MRP5_MOUSE
ID MRP5_MOUSE Reviewed; 1436 AA.
AC Q9R1X5; O88284; Q5CZY2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ATP-binding cassette sub-family C member 5;
DE EC=7.6.2.- {ECO:0000269|PubMed:17229149};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:O15440};
DE AltName: Full=Multi-specific organic anion transporter C;
DE Short=MOAT-C;
DE AltName: Full=Multidrug resistance-associated protein 5 {ECO:0000303|PubMed:10721709};
DE AltName: Full=SMRP;
GN Name=Abcc5 {ECO:0000312|MGI:MGI:1351644};
GN Synonyms=Abcc5a, Mrp5 {ECO:0000303|PubMed:10721709};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10721709; DOI=10.1016/s0378-1119(99)00529-6;
RA Suzuki T., Sasaki H., Kuh H.J., Agui M., Tatsumi Y., Tanabe S., Terada M.,
RA Saijo N., Nishio K.;
RT "Detailed structural analysis on both human MRP5 and mouse mrp5
RT transcripts.";
RL Gene 242:167-173(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 261-266, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1302-1436.
RA Suzuki T., Kuh H., Nishio K.;
RT "Molecular cloning of mouse homologue of SMRP/MRP5.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16361063; DOI=10.1016/j.neuroscience.2005.11.011;
RA Soontornmalai A., Vlaming M.L., Fritschy J.M.;
RT "Differential, strain-specific cellular and subcellular distribution of
RT multidrug transporters in murine choroid plexus and blood-brain barrier.";
RL Neuroscience 138:159-169(2006).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17229149; DOI=10.1111/j.1742-4658.2006.05591.x;
RA de Wolf C.J., Yamaguchi H., van der Heijden I., Wielinga P.R.,
RA Hundscheid S.L., Ono N., Scheffer G.L., de Haas M., Schuetz J.D.,
RA Wijnholds J., Borst P.;
RT "cGMP transport by vesicles from human and mouse erythrocytes.";
RL FEBS J. 274:439-450(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-505; SER-509 AND
RP THR-513, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=24836561; DOI=10.1016/j.cmet.2014.03.030;
RA Korolnek T., Zhang J., Beardsley S., Scheffer G.L., Hamza I.;
RT "Control of metazoan heme homeostasis by a conserved multidrug resistance
RT protein.";
RL Cell Metab. 19:1008-1019(2014).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26515061; DOI=10.1074/jbc.m115.692103;
RA Jansen R.S., Mahakena S., de Haas M., Borst P., van de Wetering K.;
RT "ATP-binding Cassette Subfamily C Member 5 (ABCC5) Functions as an Efflux
RT Transporter of Glutamate Conjugates and Analogs.";
RL J. Biol. Chem. 290:30429-30440(2015).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31338999; DOI=10.1002/oby.22521;
RA Cyranka M., Veprik A., McKay E.J., van Loon N., Thijsse A., Cotter L.,
RA Hare N., Saibudeen A., Lingam S., Pires E., Larraufie P., Reimann F.,
RA Gribble F., Stewart M., Bentley E., Lear P., McCullagh J., Cantley J.,
RA Cox R.D., de Wet H.;
RT "Abcc5 Knockout Mice Have Lower Fat Mass and Increased Levels of
RT Circulating GLP-1.";
RL Obesity 27:1292-1304(2019).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that actively extrudes physiological compounds, and xenobiotics
CC from cells. Mediates ATP-dependent transport of endogenous metabolites
CC like cyclic nucleotides, such as cAMP and cGMP, folic acid and N-
CC lactoyl-amino acids (in vitro) (By similarity) (PubMed:17229149). Acts
CC also as a general glutamate conjugate and analog transporter that can
CC limit the brain levels of endogenous metabolites, drugs, and toxins
CC (PubMed:26515061). Confers resistance to the antiviral agent PMEA (By
CC similarity). Able to transport several anticancer drugs including
CC methotrexate, and nucleotide analogs in vitro, however it does with low
CC affinity (By similarity). Acts as a heme transporter required for the
CC translocation of cytosolic heme to the secretory pathway
CC (PubMed:24836561). May play a role in energy metabolism by regulating
CC the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine
CC cells (PubMed:31338999). {ECO:0000250|UniProtKB:O15440,
CC ECO:0000269|PubMed:17229149, ECO:0000269|PubMed:24836561,
