ID Q6PSM0_RAT Unreviewed; 1272 AA. AC Q6PSM0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 133. DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189}; DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189}; GN Name=Abcb1a {ECO:0000313|RGD:619951}; GN Synonyms=Mdr1a {ECO:0000313|EMBL:AAS91649.1}; 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 {ECO:0000313|EMBL:AAS91649.1}; RN [1] {ECO:0000313|EMBL:AAS91649.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAS91649.1}; RX PubMed=16545584; DOI=10.1016/j.vascn.2005.12.004; RA Booth-Genthe C.L., Louie S.W., Carlini E.J., Li B., Leake B.F., RA Eisenhandler R., Hochman J.H., Mei Q., Kim R.B., Rushmore T.H., RA Yamazaki M.; RT "Development and characterization of LLC-PK1 cells containing Sprague- RT Dawley rat Abcb1a (Mdr1a): comparison of rat P-glycoprotein transport to RT human and mouse."; RL J. Pharmacol. Toxicol. Methods 54:78-89(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + CC phospholipidSide 2.; EC=7.6.2.1; CC Evidence={ECO:0000256|ARBA:ARBA00034036}; CC -!- INTERACTION: CC Q6PSM0; Q7TSE9: Hax1; NbExp=2; IntAct=EBI-930055, EBI-930005; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. CC {ECO:0000256|ARBA:ARBA00007577}. 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; AY582535; AAS91649.1; -; mRNA. DR AlphaFoldDB; Q6PSM0; -. DR IntAct; Q6PSM0; 2. DR ChEMBL; CHEMBL1075135; -. DR AGR; RGD:619951; -. DR RGD; 619951; Abcb1a. DR GO; GO:0045177; C:apical part of cell; IDA:RGD. DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD. DR GO; GO:0031526; C:brush border membrane; IDA:RGD. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0046581; C:intercellular canaliculus; ISO:RGD. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:RGD. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:RGD. DR GO; GO:0005524; F:ATP binding; ISO:RGD. DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD. DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid carrier activity; ISO:RGD. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:RGD. DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISO:RGD. DR GO; GO:0099038; F:ceramide floppase activity; ISO:RGD. DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD. DR GO; GO:0140328; F:floppase activity; ISO:RGD. DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:RGD. DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; ISO:RGD. DR GO; GO:0140341; F:phosphatidylethanolamine floppase activity; ISO:RGD. DR GO; GO:0022857; F:transmembrane transporter activity; ISO:RGD. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:RGD. DR GO; GO:0007512; P:adult heart development; ISO:RGD. DR GO; GO:0035932; P:aldosterone secretion; ISO:RGD. DR GO; GO:1905039; P:carboxylic acid transmembrane transport; ISO:RGD. DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD. DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IEP:RGD. DR GO; GO:0071312; P:cellular response to alkaloid; IEP:RGD. DR GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD. DR GO; GO:1905231; P:cellular response to borneol; IEP:RGD. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD. DR GO; GO:0071217; P:cellular response to external biotic stimulus; IEP:RGD. DR GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD. DR GO; GO:0036146; P:cellular response to mycotoxin; IEP:RGD. DR GO; GO:1904148; P:cellular response to nonylphenol; IEP:RGD. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD. DR GO; GO:0099040; P:ceramide translocation; ISO:RGD. DR GO; GO:0007623; P:circadian rhythm; IEP:RGD. DR GO; GO:0043215; P:daunorubicin transport; IMP:RGD. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:RGD. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IMP:RGD. DR GO; GO:0035640; P:exploration behavior; ISO:RGD. DR GO; GO:0140115; P:export across plasma membrane; ISO:RGD. DR GO; GO:0008585; P:female gonad development; ISO:RGD. DR GO; GO:0007565; P:female pregnancy; IEP:RGD. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0007507; P:heart development; ISO:RGD. DR GO; GO:0009914; P:hormone transport; IDA:RGD. DR GO; GO:0050892; P:intestinal absorption; IMP:RGD. DR GO; GO:0007595; P:lactation; IEP:RGD. DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:RGD. DR GO; GO:1904057; P:negative regulation of sensory perception of pain; IEP:RGD. DR GO; GO:0097719; P:neural tissue regeneration; ISO:RGD. DR GO; GO:0022008; P:neurogenesis; ISO:RGD. DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD. DR GO; GO:0001890; P:placenta development; IEP:RGD. DR GO; GO:1904446; P:positive regulation of establishment of Sertoli cell barrier; IMP:RGD. DR GO; GO:2001025; P:positive regulation of response to drug; IDA:RGD. DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:RGD. DR GO; GO:1902396; P:protein localization to bicellular tight junction; IMP:RGD. DR GO; GO:2001225; P:regulation of chloride transport; ISO:RGD. DR