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Multidrug resistance protein 1 (EC 3.6.3.44) (ATP-binding cassette sub-family B member 1) (P-glycoprotein 1) (CD antigen CD243)

 MDR1_RAT                Reviewed;        1277 AA.
P43245; Q63426; Q63427;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
20-JUN-2018, entry version 144.
RecName: Full=Multidrug resistance protein 1;
EC=3.6.3.44;
AltName: Full=ATP-binding cassette sub-family B member 1;
AltName: Full=P-glycoprotein 1;
AltName: CD_antigen=CD243;
Name=Abcb1; Synonyms=Mdr1, Mdr1b, Pgy1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1682220; DOI=10.1016/0378-1119(91)90203-N;
Silverman J.A., Raunio H., Gant T.W., Thorgeirsson S.S.;
"Cloning and characterization of a member of the rat multidrug
resistance (mdr) gene family.";
Gene 106:229-236(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1212-1277.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1348630; DOI=10.1016/0167-4781(92)90523-3;
Deuchars K.L., Duthie M., Ling V.;
"Identification of distinct P-glycoprotein gene sequences in rat.";
Biochim. Biophys. Acta 1130:157-165(1992).
-!- FUNCTION: Energy-dependent efflux pump responsible for decreased
drug accumulation in multidrug-resistant cells.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + xenobiotic(In) = ADP + phosphate
+ xenobiotic(Out).
-!- SUBUNIT: Interacts with PSMB5. Finds in a complex with ABCB1,
TFPI2 and PPP2R3C; leading to the dephosphorylation of ABCB1.
{ECO:0000250|UniProtKB:P08183}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
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EMBL; M81855; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X61103; CAA43415.1; -; Genomic_DNA.
EMBL; X61104; CAA43416.1; -; Genomic_DNA.
PIR; JH0502; JH0502.
UniGene; Rn.144554; -.
UniGene; Rn.154810; -.
ProteinModelPortal; P43245; -.
SMR; P43245; -.
STRING; 10116.ENSRNOP00000049952; -.
ChEMBL; CHEMBL1075229; -.
PaxDb; P43245; -.
PRIDE; P43245; -.
RGD; 3318; Abcb1.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
HOVERGEN; HBG080809; -.
InParanoid; P43245; -.
PhylomeDB; P43245; -.
PRO; PR:P43245; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; IDA:RGD.
GO; GO:0008559; F:xenobiotic transmembrane transporting ATPase activity; IEA:UniProtKB-EC.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071217; P:cellular response to external biotic stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0014045; P:establishment of endothelial blood-brain barrier; IMP:RGD.
GO; GO:0007595; P:lactation; IEP:RGD.
GO; GO:0001890; P:placenta development; IEP:RGD.
GO; GO:0097327; P:response to antineoplastic agent; IEP:RGD.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0042493; P:response to drug; IMP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:1903416; P:response to glycoside; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010046; P:response to mycotoxin; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Complete proteome; Glycoprotein;
Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1277 Multidrug resistance protein 1.
/FTId=PRO_0000093335.
TOPO_DOM 1 42 Cytoplasmic. {ECO:0000250}.
TRANSMEM 43 65 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 66 115 Extracellular. {ECO:0000250}.
TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 137 185 Cytoplasmic. {ECO:0000250}.
TRANSMEM 186 207 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 208 214 Extracellular. {ECO:0000250}.
TRANSMEM 215 235 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 236 293 Cytoplasmic. {ECO:0000250}.
TRANSMEM 294 315 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 316 329 Extracellular. {ECO:0000250}.
TRANSMEM 330 351 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 352 709 Cytoplasmic. {ECO:0000250}.
TRANSMEM 710 730 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 731 754 Extracellular. {ECO:0000250}.
TRANSMEM 755 775 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 776 830 Cytoplasmic. {ECO:0000250}.
TRANSMEM 831 853 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 854 854 Extracellular. {ECO:0000250}.