CC ECO:0000269|PubMed:26515061, ECO:0000269|PubMed:31338999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57746, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17229149};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189;
CC Evidence={ECO:0000269|PubMed:17229149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58165, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-acetyl-L-aspartyl-L-glutamate(in) = ADP + H(+) +
CC N-acetyl-L-aspartyl-L-glutamate(out) + phosphate;
CC Xref=Rhea:RHEA:66728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66729;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate(in) =
CC ADP + H(+) + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate(out) +
CC phosphate; Xref=Rhea:RHEA:66732, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:76935, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66733;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-acetyl-L-glutamate(in) = ADP + H(+) + N-acetyl-
CC L-glutamate(out) + phosphate; Xref=Rhea:RHEA:66740,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:44337, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-acetyl-L-aspartate(in) = ADP + H(+) + N-acetyl-
CC L-aspartate(out) + phosphate; Xref=Rhea:RHEA:66744,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66745;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-[5-amino-1-(beta-D-ribosyl)imidazole-4-
CC carboxamido]succinate(in) + ATP + H2O = (2S)-2-[5-amino-1-(beta-D-
CC ribosyl)imidazole-4-carboxamido]succinate(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167466, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66753;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + domoate(in) + H2O = ADP + domoate(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:66756, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167470, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-citrylglutamate(in) + H2O = ADP + beta-
CC citrylglutamate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66736,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76942, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + kainate(in) = ADP + H(+) + kainate(out) +
CC phosphate; Xref=Rhea:RHEA:66760, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:156548, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-[(S)-lactoyl]-L-phenylalanine(in) = ADP + H(+) +
CC N-[(S)-lactoyl]-L-phenylalanine(out) + phosphate;
CC Xref=Rhea:RHEA:66720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167456,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + folate(in) + H2O = ADP + folate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:66764, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:62501,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15440};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 mM for cGMP {ECO:0000269|PubMed:17229149};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O15440}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus lumen {ECO:0000250|UniProtKB:O15440}.
CC Endosome membrane {ECO:0000250|UniProtKB:O15440}. Cytoplasmic granule
CC {ECO:0000269|PubMed:24836561}. Apical cell membrane
CC {ECO:0000269|PubMed:16361063}; Multi-pass membrane protein
CC {ECO:0000255}. Note=In most cells, routes to the basolateral plasma
CC membrane, but in the brain capillary endothelial cells that form the
CC blood-brain barrier, resides in the apical membrane.
CC {ECO:0000250|UniProtKB:O15440, ECO:0000269|PubMed:16361063}.
CC -!- TISSUE SPECIFICITY: Detected in brain endothelial cells.
CC {ECO:0000269|PubMed:16361063}.
CC -!- DISRUPTION PHENOTYPE: Mrp5 knockout mice are viable with no overt
CC phenotypes, deficient mice accumulate endogenous glutamate conjugates
CC in several tissues, including the inhibitory neuropeptides N-
CC acetylaspartylglutamate (NAAG) and N-acetylaspartyldiglutamate (NAAG2),
CC but brain in particular (PubMed:26515061). Abcc5-/- mice show lower
CC white and brown adipose tissue and increased glucagon-like peptide 1
CC (GLP-1) release from enteroendocrine cells of the small intestine, and
CC are more insulin sensitive (PubMed:31338999).
CC {ECO:0000269|PubMed:26515061, ECO:0000269|PubMed:31338999}.
