ABCA4_BOVIN
ID ABCA4_BOVIN Reviewed; 2281 AA.
AC F1MWM0; O02698;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Retinal-specific phospholipid-transporting ATPase ABCA4 {ECO:0000250|UniProtKB:P78363};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P78363};
DE AltName: Full=ATP-binding cassette sub-family A member 4;
DE AltName: Full=RIM ABC transporter;
DE Short=RIM protein {ECO:0000303|PubMed:9092582, ECO:0000303|PubMed:9202155};
DE Short=RmP {ECO:0000303|PubMed:9092582, ECO:0000303|PubMed:9202155};
DE AltName: Full=Retinal-specific ATP-binding cassette transporter;
GN Name=ABCA4 {ECO:0000250|UniProtKB:P78363};
GN Synonyms=ABCR {ECO:0000250|UniProtKB:P78363};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, TISSUE SPECIFICITY, SITE, AND PROTEOLYTIC CLEAVAGE.
RC TISSUE=Retinal rod cell;
RX PubMed=9092582; DOI=10.1074/jbc.272.15.10303;
RA Illing M., Molday L.L., Molday R.S.;
RT "The 220-kDa rim protein of retinal rod outer segments is a member of the
RT ABC transporter superfamily.";
RL J. Biol. Chem. 272:10303-10310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [3]
RP PROTEIN SEQUENCE OF 1-16, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9202155; DOI=10.1016/s0014-5793(97)00517-6;
RA Azarian S.M., Travis G.H.;
RT "The photoreceptor rim protein is an ABC transporter encoded by the gene
RT for recessive Stargardt's disease (ABCR).";
RL FEBS Lett. 409:247-252(1997).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9288089; DOI=10.1038/ng0997-15;
RA Sun H., Nathans J.;
RT "Stargardt's ABCR is localized to the disc membrane of retinal rod outer
RT segments.";
RL Nat. Genet. 17:15-16(1997).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10075733; DOI=10.1074/jbc.274.12.8269;
RA Sun H., Molday R.S., Nathans J.;
RT "Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the
RT photoreceptor-specific ATP-binding cassette transporter responsible for
RT Stargardt disease.";
RL J. Biol. Chem. 274:8269-8281(1999).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10767284; DOI=10.1074/jbc.m000555200;
RA Ahn J., Wong J.T., Molday R.S.;
RT "The effect of lipid environment and retinoids on the ATPase activity of
RT ABCR, the photoreceptor ABC transporter responsible for Stargardt macular
RT dystrophy.";
RL J. Biol. Chem. 275:20399-20405(2000).
RN [7]
RP PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=11320094; DOI=10.1074/jbc.m101902200;
RA Bungert S., Molday L.L., Molday R.S.;
RT "Membrane topology of the ATP binding cassette transporter ABCR and its
RT relationship to ABC1 and related ABCA transporters: identification of N-
RT linked glycosylation sites.";
RL J. Biol. Chem. 276:23539-23546(2001).
RN [8]
RP FUNCTION.
RX PubMed=15471866; DOI=10.1074/jbc.m405216200;
RA Beharry S., Zhong M., Molday R.S.;
RT "N-retinylidene-phosphatidylethanolamine is the preferred retinoid
RT substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR).";
RL J. Biol. Chem. 279:53972-53979(2004).
RN [9]
RP FUNCTION.
RX PubMed=20552428; DOI=10.1007/978-1-60327-325-1_9;
RA Zhong M., Molday R.S.;
RT "Binding of retinoids to ABCA4, the photoreceptor ABC transporter
RT associated with Stargardt macular degeneration.";
RL Methods Mol. Biol. 652:163-176(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-415; ASN-504;
RP ASN-1455; ASN-1527; ASN-1586 AND ASN-1660, PHOSPHORYLATION AT THR-901;
RP SER-1185; THR-1313; SER-1317 AND SER-1319, MUTAGENESIS OF THR-901;
RP SER-1185; THR-1313 AND SER-1317, AND SUBCELLULAR LOCATION.
