MRP7_HUMAN
ID MRP7_HUMAN Reviewed; 1492 AA.
AC Q5T3U5; Q8NHX7; Q9H7N2; Q9NXY3; Q9UF48;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-binding cassette sub-family C member 10;
DE EC=7.6.2.2 {ECO:0000269|PubMed:15256465};
DE EC=7.6.2.3 {ECO:0000269|PubMed:23087055};
DE AltName: Full=Multidrug resistance-associated protein 7;
GN Name=ABCC10; Synonyms=MRP7, SIMRP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Small intestine;
RX PubMed=12566991; DOI=10.1159/000068078;
RA Kao H.-H., Chang M.-S., Cheng J.-F., Huang J.-D.;
RT "Genomic structure, gene expression, and promoter analysis of human
RT multidrug resistance-associated protein 7.";
RL J. Biomed. Sci. 10:98-110(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1492 (ISOFORMS 1/2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=12527806; DOI=10.1124/mol.63.2.351;
RA Chen Z.-S., Hopper-Borge E., Belinsky M.G., Shchaveleva I., Kotova E.,
RA Kruh G.D.;
RT "Characterization of the transport properties of human multidrug resistance
RT protein 7 (MRP7, ABCC10).";
RL Mol. Pharmacol. 63:351-358(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=15256465; DOI=10.1158/0008-5472.can-03-3111;
RA Hopper-Borge E., Chen Z.-S., Shchaveleva I., Belinsky M.G., Kruh G.D.;
RT "Analysis of the drug resistance profile of multidrug resistance protein 7
RT (ABCC10): resistance to docetaxel.";
RL Cancer Res. 64:4927-4930(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463 AND SER-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23087055; DOI=10.1158/0008-5472.can-12-1340;
RA Malofeeva E.V., Domanitskaya N., Gudima M., Hopper-Borge E.A.;
RT "Modulation of the ATPase and transport activities of broad-acting
RT multidrug resistance factor ABCC10 (MRP7).";
RL Cancer Res. 72:6457-6467(2012).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that actively extrudes physiological compounds, and xenobiotics
CC from cells. Lipophilic anion transporter that mediates ATP-dependent
CC transport of glucuronide conjugates such as estradiol-17-beta-o-
CC glucuronide and GSH conjugates such as leukotriene C4 (LTC4)
CC (PubMed:12527806, PubMed:15256465). Mediates multidrug resistance (MDR)
CC in cancer cells by preventing the intracellular accumulation of certain
CC antitumor drugs, such as, docetaxel and paclitaxel (PubMed:15256465,
CC PubMed:23087055). Does not transport glycocholic acid, taurocholic
CC acid, MTX, folic acid, cAMP, or cGMP (PubMed:12527806).
CC {ECO:0000269|PubMed:12527806, ECO:0000269|PubMed:15256465,
CC ECO:0000269|PubMed:23087055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:15256465,
CC ECO:0000269|PubMed:23087055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000269|PubMed:23087055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000305|PubMed:23087055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12527806, ECO:0000269|PubMed:23087055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000305|PubMed:23087055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23087055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.057 mM for leukotriene C4 {ECO:0000269|PubMed:23087055};
CC KM=3.3 mM for ATP {ECO:0000269|PubMed:23087055};
CC KM=57.8 uM for 17-beta-estradiol 17-(beta-D-glucuronide) (at 37
CC degrees Celsius) {ECO:0000269|PubMed:12527806};
CC Vmax=20 pmol/min/mg enzyme toward 17-beta-estradiol 17-(beta-D-
CC glucuronide) (at 37 degrees Celsius) {ECO:0000269|PubMed:12527806};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:23087055};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12566991,
CC ECO:0000269|PubMed:15256465}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:12566991,
CC ECO:0000269|PubMed:15256465}. Basolateral cell membrane
CC {ECO:0000269|PubMed:23087055}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mrp7;
CC IsoId=Q5T3U5-1; Sequence=Displayed;
CC Name=2; Synonyms=Mrp7A;
CC IsoId=Q5T3U5-2; Sequence=VSP_021078, VSP_021079, VSP_021080;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Specifically expressed in spleen.
CC {ECO:0000269|PubMed:12566991}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed.
CC {ECO:0000269|PubMed:12566991}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15736.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY032599; AAK39642.1; -; mRNA.
DR EMBL; AK000002; BAA92227.1; ALT_INIT; mRNA.