CC -!- MISCELLANEOUS: Although other labs have confirmed the ability of ABCC5
CC to transport cGMP in an ATP-dependent manner, they obtained a much
CC lower affinity for this substrate (By similarity) (PubMed:17229149).
CC The authors conclude that ABCC5 is a low-affinity cyclic nucleotide
CC transporter and a major function in cGMP excretion is unlikely (By
CC similarity) (PubMed:17229149). {ECO:0000250|UniProtKB:O15440,
CC ECO:0000269|PubMed:17229149}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AB019003; BAA76609.1; -; mRNA.
DR EMBL; AB012090; BAA32782.1; -; mRNA.
DR EMBL; CH466521; EDK97565.1; -; Genomic_DNA.
DR EMBL; BC090629; AAH90629.1; -; mRNA.
DR CCDS; CCDS28045.1; -.
DR RefSeq; NP_038818.2; NM_013790.2.
DR RefSeq; XP_006522271.1; XM_006522208.3.
DR AlphaFoldDB; Q9R1X5; -.
DR SMR; Q9R1X5; -.
DR BioGRID; 205221; 1.
DR STRING; 10090.ENSMUSP00000078158; -.
DR GlyGen; Q9R1X5; 8 sites.
DR iPTMnet; Q9R1X5; -.
DR PhosphoSitePlus; Q9R1X5; -.
DR EPD; Q9R1X5; -.
DR jPOST; Q9R1X5; -.
DR MaxQB; Q9R1X5; -.
DR PaxDb; Q9R1X5; -.
DR PeptideAtlas; Q9R1X5; -.
DR PRIDE; Q9R1X5; -.
DR ProteomicsDB; 291410; -.
DR Antibodypedia; 18937; 421 antibodies from 38 providers.
DR DNASU; 27416; -.
DR Ensembl; ENSMUST00000079158; ENSMUSP00000078158; ENSMUSG00000022822.
DR Ensembl; ENSMUST00000115547; ENSMUSP00000111209; ENSMUSG00000022822.
DR GeneID; 27416; -.
DR KEGG; mmu:27416; -.
DR UCSC; uc007ypp.1; mouse.
DR CTD; 10057; -.
DR MGI; MGI:1351644; Abcc5.
DR VEuPathDB; HostDB:ENSMUSG00000022822; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000155470; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9R1X5; -.
DR OMA; FVKFFGW; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9R1X5; -.
DR TreeFam; TF105202; -.
DR Reactome; R-MMU-2142850; Hyaluronan biosynthesis and export.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 27416; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Abcc5; mouse.
DR PRO; PR:Q9R1X5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9R1X5; protein.
DR Bgee; ENSMUSG00000022822; Expressed in superior frontal gyrus and 255 other tissues.
DR ExpressionAtlas; Q9R1X5; baseline and differential.
DR Genevisible; Q9R1X5; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IMP:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IMP:MGI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1901505; F:carbohydrate derivative transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015232; F:heme transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022884; F:macromolecule transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015216; F:purine nucleotide transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0070730; P:cAMP transport; ISO:MGI.
DR GO; GO:0070731; P:cGMP transport; ISO:MGI.
DR GO; GO:0140115; P:export across plasma membrane; ISO:MGI.
DR GO; GO:0098838; P:folate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034775; P:glutathione transmembrane transport; ISO:MGI.
DR GO; GO:0035351; P:heme transmembrane transport; ISS:UniProtKB.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IMP:MGI.
DR GO; GO:0015865; P:purine nucleotide transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042908; P:xenobiotic transport; ISO:MGI.
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; IPR030238; ABCC5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF196; PTHR24223:SF196; 1.