RX PubMed=21721517; DOI=10.1021/bi200774w;
RA Tsybovsky Y., Wang B., Quazi F., Molday R.S., Palczewski K.;
RT "Posttranslational modifications of the photoreceptor-specific ABC
RT transporter ABCA4.";
RL Biochemistry 50:6855-6866(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=22735453; DOI=10.1038/ncomms1927;
RA Quazi F., Lenevich S., Molday R.S.;
RT "ABCA4 is an N-retinylidene-phosphatidylethanolamine and
RT phosphatidylethanolamine importer.";
RL Nat. Commun. 3:925-925(2012).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24707049; DOI=10.1073/pnas.1400780111;
RA Quazi F., Molday R.S.;
RT "ATP-binding cassette transporter ABCA4 and chemical isomerization protect
RT photoreceptor cells from the toxic accumulation of excess 11-cis-retinal.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5024-5029(2014).
CC -!- FUNCTION: Flippase that catalyzes in an ATP-dependent manner the
CC transport of retinal-phosphatidylethanolamine conjugates like the 11-
CC cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine
CC from the lumen to the cytoplasmic leaflet of photoreceptor outer
CC segment disk membranes, where N-cis-retinylidene-
CC phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-
CC trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-
CC retinol (all-trans-rol) and therefore prevents the accumulation of
CC excess of 11-cis-retinal and its schiff-base conjugate and the
CC formation of toxic bisretinoid (PubMed:22735453, PubMed:20552428,
CC PubMed:10075733, PubMed:10767284, PubMed:24707049). Displays both
CC ATPase and GTPase activity that is strongly influenced by the lipid
CC environment and the presence of retinoid compounds (PubMed:10767284).
CC Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine
CC with high affinity in the absence of ATP and ATP binding and hydrolysis
CC induce a protein conformational change that causes the dissociation of
CC N-retinylidene-phosphatidylethanolamine (PubMed:15471866,
CC PubMed:20552428, PubMed:22735453). {ECO:0000269|PubMed:10075733,
CC ECO:0000269|PubMed:10767284, ECO:0000269|PubMed:15471866,
CC ECO:0000269|PubMed:20552428, ECO:0000269|PubMed:22735453,
CC ECO:0000269|PubMed:24707049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-all-trans-
CC retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-
CC retinylidenephosphatidylethanolamine(in) + phosphate;
CC Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453,
CC ECO:0000269|PubMed:24707049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189;
CC Evidence={ECO:0000305|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22735453};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out)
CC = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) +
CC phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167887, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24707049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193;
CC Evidence={ECO:0000305|PubMed:24707049};
CC -!- ACTIVITY REGULATION: All-trans-retinal transport activity is reduced by
CC EDTA chelation of Mg2+ (PubMed:22735453). All-trans-retinal transport
CC activity is inhibited by N-ethylmaleimide (NEM) (PubMed:22735453).
CC Phosphatidylethanolamine transport is strongly inhibited by beryllium
CC fluoride and NEM (PubMed:22735453). {ECO:0000269|PubMed:22735453}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=278 uM for ATP (with a purified ABCA4)
CC {ECO:0000269|PubMed:10075733};
CC KM=33 uM for ATP (with ABCA4 reconstituted into brain lipid membrane)
CC {ECO:0000269|PubMed:10075733};
CC KM=725 uM for ATP (reconstituted into brain lipid membrane, plus 80
CC uM all-trans-retinal) {ECO:0000269|PubMed:10075733};
CC KM=18 uM for ATP (with amiodarone) {ECO:0000269|PubMed:10075733};
CC KM=400 uM for ATP (with all-trans-retinal)
CC {ECO:0000269|PubMed:10075733};
CC KM=666 uM for ATP (with all-trans-retinal plus amiodarone)
CC {ECO:0000269|PubMed:10075733};
CC KM=75 uM for ATP (with CHAPS-solubilized ABCA4)
CC {ECO:0000269|PubMed:10767284};
CC KM=32 uM for ATP (with ABCA4 reconstituted into soybean phospholipid)
CC {ECO:0000269|PubMed:10767284};
CC KM=20 uM for ATP (with ABCA4 reconstituted into brain polar lipid)
CC {ECO:0000269|PubMed:10767284};
CC KM=25 uM for ATP (with ABCA4 reconstituted into ROS phospholipid)
CC {ECO:0000269|PubMed:10767284};
CC KM=112 uM for ATP (with CHAPS-solubilized ABCA4 and 60 uM all-trans-
