       2220       2230       2240       2250
HHSMLQFQVP SSSLARIFQL LISHKDSLLI EEYSVTQTTL DQVFVNFAKQ 
      2260       2270       2280       2290       2300
QTETYDLPLH PRAAGASWQA KLEEKSGRLQ TQEPLPAGSE QLANGSNPTA 
      2310
AEDKHTRSPQ
Length:2,310
Mass (Da):260,209
Last modified:January 1, 1998 - v1
<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:i8370C6C8A62EF294
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
A0A0G2JGG8A0A0G2JGG8_MOUSE
Retinal-specific phospholipid-trans...
Abca4
1,102Annotation score:

Annotation score:2 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF000149 mRNA Translation: AAC23916.1
BC057853 mRNA Translation: AAH57853.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS38617.1

NCBI Reference Sequences

More...RefSeqi		NP_031404.1, NM_007378.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000013995; ENSMUSP00000013995; ENSMUSG00000028125

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11304

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11304

UCSC genome browser

More...UCSCi		uc008rel.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000149 mRNA Translation: AAC23916.1
BC057853 mRNA Translation: AAH57853.1
CCDSiCCDS38617.1
RefSeqiNP_031404.1, NM_007378.1

3D structure databases

AlphaFoldDBiO35600
SMRiO35600
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi197901, 2 interactors
STRINGi10090.ENSMUSP00000013995

PTM databases

GlyConnecti2683, 3 N-Linked glycans (1 site)
GlyGeniO35600, 8 sites, 3 N-linked glycans (1 site)
iPTMnetiO35600
PhosphoSitePlusiO35600

Proteomic databases

MaxQBiO35600
PaxDbiO35600
PRIDEiO35600
ProteomicsDBi285899

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		33661, 193 antibodies from 32 providers

The DNASU plasmid repository

More...DNASUi		11304

Genome annotation databases

EnsembliENSMUST00000013995; ENSMUSP00000013995; ENSMUSG00000028125
GeneIDi11304
KEGGimmu:11304
UCSCiuc008rel.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		24
MGIiMGI:109424, Abca4
VEuPathDBiHostDB:ENSMUSG00000028125

Phylogenomic databases

eggNOGiKOG0059, Eukaryota
GeneTreeiENSGT00940000155624
HOGENOMiCLU_000604_19_0_1
InParanoidiO35600
OMAiDPVYSYD
OrthoDBi131191at2759
PhylomeDBiO35600
TreeFamiTF105191

Enzyme and pathway databases

ReactomeiR-MMU-2453902, The canonical retinoid cycle in rods (twilight vision)
R-MMU-382556, ABC-family proteins mediated transport

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		11304, 2 hits in 74 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Abca4, mouse

Protein Ontology

More...PROi		PR:O35600
RNActiO35600, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000028125, Expressed in retina and 128 other tissues
GenevisibleiO35600, MM

Family and domain databases

Gene3Di3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR003439, ABC_transporter-like_ATP-bd
IPR017871, ABC_transporter-like_CS
IPR026082, ABCA
IPR005951, ABCA4/ABCR
IPR027417, P-loop_NTPase
PANTHERiPTHR19229, PTHR19229, 1 hit
PfamiView protein in Pfam
PF00005, ABC_tran, 2 hits
SMARTiView protein in SMART
SM00382, AAA, 2 hits
SUPFAMiSSF52540, SSF52540, 2 hits
TIGRFAMsiTIGR01257, rim_protein, 1 hit
PROSITEiView protein in PROSITE
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiABCA4_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O35600
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 1, 1998
Last modified: May 25, 2022
This is version 159 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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