MRP5_RAT
ID MRP5_RAT Reviewed; 1436 AA.
AC Q9QYM0; A0A0G2K6R4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ATP-binding cassette sub-family C member 5;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O15440};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:O15440};
DE AltName: Full=Multidrug resistance-associated protein 5;
GN Name=Abcc5 {ECO:0000312|RGD:70913}; Synonyms=Mrp5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Homma M., Suzuki H., Sugiyama Y.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro).
CC Acts also as a general glutamate conjugate and analog transporter that
CC can limit the brain levels of endogenous metabolites, drugs, and
CC toxins. Confers resistance to the antiviral agent PMEA. Able to
CC transport several anticancer drugs including methotrexate, and
CC nucleotide analogs in vitro, however it does with low affinity, thus
CC the exact role of ABCC5 in mediating resistance still needs to be
CC elucidated. Acts as a heme transporter required for the translocation
CC of cytosolic heme to the secretory pathway (By similarity). May play a
CC role in energy metabolism by regulating the glucagon-like peptide 1
CC (GLP-1) secretion from enteroendocrine cells (By similarity).
CC {ECO:0000250|UniProtKB:O15440, ECO:0000250|UniProtKB:Q9R1X5}.
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:0000250|UniProtKB:O15440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189;
CC Evidence={ECO:0000250|UniProtKB:O15440};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66757;
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66737;
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66721;
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66765;
CC Evidence={ECO:0000250|UniProtKB:O15440};
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:0000250|UniProtKB:Q9R1X5}. Apical cell membrane
CC {ECO:0000250|UniProtKB:O15440}; 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}.
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. The authors conclude that ABCC5 is a
CC low-affinity cyclic nucleotide transporter and a major function in cGMP
CC excretion is unlikely. {ECO:0000250|UniProtKB:O15440,
CC ECO:0000250|UniProtKB:Q9R1X5}.
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; AB020209; BAA88897.1; -; mRNA.
DR EMBL; AABR07034695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07034696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_446376.1; NM_053924.1.
DR AlphaFoldDB; Q9QYM0; -.
DR SMR; Q9QYM0; -.
DR STRING; 10116.ENSRNOP00000002316; -.
DR GlyGen; Q9QYM0; 8 sites.
DR PaxDb; Q9QYM0; -.
DR PRIDE; Q9QYM0; -.
DR GeneID; 116721; -.
DR KEGG; rno:116721; -.
DR CTD; 10057; -.
DR RGD; 70913; Abcc5.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; Q9QYM0; -.
DR OMA; FVKFFGW; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9QYM0; -.
DR Reactome; R-RNO-2142850; Hyaluronan biosynthesis and export.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:Q9QYM0; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000029178; Expressed in stomach and 19 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
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:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015232; F:heme transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015216; F:purine nucleotide transmembrane transporter activity; ISO:RGD.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:RGD.
DR GO; GO:0070730; P:cAMP transport; ISO:RGD.
DR GO; GO:0070731; P:cGMP transport; ISO:RGD.
DR GO; GO:0140115; P:export across plasma membrane; ISO:RGD.
DR GO; GO:0098838; P:folate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034775; P:glutathione transmembrane transport; ISO:RGD.
DR GO; GO:0035351; P:heme transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015865; P:purine nucleotide transport; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042908; P:xenobiotic transport; ISO:RGD.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Endosome; Glycoprotein; Golgi apparatus;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1436
FT /note="ATP-binding cassette sub-family C member 5"
FT /id="PRO_0000093365"
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 12..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
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 COMPBIAS 796..810
FT /note="Polar 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:0000250|UniProtKB:Q9R1X5"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15440"
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 29
FT /note="T -> Q (in Ref. 1; BAA88897)"
FT CONFLICT 35..42
FT /note="DPSSGEQI -> EPRFRRTR (in Ref. 1; BAA88897)"
FT CONFLICT 1270
FT /note="A -> T (in Ref. 1; BAA88897)"
SQ SEQUENCE 1436 AA; 160514 MW; 37E3CD29410B8E33 CRC64;
MKDIDMGKEY IIPSPGYRSV RDRSTIPGTH GDREDPSSGE QISLECQDAL ETAARVEGLS
LDISVHSHLQ ILDEEHTKGK YHHGLSALKP FRTTTKHQHP VDNAGLFSYM TFSWLSPLAQ
VVHKKGELLM EDVWPLSKYE SSDVNCRRLE RLWQEELNEV GPDAASLRRV VWIFCRTRLI
LSIVCLMITQ LAGFSGPAFV VKHLLEYTQA TESNLQYSLL LVLGLLLTEV VRSWSLALTW
ALNYRTGVRL RGAVLTMAFK KILKLKNIKE KSLGELINIC SNDGQRMFEA AAVGSLLAGG
PVVAILGMIY NVIILGPTGF LGSAVFILFY PAMMFVSRLT AYFRRKCVAA TDDRVQKMNE
VLTYIKFIKM YAWVKAFSQC VQKIREEERR ILEKAGYFQS ITVGVAPIVV VIASVVTFSV
HMTLGFDLTA AQAFTVVTVF NSMTFALKVT PFSVKSLSEA SVAVDRFKSL FLMEEVHMIK
NKPASPHIKI EMKNATLAWD SSHSSTQSSP KLTPKVKKDK RAPKGKKEKS RQLQHTEHQA
VLAEQKGHLL LDSDERPSPE EEEGKQIHAG SMRLQRTLYN IDLEIEEGKL VGICGSVGSG
KTSLISAILG QMTLLEGSIA VSGTFAYVAQ QAWILNATLR DNILFGKEFD EERYNSVLNS
CCLRPDLAIL PNSDLTEIGE RGANLSGGQR QRISLARALY SDRSIYILDD PLSALDAHVG
NHIFNSAIRK RLKSKTVLFV THQLQYLVDC DEVIFMKEGC ITERGTHEEL MNLNGDYATI
FNNLLLGETP PVEINSKKEA SGSQKSQDKG PKPGSVKKEK AVKSEEGQLV QVEEKGQGSV
PWSVYWVYIQ AAGGPLAFLV IMVLFMLNVG STAFSTWWLS YWIKQGSGNS TVFEGNRSSV
SDSMRDNPFL QYYASIYALS MAVMLILKAI RGVVFVKGTL RASSRLHDEL FRRILRSPMK
FFDTTPTGRI LNRFSKDMDE VDVRLPFQAE MFIQNVILVF FCVGMIAGVF PWFLVAVGPL
LILFSVLHIV SRVLIRELKR LDNITQSPFL SHITSSIQGL ATIHAYNKRQ EFLHRYQELL
DDNQAPFFLF TCAMRWLAVR LDLISIALIT TTGLMIVLMH GQIPSAYAGL AISYAVQLTG
LFQFTVRLAS ETEARFTSVE RINHYIKTLS LEAPARIKNK APPHDWPQEG EITFENAEMR
YRENLPLVLK KVSFTIKPKE KIGIVGRTGS GKSSLGMALF RLVELSGGCI KIDGVRISDI
GLADLRSKLA IIPQEPVLFS GTVRSNLDPF NQYTEEQIWD ALERTHMKEC IAQLPLKLES
EVMENGDNFS VGERQLLCIA RALLRHCKIL ILDEATAAMD TETDLLIQET IREAFADCTM
LTIAHRLHTV LGSDRIMVLA QGQVVEFDTP SVLLSNDSSR FYAMCAAAEN KVAVKG