TRANSMEM 855 874 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 875 934 Cytoplasmic. {ECO:0000250}.
TRANSMEM 935 957 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 958 973 Extracellular. {ECO:0000250}.
TRANSMEM 974 995 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 996 1277 Cytoplasmic. {ECO:0000250}.
DOMAIN 49 356 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 391 627 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 709 1000 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1035 1272 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 426 433 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1070 1077 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 641 641 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06795}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:P06795}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 1227 1227 V -> I (in Ref. 2; CAA43415/CAA43416).
{ECO:0000305}.
CONFLICT 1270 1270 V -> VSV (in Ref. 2; CAA43415).
{ECO:0000305}.
SEQUENCE 1277 AA; 141387 MW; 8AFDDD619D2934C1 CRC64;
MEFEEGLNGR ADKNFSKMGK KSKKEKEKKP AVGIFGMFRY ADWLDKLCMA LGTLAAIIHG
TLLPLLMLVF GYMTDSFTPS RDPHSDRAIT NQSEINSTHT VSDTSLEEDM AMYAYYYTGI
GAGVLIVAYI QVSLWCLAAG RQIHKIRQKF FHAIMNQEIG WFDVNDAGEL NTRLTDDVSK
INDGIGDKLG MFFQSITTFS AGFIIGFISG WKLTLVILAV SPLIGLSSAM WAKVLTSFTN
KELQAYAKAG AVAEEVLAAI RTVIAFGGQK KELERYNKNL EEAKRVGIKK AITANISIGI
AYLLVYASYA LAFWYGTSLV LSNEYSIGQV LTVFFSILLG TFSIGHLAPN IEAFANARGA
AYEIFKIIDN EPSIDSFSTK GHKPDSIMGN LEFKNVYFNY PSRSEVKILK GLNLKVKSGQ
TVALVGNSGC GKSTTVQLLQ RLYDPIEGEV SIDGQDIRTI NVRYLREIIG VVSQEPVLFA
TTIAENIRYG RENVTMDEIE KAVKEANAYD FIMKLPHKFD TLVGERGAQL SGGQKQRIAI
ARALVRNPKI LLLDEATSAL DTESEAVVQA ALDKAREGRT TIVIAHRLST VRNADVIAGF
DGGVIVEQGN HEELMKEKGI YFKLVMTQTR GNEIEPGNNA YESQSDTGAS ELTSEESKSP
LIRRSIRRSI HRRQDQERRL SSKEDVDEDV PMVSFWQILK LNISEWPYLV VGVLCAVING
CIQPVFAIVF SKIVGVFSRD DDHETKQRNC NLFSLLFLVM GMISFVTYFF QGFTFGKAGE
ILTKRLRYMV FKSMLRQDIS WFDDHKNTTG SLTTRLASDA SNVKGAMGSR LAVVTQNVAN
LGTGIILSLV LVYGWQLTLL LVVIIPLIVL GGIIEMKLLS GQALKDKKEL EISGKIATEA
IENFRTVVSL TREQKFETMY AQSLQIPYRN ALKKAHVFGI TFAFTQAMIY FSYAACFRFG
AYLVARELMT FENVMLVFSA VVFGAMAAGN TSSFAPDYAK AKVSASHIIG IIEKIPEIDS
YSTEGLKPNW LEGNVKFNGV KFNYPTRPNI PVLQGLSFEV KKGQTLRLVG SSGCGKSTVV
QLLERFYNPM AGTVFLDGKE IKQLNVQCVR ALGIVSQEPI LFDCSIAENI AYGDNSRVVS
HEEIVRAARE ANIHQFIDSL PEKYNTRVGD KGTQLSGGQK QRIAIARALV RQPHILLLDE
ATSALDTESE KVVQEALDKA REGRTCVVIA HRLSTIQNAD LIVVIQNGQV KEHGTHQQLL
AQKGIYFSMV QAGAKRS


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