ID G5C4X3_HETGA Unreviewed; 1442 AA.
AC G5C4X3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Multidrug resistance protein 1 {ECO:0000313|EMBL:EHB16584.1};
GN ORFNames=GW7_15201 {ECO:0000313|EMBL:EHB16584.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16584.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB16584.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; JH173394; EHB16584.1; -; Genomic_DNA.
DR STRING; 10181.G5C4X3; -.
DR eggNOG; KOG0055; Eukaryota.
DR InParanoid; G5C4X3; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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 Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003475097"
FT TRANSMEM 56..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 918..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..300
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 335..582
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 875..1163
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1198..1436
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 720..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 678..705
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 826..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 158004 MW; 9ED5D8C467821151 CRC64;
MVLGTLASII HGAALPLMML VFGDMTDSFA NAGSNSQSAA NTTVSFNLEE EMTTYAYYYT
GIGAGVLIAA YIQVSFWCLA AGRQTQKIRK QFFHAIMKQE VGWFDVHDVG ELNTRLTDDV
FKINEGIGDK IGMFFQSMAT FVAGFIIGFT RGWKLTLVIL AVSPVLGLSA AIWAKVLSSF
TDKELLAYAK AGAVAEEVLA AIRTVIAFGG QNKELERYNK NLEEAKRIGI KKAVSQHFSI
GAAFLLLLMY ASYALAFWYG TTLVLSGEYS IGKVLTVFFS VLIGAFSIGQ ASPNIEAFAN
ARGAAYEIFK IVDNEPCIDS FSTNGHKPDN IKGNLEFRNI HFSYPSRKEV KILKGLNLKV
QSGQTVALVG NSGCGKSTTV QLLQRLYDPS EGTVTIDGQD IRTINVRYLR EIIGVVSQEP
VLFATTIAEN IRYGRENVTM DEIQKAVKEA NAYDFIMKLP HKFDTLVGER GAQLSGGQKQ
RIAIARALVR NPKILLLDEA TSALDTESEA VVQVALDKPA ILSGDKSENV QDLLLLDVTP
LCLGIETAGG VMMVLIKHNT NIPTKKTQTF ATYSDNQPGV LIQIYEGERA MTKDNNLLGK
FELIGIPPTP PSVPQIEVTF DIDASGTLTV SAVDRSTRKE NKNTITNDKG CLSKEGKIND
EDKQKILDKC NEIIKWLDKN QTAEKEEFER QQKELEKVCN SINTKLYQSA NGMPGGMPGV
FPGGGAPPSG GASSGPTNEE AREGRTTIVI AHRLSTVRNA DVIAGFEDGV IVEKGNHEEL
MKEKGVYYKL VTMQTGGNEI ELGNEIFESK SEIDALVSSK DSGSSLIRRS TRRSTLGSQG
QDRRLSAKED LDENIPSVSF WRILKLNLTE WPYFVVGIFC AIVNGGLQPA FAVIFSRIIG
VFTRNDDAET KRQNSNLFSL LFLILGIISF ITFFLQGFTF GKAGEILTRR LRYLVFRSML
RQDVSWFDDP KNTTGALTAR LASDAAQVKG AVGSRLAVVA QNVANLGTGI IISFIYGWQL
TLLLLAIVPI IATAGVVEMK MLSGNALRDK EELEVSGKIA TEAIENFRTV VSLTREEKFE
HMYGQSLQIP YRNSLKKAHI FGITFSFTQA MMYFSYAACF RFGAFLVAHG FMSFENVMLV
FSAIVFGAMA VGQVSSFAPD YAKAKVSAAH IIRIIEKVPA IDSYSTEGLK PNMLEGNVTF
SDVVFKYPTR PDIPVLQGLS LQVKKGQTLA LVGSSGCGKS TAVQLLERFY DPLAGTVLVD
GTEIQQLNVQ WLRAQLGIVS QEPILFDCSI EENIAYGDNS RTVSQEEIVK AAKEANIHQF
IESLPEKYTT RVGDKGTQLS GGQKQRIAIA RALVRQPHIL LLDEATSALD TESEKVVQEA
LDKAREGRTC IVIAHRLSTI QNANVIVVIQ NGRVKEHGTH QQLLAQKGVY FSMVSVQAGA
KR
//