CC retinal) {ECO:0000269|PubMed:10767284};
CC KM=56 uM for ATP (with ABCA4 reconstituted into soybean phospholipid
CC and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284};
CC KM=106 uM for ATP (with ABCA4 reconstituted into brain polar lipid
CC and 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284};
CC KM=75 uM for ATP (with ABCA4 reconstituted into ROS phospholipid and
CC 60 uM all-trans-retinal) {ECO:0000269|PubMed:10767284};
CC KM=0.02 mM for ATP (in the presence of 40 uM retinal)
CC {ECO:0000269|PubMed:24707049};
CC Vmax=27 nmol/min/mg enzyme (for ATP hydrolysis and with a purified
CC ABCA4) {ECO:0000269|PubMed:10075733};
CC Vmax=1.3 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into brain lipid membrane)
CC {ECO:0000269|PubMed:10075733};
CC Vmax=29 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into brain lipid membrane, plus 80 uM all-trans-
CC retinal) {ECO:0000269|PubMed:10075733};
CC Vmax=2 nmol/min/mg enzyme (for ATP hydrolysis and with amiodarone as
CC substrate) {ECO:0000269|PubMed:10075733};
CC Vmax=20 nmol/min/mg enzyme (for ATP hydrolysis and with all-trans-
CC retinal as substrate) {ECO:0000269|PubMed:10075733};
CC Vmax=50 nmol/min/mg enzyme (for ATP hydrolysis and with all-trans-
CC retinal and amiodarone as substrates) {ECO:0000269|PubMed:10075733};
CC Vmax=190 nmol/min/mg enzyme (for ATP hydrolysis and with CHAPS-
CC solubilized ABCA4) {ECO:0000269|PubMed:10767284};
CC Vmax=50 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into soybean phospholipid)
CC {ECO:0000269|PubMed:10767284};
CC Vmax=29 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into brain polar lipid) {ECO:0000269|PubMed:10767284};
CC Vmax=202 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into ROS phospholipid) {ECO:0000269|PubMed:10767284};
CC Vmax=402 nmol/min/mg enzyme (for ATP hydrolysis and with CHAPS-
CC solubilized ABCA4 and 60 uM all-trans-retinal)
CC {ECO:0000269|PubMed:10767284};
CC Vmax=110 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into soybean phospholipid and 60 uM all-trans-retinal)
CC {ECO:0000269|PubMed:10767284};
CC Vmax=171 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into brain polar lipid and 60 uM all-trans-retinal)
CC {ECO:0000269|PubMed:10767284};
CC Vmax=673 nmol/min/mg enzyme (for ATP hydrolysis and with ABCA4
CC reconstituted into ROS phospholipid and 60 uM all-trans-retinal)
CC {ECO:0000269|PubMed:10767284};
CC Vmax=35.5 pmol/min/ug enzyme toward all-trans-retinal (in liposome)
CC {ECO:0000269|PubMed:22735453};
CC Vmax=4.9 nmol/min/mg enzyme towards all-trans-retinal (in rod outer
CC segments) {ECO:0000269|PubMed:22735453};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:22735453};
CC -!- INTERACTION:
CC F1MWM0; Q28181: CNGB1; NbExp=3; IntAct=EBI-7079806, EBI-6979031;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000269|PubMed:9092582, ECO:0000269|PubMed:9202155,
CC ECO:0000269|PubMed:9288089}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21721517}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P78363}. Note=Localized to the rim and incisures
CC of rod outer segments disks. {ECO:0000269|PubMed:9092582,
CC ECO:0000269|PubMed:9288089}.
CC -!- TISSUE SPECIFICITY: Expressed in retina namely in the periphery and
CC incisures of the rod outer segments (ROS). {ECO:0000269|PubMed:9092582,
CC ECO:0000269|PubMed:9202155}.
CC -!- DOMAIN: The second extracellular domain (ECD2, aa 1395-1680) undergoes
CC conformational change in response to its specific interaction with its
CC substrate all-trans-retinal. Nucleotide binding domain 1 (NBD1, aa 854-
CC 1375) binds preferentially and with high affinity with the 11-cis
CC retinal. {ECO:0000250|UniProtKB:P78363}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11320094,
CC ECO:0000269|PubMed:9092582, ECO:0000269|PubMed:9202155}.
CC -!- PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal
CC fragment and a 115-kDa C-terminal fragment that are linked through
CC disulfide bonds. {ECO:0000269|PubMed:11320094,
CC ECO:0000269|PubMed:9092582}.
CC -!- PTM: Phosphorylation is independent of light exposure and modulates
CC ATPase activity. {ECO:0000269|PubMed:21721517}.
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DR EMBL; U90126; AAC48716.1; -; mRNA.
DR EMBL; DAAA02007872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_776646.1; NM_174221.2.
DR SMR; F1MWM0; -.