DR EMBL; AK024446; BAB15736.1; ALT_SEQ; mRNA.
DR EMBL; AL359813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133613; CAB63742.1; -; mRNA.
DR CCDS; CCDS4896.1; -. [Q5T3U5-2]
DR CCDS; CCDS56430.1; -. [Q5T3U5-1]
DR PIR; T43469; T43469.
DR RefSeq; NP_001185863.1; NM_001198934.1. [Q5T3U5-1]
DR RefSeq; NP_258261.2; NM_033450.2. [Q5T3U5-2]
DR AlphaFoldDB; Q5T3U5; -.
DR SMR; Q5T3U5; -.
DR BioGRID; 124617; 35.
DR IntAct; Q5T3U5; 9.
DR STRING; 9606.ENSP00000361608; -.
DR ChEMBL; CHEMBL2073687; -.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB00987; Cytarabine.
DR DrugBank; DB00694; Daunorubicin.
DR DrugBank; DB01248; Docetaxel.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB00773; Etoposide.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB01229; Paclitaxel.
DR DrugBank; DB00203; Sildenafil.
DR DrugBank; DB04348; Taurocholic acid.
DR DrugBank; DB00300; Tenofovir disoproxil.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB00541; Vincristine.
DR DrugCentral; Q5T3U5; -.
DR TCDB; 3.A.1.208.31; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q5T3U5; -.
DR PhosphoSitePlus; Q5T3U5; -.
DR BioMuta; ABCC10; -.
DR DMDM; 74756298; -.
DR EPD; Q5T3U5; -.
DR jPOST; Q5T3U5; -.
DR MassIVE; Q5T3U5; -.
DR MaxQB; Q5T3U5; -.
DR PaxDb; Q5T3U5; -.
DR PeptideAtlas; Q5T3U5; -.
DR PRIDE; Q5T3U5; -.
DR ProteomicsDB; 64416; -. [Q5T3U5-1]
DR ProteomicsDB; 64417; -. [Q5T3U5-2]
DR Antibodypedia; 30398; 275 antibodies from 30 providers.
DR DNASU; 89845; -.
DR Ensembl; ENST00000244533.7; ENSP00000244533.3; ENSG00000124574.15. [Q5T3U5-2]
DR Ensembl; ENST00000372530.9; ENSP00000361608.4; ENSG00000124574.15. [Q5T3U5-1]
DR GeneID; 89845; -.
DR KEGG; hsa:89845; -.
DR MANE-Select; ENST00000372530.9; ENSP00000361608.4; NM_001198934.2; NP_001185863.1.
DR UCSC; uc003ouy.2; human. [Q5T3U5-1]
DR CTD; 89845; -.
DR DisGeNET; 89845; -.
DR GeneCards; ABCC10; -.
DR HGNC; HGNC:52; ABCC10.
DR HPA; ENSG00000124574; Low tissue specificity.
DR MIM; 612509; gene.
DR neXtProt; NX_Q5T3U5; -.
DR OpenTargets; ENSG00000124574; -.
DR PharmGKB; PA24392; -.
DR VEuPathDB; HostDB:ENSG00000124574; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161082; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q5T3U5; -.
DR OMA; PPYAWPS; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q5T3U5; -.
DR TreeFam; TF105203; -.
DR BRENDA; 7.6.2.2; 2681.
DR PathwayCommons; Q5T3U5; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR SABIO-RK; Q5T3U5; -.
DR SignaLink; Q5T3U5; -.
DR BioGRID-ORCS; 89845; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; ABCC10; human.
DR GeneWiki; ABCC10; -.
DR GenomeRNAi; 89845; -.
DR Pharos; Q5T3U5; Tbio.
DR PRO; PR:Q5T3U5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T3U5; protein.
DR Bgee; ENSG00000124574; Expressed in right hemisphere of cerebellum and 190 other tissues.
DR ExpressionAtlas; Q5T3U5; baseline and differential.
DR Genevisible; Q5T3U5; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IDA:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006691; P:leukotriene metabolic process; IDA:UniProtKB.
