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Entry version 159 (25 May 2022)
Sequence version 1 (01 Jan 1998)
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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

GO - Biological processi

<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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

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

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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
UniProt is an ELIXIR core data resource
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