UniProtKB - O35600 (ABCA4_MOUSE)
Retinal-specific phospholipid-transporting ATPase ABCA4
Abca4
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 PublicationsCatalytic activityi
- ATP + H2O + N-all-trans-retinylidenephosphatidylethanolamine(out) = ADP + H+ + N-all-trans-retinylidenephosphatidylethanolamine(in) + phosphate3 PublicationsThis reaction proceeds in the forward1 Publication direction.
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H+ + phosphate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) = ADP + H+ + N-11-cis-retinylidenephosphatidylethanolamine(in) + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).1 Publication EC:7.6.2.1
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 1054 | ATPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 963 – 970 | ATPPROSITE-ProRule annotationBy similarity | 8 | |
Nucleotide bindingi | 1971 – 1979 | ATPPROSITE-ProRule annotationBy similarity | 9 | |
Nucleotide bindingi | 2072 – 2073 | ATPBy similarity | 2 |
GO - Molecular functioni
- 11-cis retinal binding Source: UniProtKB
- ABC-type transporter activity Source: InterPro
- all-trans retinal binding Source: UniProtKB
- ATPase-coupled intramembrane lipid transporter activity Source: MGI
- ATPase-coupled transmembrane transporter activity Source: GO_Central
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: UniProtKB
- flippase activity Source: UniProtKB
- GTPase activity Source: UniProtKB
- lipid transporter activity Source: GO_Central
- N-retinylidene-phosphatidylethanolamine flippase activity Source: UniProtKB
- phosphatidylethanolamine flippase activity Source: MGI
- phospholipid transporter activity Source: GO_Central
- retinoid binding Source: UniProtKB
GO - Biological processi
- lipid transport Source: GO_Central
- phospholipid transfer to membrane Source: MGI
- phospholipid translocation Source: MGI
- photoreceptor cell maintenance Source: MGI
- response to stimulus Source: UniProtKB-KW
- retinal metabolic process Source: UniProtKB
- retinoid metabolic process Source: UniProtKB
- visual perception Source: MGI
Keywordsi
Molecular function | Translocase |
Biological process | Sensory transduction, Transport, Vision |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-MMU-2453902, The canonical retinoid cycle in rods (twilight vision) R-MMU-382556, ABC-family proteins mediated transport |
Names & Taxonomyi
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 |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:109424, Abca4 |
VEuPathDBi | HostDB:ENSMUSG00000028125 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Other locations
- Membrane ; Multi-pass membrane protein Sequence analysis
- photoreceptor outer segment 1 Publication
Note: Localized to the rim and incisures of rod outer segments disks.1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Plasma Membrane
- integral component of plasma membrane Source: MGI
Other locations
- cytoplasmic vesicle Source: UniProtKB
- intracellular membrane-bounded organelle Source: GO_Central
- photoreceptor outer segment Source: UniProtKB
- rod photoreceptor disc membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 21 | CytoplasmicCuratedAdd BLAST | 21 | |
Transmembranei | 22 – 42 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 43 – 646 | ExtracellularBy similarityAdd BLAST | 604 | |
Transmembranei | 647 – 667 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 668 – 699 | CytoplasmicCuratedAdd BLAST | 32 | |
Transmembranei | 700 – 720 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 721 – 730 | ExtracellularCurated | 10 | |
Transmembranei | 731 – 751 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 752 – 759 | CytoplasmicCurated | 8 | |
Transmembranei | 760 – 780 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 781 – 835 | ExtracellularCuratedAdd BLAST | 55 | |
Transmembranei | 836 – 856 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 857 – 1375 | CytoplasmicCuratedAdd BLAST | 519 | |
Transmembranei | 1376 – 1396 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1397 – 1726 | ExtracellularBy similarityAdd BLAST | 330 | |
Transmembranei | 1727 – 1747 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1748 – 1758 | CytoplasmicCuratedAdd BLAST | 11 | |
Transmembranei | 1759 – 1779 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1780 – 1791 | ExtracellularCuratedAdd BLAST | 12 | |
Transmembranei | 1792 – 1812 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1813 – 1830 | CytoplasmicCuratedAdd BLAST | 18 | |
Transmembranei | 1831 – 1851 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1852 – 1872 | ExtracellularCuratedAdd BLAST | 21 | |
Transmembranei | 1873 – 1893 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1894 – 2310 | CytoplasmicCuratedAdd BLAST | 417 |
Keywords - Cellular componenti
Cell projection, Endoplasmic reticulum, MembranePathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000093302 | 1 – 2310 | Retinal-specific phospholipid-transporting ATPase ABCA4Add BLAST | 2310 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 54 ↔ 81 | By similarity | ||
Disulfide bondi | 75 ↔ 324 | By similarity | ||
Glycosylationi | 98 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 370 ↔ 519 | By similarity | ||