GO; GO:1904478; P:regulation of intestinal absorption; IMP:RGD. DR GO; GO:0097305; P:response to alcohol; IEP:RGD. DR GO; GO:0097327; P:response to antineoplastic agent; IEP:RGD. DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD. DR GO; GO:1905233; P:response to codeine; IEP:RGD. DR GO; GO:1905237; P:response to cyclosporin A; IEP:RGD. DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0033762; P:response to glucagon; IEP:RGD. DR GO; GO:1903416; P:response to glycoside; IEP:RGD. DR GO; GO:0001666; P:response to hypoxia; IEP:RGD. DR GO; GO:1902065; P:response to L-glutamate; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0010046; P:response to mycotoxin; IEP:RGD. DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD. DR GO; GO:0032570; P:response to progesterone; IEP:RGD. DR GO; GO:1905235; P:response to quercetin; IEP:RGD. DR GO; GO:0097068; P:response to thyroxine; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; ISO:RGD. DR GO; GO:0033189; P:response to vitamin A; IEP:RGD. DR GO; GO:0033280; P:response to vitamin D; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0072089; P:stem cell proliferation; ISO:RGD. DR GO; GO:0046865; P:terpenoid transport; ISO:RGD. DR GO; GO:0070633; P:transepithelial transport; ISO:RGD. DR GO; GO:0055085; P:transmembrane transport; IDA:RGD. DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:RGD. DR GO; GO:0042908; P:xenobiotic transport; ISO:RGD. DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IMP:RGD. DR CDD; cd18558; ABC_6TM_Pgp_ABCB1; 1. DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1. DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2. DR FunFam; 1.20.1560.10:FF:000043; Multidrug resistance protein 1A; 2. DR FunFam; 3.40.50.300:FF:000479; Multidrug resistance protein 1A; 2. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR039421; Type_1_exporter. DR PANTHER; PTHR43394:SF28; ATP-BINDING CASSETTE SUBFAMILY B MEMBER 1; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00434}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00434}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 48..71 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 107..132 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 182..200 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 206..225 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 285..308 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 320..338 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 700..724 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 744..769 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 851..871 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 927..946 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 966..987 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 51..349 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 384..620 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT DOMAIN 704..992 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 1027..1265 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 638..680 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 644..653 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 655..665 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..679 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 419..426 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" FT BINDING 1062..1069 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" SQ SEQUENCE 1272 AA; 140284 MW; 754F9496700083E5 CRC64; MELEEDLNGR ADKNFSKMGK KSKKEKKEKK PAVSVLTMFR YAGWLDRFYM LLGTLAAIIH GIALPLMMLV FGDMTDSFAN VGNNRSMSFY NATDIYAKLK DEMTTYAYYY TGIGAGVLIV AYIQVSLWCL AAGRQIHKIR QKFFHAIMNQ EIGWFDVHDV GELNTRLTDD VSKINEGIGD KIGMFFQAMA TFFGGFIIGF TRGWKLTLVI LAISPVLGLS AGIWAKILSS FTDKELQAYA KAGAVAEEVL AAIRTVIAFG GQKKELERYN NNLEEAKRLG IKKAITANIS MGAAFLLIYA SYALAFWYGT SLVISKEYTI GQVLTVFFSV LIGAFSVGQA SPNIEAFANA RGAAYEVFSI IDNKPSIDSF SKSGHKPDNI QGNLEFKNIH FSYPSRKDVQ ILKGLNLKVK SGQTVALVGN SGCGKSTTVQ LLQRLYDPIE GEVSIDGQDI RTINVRYLRE IIGVVSQEPV LFATTIAENI RYGRENVTMD EIEKAVKEAN AYDFIMKLPH KFDTLVGERG AQLSGGQKQR IAIARALVRN PKILLLDEAT SALDTESEAV VQAALDKARE GRTTIVIAHR LSTVRNADVI AGFDGGVIVE QGNHDELMRE KGIYFKLVMT QTAGNEIELG NEACESKDGI DNVDMSSKDS GSSLIRRRST RKSIRGPHDQ DGELSTKEAL DDDVPPASFW RILKLNSTEW PYFVVGVFCA IINGGLQPAF SIIFSKVVGV FTKNDTPEIQ RQNSNLFSLL FLILGIISFI TFFLQGFTFG KAGEILTKRL RYMVFKSMLR QDISWFDDPK NTTGALTTRL ANDAAQVKGA TGSRLAVITQ NIANLGTGII ISLIYGWQLT LLLLAIVPII AIAGVVEMKM LSGQALKDKK ELEGSGKIAT EAIENFRTVV SLTREQKFET MYAQSLQIPY RNALKKAHVF GITFSFTQAM MYFSYAACFR FGAYLVAREL MTFENVLLVF SAIVFGAMAV GQVSSFAPDY AKAKVSASHI IRIIEKIPEI DSYSTEGLKP NMLEGNVKFN GVMFNYPTRP NIPVLQGLSL EGKKGQTLAL VGSSGCGKST VVQLLERFYD PMAGTVFLDG KEIKQLNVQW LRAHLGIVSQ EPILFDCSIA ENIAYGDNSR VVSHEEIVKA AKEANIHQFI DSLPEKYNTR VGDKGTQLSG GQKQRIAIAR ALVRQPHILL LDEATSALDT ESEKVVQEAL DKAREGRTCI VIAHRLSTIQ NADLIVVIQN GQVKEHGTHQ QLLAQKGIYF SMVSVQAGAK RS //