DR GO; GO:0071716; P:leukotriene transport; IDA:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1492
FT /note="ATP-binding cassette sub-family C member 10"
FT /id="PRO_0000253576"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 933..953
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1182..1202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 285..563
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 598..824
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 885..1210
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1246..1479
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 825..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 633..640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1280..1287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12566991"
FT /id="VSP_021078"
FT VAR_SEQ 44..52
FT /note="VLSACYLGT -> MCLLVFPLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12566991"
FT /id="VSP_021079"
FT VAR_SEQ 588
FT /note="P -> PDCGRLGAQIKWLLCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12566991"
FT /id="VSP_021080"
FT VARIANT 948
FT /note="I -> T (in dbSNP:rs2125739)"
FT /id="VAR_028391"
FT CONFLICT 208
FT /note="D -> E (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="Missing (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="I -> T (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="L -> P (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="S -> P (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="I -> T (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="S -> F (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="L -> F (in Ref. 2; BAB15736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="L -> V (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1455
FT /note="G -> E (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1481
FT /note="S -> C (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1490
FT /note="G -> R (in Ref. 1; AAK39642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1492 AA; 161629 MW; 6FBC260DEFB3DF30 CRC64;
MERLLAQLCG SSAAWPLPLW EGDTTGHCFT QLVLSALPHA LLAVLSACYL GTPRSPDYIL
PCSPGWRLRL AASFLLSVFP LLDLLPVALP PGAGPGPIGL EVLAGCVAAV AWISHSLALW
VLAHSPHGHS RGPLALALVA LLPAPALVLT VLWHCQRGTL LPPLLPGPMA RLCLLILQLA
ALLAYALGWA APGGPREPWA QEPLLPEDQE PEVAEDGESW LSRFSYAWLA PLLARGACGE
LRQPQDICRL PHRLQPTYLA RVFQAHWQEG ARLWRALYGA FGRCYLALGL LKLVGTMLGF
SGPLLLSLLV GFLEEGQEPL SHGLLYALGL AGGAVLGAVL QNQYGYEVYK VTLQARGAVL
NILYCKALQL GPSRPPTGEA LNLLGTDSER LLNFAGSFHE AWGLPLQLAI TLYLLYQQVG
VAFVGGLILA LLLVPVNKVI ATRIMASNQE MLQHKDARVK LVTELLSGIR VIKFCGWEQA
LGARVEACRA RELGRLRVIK YLDAACVYLW AALPVVISIV IFITYVLMGH QLTATKVFTA
LALVRMLILP LNNFPWVING LLEAKVSLDR IQLFLDLPNH NPQAYYSPDP PAEPSTVLEL
HGALFSWDPV GTSLETFISH LEVKKGMLVG IVGKVGCGKS SLLAAIAGEL HRLRGHVAVR
GLSKGFGLAT QEPWIQFATI RDNILFGKTF DAQLYKEVLE ACALNDDLSI LPAGDQTEVG
EKGVTLSGGQ RARIALARAV YQEKELYLLD DPLAAVDADV ANHLLHRCIL GMLSYTTRLL
CTHRTEYLER ADAVLLMEAG RLIRAGPPSE ILPLVQAVPK AWAENGQESD SATAQSVQNP
EKTKEGLEEE QSTSGRLLQE ESKKEGAVAL HVYQAYWKAV GQGLALAILF SLLLMQATRN
AADWWLSHWI SQLKAENSSQ EAQPSTSPAS MGLFSPQLLL FSPGNLYIPV FPLPKAAPNG
SSDIRFYLTV YATIAGVNSL CTLLRAVLFA AGTLQAAATL HRRLLHRVLM APVTFFNATP
TGRILNRFSS DVACADDSLP FILNILLANA AGLLGLLAVL GSGLPWLLLL LPPLSIMYYH
VQRHYRASSR ELRRLGSLTL SPLYSHLADT LAGLSVLRAT GATYRFEEEN LRLLELNQRC
QFATSATMQW LDIRLQLMGA AVVSAIAGIA LVQHQQGLAN PGLVGLSLSY ALSLTGLLSG
LVSSFTQTEA MLVSVERLEE YTCDLPQEPQ GQPLQLGTGW LTQGGVEFQD VVLAYRPGLP
NALDGVTFCV QPGEKLGIVG RTGSGKSSLL LVLFRLLEPS SGRVLLDGVD TSQLELAQLR
SQLAIIPQEP FLFSGTVREN LDPQGLHKDR ALWQALKQCH LSEVITSMGG LDGELGEGGR
SLSLGQRQLL CLARALLTDA KILCIDEATA SVDQKTDQLL QQTICKRFAN KTVLTIAHRL
NTILNSDRVL VLQAGRVVEL DSPATLRNQP HSLFQQLLQS SQQGVPASLG GP