Glycosylationi | 415 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 504 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 641 ↔ 1489 | InterchainBy similarity | ||
Modified residuei | 901 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1185 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1443 ↔ 1454 | By similarity | ||
Glycosylationi | 1468 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1487 ↔ 1501 | By similarity | ||
Glycosylationi | 1528 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1587 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1661 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1309 | Cleavage; by trypsinBy similarity | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
MaxQBi | O35600 |
PaxDbi | O35600 |
PRIDEi | O35600 |
ProteomicsDBi | 285899 |
PTM databases
GlyConnecti | 2683, 3 N-Linked glycans (1 site) |
GlyGeni | O35600, 8 sites, 3 N-linked glycans (1 site) |
iPTMneti | O35600 |
PhosphoSitePlusi | O35600 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000028125, Expressed in retina and 128 other tissues |
Genevisiblei | O35600, MM |
Interactioni
Protein-protein interaction databases
BioGRIDi | 197901, 2 interactors |
STRINGi | 10090.ENSMUSP00000013995 |
Miscellaneous databases
RNActi | O35600, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 929 – 1160 | ABC transporter 1PROSITE-ProRule annotationAdd BLAST | 232 | |
Domaini | 1937 – 2169 | ABC transporter 2PROSITE-ProRule annotationAdd BLAST | 233 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 891 – 910 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 1311 – 1344 | DisorderedSequence analysisAdd BLAST | 34 | |
Regioni | 2243 – 2248 | Essential for ATP binding and ATPase activityBy similarity | 6 | |
Regioni | 2266 – 2310 | DisorderedSequence analysisAdd BLAST | 45 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2282 – 2310 | Polar residuesSequence analysisAdd BLAST | 29 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0059, Eukaryota |
GeneTreei | ENSGT00940000155624 |
HOGENOMi | CLU_000604_19_0_1 |
InParanoidi | O35600 |
OMAi | DPVYSYD |
OrthoDBi | 131191at2759 |
PhylomeDBi | O35600 |
TreeFami | TF105191 |
Family and domain databases
Gene3Di | 3.40.50.300, 2 hits |
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 |
PANTHERi | PTHR19229, PTHR19229, 1 hit |
Pfami | View protein in Pfam PF00005, ABC_tran, 2 hits |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits |
TIGRFAMsi | TIGR01257, rim_protein, 1 hit |
PROSITEi | View protein in PROSITE PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2JGG8 | A0A0G2JGG8_MOUSE | Retinal-specific phospholipid-trans... | Abca4 | 1,102 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF000149 mRNA Translation: AAC23916.1 BC057853 mRNA Translation: AAH57853.1 |
CCDSi | CCDS38617.1 |
RefSeqi | NP_031404.1, NM_007378.1 |
Genome annotation databases
Ensembli | ENSMUST00000013995; ENSMUSP00000013995; ENSMUSG00000028125 |
GeneIDi | 11304 |
KEGGi | mmu:11304 |
UCSCi | uc008rel.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF000149 mRNA Translation: AAC23916.1 BC057853 mRNA Translation: AAH57853.1 |
CCDSi | CCDS38617.1 |
RefSeqi | NP_031404.1, NM_007378.1 |
3D structure databases
AlphaFoldDBi | O35600 |
SMRi | O35600 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 197901, 2 interactors |
STRINGi | 10090.ENSMUSP00000013995 |
PTM databases
GlyConnecti | 2683, 3 N-Linked glycans (1 site) |
GlyGeni | O35600, 8 sites, 3 N-linked glycans (1 site) |
iPTMneti | O35600 |
PhosphoSitePlusi | O35600 |
Proteomic databases
MaxQBi | O35600 |
PaxDbi | O35600 |
PRIDEi | O35600 |
ProteomicsDBi | 285899 |
Protocols and materials databases
Antibodypediai | 33661, 193 antibodies from 32 providers |
DNASUi | 11304 |
Genome annotation databases
Ensembli | ENSMUST00000013995; ENSMUSP00000013995; ENSMUSG00000028125 |
GeneIDi | 11304 |
KEGGi | mmu:11304 |
UCSCi | uc008rel.1, mouse |
Organism-specific databases
CTDi | 24 |
MGIi | MGI:109424, Abca4 |
VEuPathDBi | HostDB:ENSMUSG00000028125 |
Phylogenomic databases
eggNOGi | KOG0059, Eukaryota |
GeneTreei | ENSGT00940000155624 |
HOGENOMi | CLU_000604_19_0_1 |
InParanoidi | O35600 |
OMAi | DPVYSYD |
OrthoDBi | 131191at2759 |
PhylomeDBi | O35600 |
TreeFami | TF105191 |
Enzyme and pathway databases
Reactomei | R-MMU-2453902, The canonical retinoid cycle in rods (twilight vision) R-MMU-382556, ABC-family proteins mediated transport |
Miscellaneous databases
BioGRID-ORCSi | 11304, 2 hits in 74 CRISPR screens |
ChiTaRSi | Abca4, mouse |
PROi | PR:O35600 |
RNActi | O35600, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000028125, Expressed in retina and 128 other tissues |
Genevisiblei | O35600, MM |
Family and domain databases
Gene3Di | 3.40.50.300, 2 hits |
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 |
PANTHERi | PTHR19229, PTHR19229, 1 hit |
Pfami | View protein in Pfam PF00005, ABC_tran, 2 hits |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits |
TIGRFAMsi | TIGR01257, rim_protein, 1 hit |
PROSITEi | View protein in PROSITE PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ABCA4_MOUSE | |
Accessioni | O35600Primary (citable) accession number: O35600 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families