DR IntAct; F1MWM0; 1.
DR MINT; F1MWM0; -.
DR STRING; 9913.ENSBTAP00000023982; -.
DR GlyConnect; 812; 12 N-Linked glycans (6 sites).
DR PaxDb; F1MWM0; -.
DR Ensembl; ENSBTAT00000023982; ENSBTAP00000023982; ENSBTAG00000018010.
DR GeneID; 281584; -.
DR KEGG; bta:281584; -.
DR CTD; 24; -.
DR VEuPathDB; HostDB:ENSBTAG00000018010; -.
DR VGNC; VGNC:25458; ABCA4.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000155624; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR InParanoid; F1MWM0; -.
DR OMA; DPVYSYD; -.
DR OrthoDB; 131191at2759; -.
DR TreeFam; TF105191; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018010; Expressed in retina and 16 other tissues.
DR ExpressionAtlas; F1MWM0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0120202; C:rod photoreceptor disc membrane; IDA:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005503; F:all-trans retinal binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0140347; F:N-retinylidene-phosphatidylethanolamine flippase activity; IDA:UniProtKB.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:Ensembl.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0005501; F:retinoid binding; IDA:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
DR GO; GO:0045332; P:phospholipid translocation; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR005951; ABCA4/ABCR.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01257; rim_protein; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..2281
FT /note="Retinal-specific phospholipid-transporting ATPase
FT ABCA4"
FT /id="PRO_0000453425"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..646
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..730
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..835
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..1374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1375..1395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1396..1679
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT TRANSMEM 1680..1700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1701..1725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1726..1746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1747..1757
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1758..1778
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1779..1790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1791..1811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1812..1829
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1830..1850
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1851..1879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1880..1900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1901..2281
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 929..1160
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1936..2168
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1295..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2242..2247
FT /note="Essential for ATP binding and ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT REGION 2262..2281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 963..970
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1054
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT BINDING 1970..1978
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 2071..2072
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT SITE 1309
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000269|PubMed:9092582"
FT MOD_RES 901
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT MOD_RES 1313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 415
FT /note="N-linked (Hex...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:21721517"
FT CARBOHYD 504
FT /note="N-linked (Hex...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:21721517"
FT CARBOHYD 1455
FT /note="N-linked (Hex...) asparagine"
FT /evidence="ECO:0000269|PubMed:21721517"
FT CARBOHYD 1527
FT /note="N-linked (Hex...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:21721517"
FT CARBOHYD 1586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1660
FT /note="N-linked (Hex...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:21721517"
FT CARBOHYD 1817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 54..81
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 75..324
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 370..519
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 641..1488
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 1442..1453
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 1486..1500
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT MUTAGEN 901
FT /note="T->A: Decreases expression level. Affects
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:21721517"
FT MUTAGEN 1185
FT /note="S->A: Does not affect subcellular location. Does not
FT affect expression level. Does not affect ATPase activity.
FT Reduces the stimulating effect of all-trans-retinal on ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:21721517"
FT MUTAGEN 1313
FT /note="T->A: Does not affect subcellular location. Does not
FT affect expression level. Does not affect ATPase activity.
FT Reduces the stimulating effect of all-trans-retinal on ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:21721517"
FT MUTAGEN 1317
FT /note="S->A: Does not affect subcellular location. Does not
FT affect expression level. Affects both the basal and
FT stimulated ATPase activity."