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 ATP-binding; Cell membrane; Direct protein sequencing; Endosome;
KW Glycoprotein; Golgi apparatus; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1436
FT /note="ATP-binding cassette sub-family C member 5"
FT /id="PRO_0000093364"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1126..1146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 179..459
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 562..783
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 858..1154
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1192..1426
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 595..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1226..1233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 146
FT /note="S -> C (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> M (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Y -> C (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="V -> I (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="C -> R (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1098
FT /note="A -> P (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1103
FT /note="L -> I (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="T -> S (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118..1124
FT /note="LMHGQIP -> SGMARSL (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="T -> I (in Ref. 1; BAA76609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1436 AA; 161125 MW; 6B40BA516D8BE87D CRC64;
MKDIDMGKEY IIPSPGYRSD RDRSAVPGQH RDPEEPRFRR TRSLECQDAL ETAARVEGLS
LDISVHSHLQ ILDEEHSKGK YHHGLSVLKP FRTTTKHQHP VDNAGLFSYM TFSWLSPLAR
VVHKKGELLM EDVWPLSKYE SSDVNSRRLE RLWQEELNEV GPDAASLRRV VWIFCRTRLI
LSIVCLMITQ LAGFSGPAFV VKHLLEYTQA TESNLQYSLL LVLGLLLTEV VRSWSLALTW
ALNYRTGVRL RGAILTMAFK KILKLKNIKE KSLGELINIC SNDGQRMFEA AAVGSLLAGG
PVVAILGMIY NVIILGPTGF LGSAVFILFY PAMMFVSRLT AYFRRKCVAA TDDRVQKMNE
VLTYIKFIKM YAWVKAFSQC VQKIREEERR ILEKAGYFQS ITVGVAPIVV VIASVVTFSV
HMTLGFHLTA AQAFTVVTVF NSMTFALKVT PFSVKSLSEA SVAVDRFKSL FLMEEVHMIK
NKPASPHIKI EMKNATLAWD SSHSSIQNSP KLTPKMKKDK RATRGKKEKS RQLQHTEHQA
VLAEQKGHLL LDSDERPSPE EEEGKQIHTG SLRLQRTLYN IDLEIEEGKL VGICGSVGSG
KTSLVSAILG QMTLLEGSIA VSGTFAYVAQ QAWILNATLR DNILFGKEFD EERYNSVLNS
CCLRPDLAIL PNSDLTEIGE RGANLSGGQR QRISLARALY SDRSIYILDD PLSALDAHVG
NHIFNSAIRK RLKSKTVLFV THQLQYLVDC DEVIFMKEGC ITERGTHEEL MNLNGDYATI
FNNLLLGETP PVEINSKKEA TGSQKSQDKG PKPGSVKKEK AVKSEEGQLV QVEEKGQGSV
PWSVYWVYIQ AAGGPLAFLV IMVLFMLNVG STAFSTWWLS YWIKQGSGNS TVYQGNRSFV
SDSMKDNPFM QYYASIYALS MAVMLILKAI RGVVFVKGTL RASSRLHDEL FRRILRSPMK
FFDTTPTGRI LNRFSKDMDE VDVRLPFQAE MFIQNVILVF FCVGMIAGVF PWFLVAVGPL
LILFSLLHIV SRVLIRELKR LDNITQSPFL SHITSSIQGL ATIHAYNKRQ EFLHRYQELL
DDNQAPFFLF TCAMRWLAVR LDLISIALIT TTGLMIVLMH GQIPSAYAGL AISYAVQLTG
LFQFTVRLAS ETEARFTSVE RINHYIKTLS LEAPARIKNK APPHDWPQEG EVTFENAEMR
YRENLPLVLK KVSFTIKPKE KIGIVGRTGS GKSSLGMALF RLVELSGGCI KIDGIRISDI
GLADLRSKLA IIPQEPVLFS GTVRSNLDPF NQYTEDQIWD ALERTHMKEC IAQLPLKLES
EVMENGDNFS VGERQLLCIA RALLRHCKIL ILDEATAAMD TETDLLIQET IREAFADCTM
LTIAHRLHTV LGSDRIMVLA QGQVVEFDTP SVLLSNDSSR FYAMFAAAEN KVAVKG