FT /evidence="ECO:0000269|PubMed:21721517"
FT CONFLICT 1037
FT /note="K -> E (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="Q -> R (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="R -> G (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="L -> P (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 1858..1862
FT /note="RFGEE -> QFGEA (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118
FT /note="G -> E (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 2203
FT /note="M -> T (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
FT CONFLICT 2262
FT /note="A -> T (in Ref. 1; AAC48716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2281 AA; 257376 MW; 26C8C84FB3CB243F CRC64;
MGFARQIKLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNVNPLYS KHECHFPNKA
MPSAGMLPWL QGIFCNVNNP CFQSPTAGES PGIVSNYNNS ILARVYRDFQ ELLMDAPESQ
HLGQVWRELR TLSQLMNTLR MHPERIAGRG IRIREVLKDD EMLTLFLVKN IGLSDSVVYL
LVNSQVRPEQ FARGVPDLML KDIACSEALL ERFLIFPQRR AAQTVRGSLC SLSQGTLQWM
EDTLYANVDF FKLFHVFPRL LDSRSQGMNL RSWGRILSDM SPRIQEFIHR PSVQDLLWVT
RPLVQTGGPE TFTQLMGILS DLLCGYPEGG GSRVFSFNWY EDNNYKAFLG IDSTRKDPIY
SYDERTTTFC NALIQSLESN PLTKIAWRAA KPLLMGKILF TPDSPATRRI LKNANSTFEE
LERVRKLVKV WEEVGPQIWY FFDKSTQMSM IRDTLENPTV KAFWNRQLGE EGITAEAVLN
FLYNGPREGQ ADDVDNFNWR DIFNITDRAL RLANQYLECL ILDKFESYDD EFQLTQRALS
LLEENRFWAG VVFPDMHPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED
FRYIWGGFAY LQDMVEHGIT RSQAQEEVPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV
LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNRVIWCTW FLDSFSIMSM SICLLTIFIM
HGRILHYSNP FILFLFLLAF SIATIMQCFL LSTFFSRASL AAACSGVIYF TLYLPHILCF
AWQDRITADM KMAVSLLSPV AFGFGTEYLA RFEEQGVGLQ WSNIGNSPME GDEFSFLMSM
KMMLLDAALY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPI
TEEMEDPEYP EGINDCFFER ELPGLVPGVC VKNLVKIFEP YGRPAVDRLN ITFYESQITA
FLGHNGAGKT TTLSIMTGLL PPTSGTVLVG GKDIETNLDA IRQSLGMCPQ HNILFHHLTV
AEHILFYAQL KGRSWDKAQL EMEAMLEDTG LHHKRNEEAQ DLSGGVQRKL SVAIAFVGDA
KVVVLDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADILGDRI AIISQGRLYC
SGTPLFLKNC FGTGFYLTLV RRMKTIQSQG RGREATCSCA SKGFSVRCPA CAEAITPEQV
LDGDVNELTD MVHHHVPEAK LVECIGQELI FLLPNKNFKQ RAYASLFREL EETLADLGLS
SFGISDTPLE EIFLKVTEDL DSGHLFAGGT QQKRENINLR HPCSGPSEKA GQTPQGSSSH
PREPAAHPEG QPPPEREGHS RLNSGARLIV QHVQALLVKR FQHTIRSHKD FLAQIVLPAT
FVFLALMLSL IIPPFGEYPA LTLHPWMYGQ QYTFFSMDQL DSEWLSALAD VLVNKPGFGN
RCLKEEWLPE FPCGNSSPWK TPSVSPDVTH LLQQQKWTAD QPSPSCRCST REKLTMLPEC
PEGAGGLPPP QRIQRSTEIL QDLTDRNVSD FLVKTYPALI RSSLKSKFWV NEQRYGGISV
GGKLPAPPFT GEALVGFLSD LGQLMNVSGG PMTREAAKEM PAFLKQLETE DNIKVWFNNK
GWHALVSFLN VAHNAILRAS LHKDKNPEEY GITVISQPLN LTKEQLSEIT VLTTSVDAVV
AICVIFAMSF VPASFVLYLI QERVNKAKHL QFVSGVSPTT YWLTNFLWDI MNYTVSAALV
VGIFIGFQKK AYTSSENLPA LVALLMLYGW AVIPMMYPAS FLFDIPSTAY VALSCANLFI
GINSSAITFV LELFENNRTL LRINAMLRKL LIIFPHFCLG RGLIDLALSQ AVTDVYARFG
EEHSSNPFQW DLIGKNLAAM AVEGVVYFLL TLLIQYQFFF SRWTTEPAKE PITDEDDDVA
EERQRIISGG NKTDILRLNE LTKVYSGTSS PAVDRLCVGV RPGECFGLLG VNGAGKTTTF
KMLTGDTAVT SGDATVAGKS ILTNISDVHQ SMGYCPQFDA IDDLLTGREH LYLYARLRGV
PAEEIERVTN WSIQSLGLSL YADRLAGTYS GGNKRKLSTA IALIGCPPLV LLDEPTTGMD
PQARRMLWNT IMGIIREGRA VVLTSHSMEE CEALCTRLAI MVKGAFQCLG TIQHLKSKFG
DGYIVTMKIR SPKDDLLPDL GPVEQFFQGN FPGSVQRERH YNMLQFQVSS SSLARIFRLL
VSHKDSLLIE EYSVTQTTLD QVFVNFAKQQ NETYDLPLHP RAAGASRQAK EVDKGNSAPQ
G
