ID B9SAP4_RICCO Unreviewed; 1506 AA.
AC B9SAP4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=ABC-type xenobiotic transporter {ECO:0000256|ARBA:ARBA00012191};
DE EC=7.6.2.2 {ECO:0000256|ARBA:ARBA00012191};
GN ORFNames=RCOM_1177870 {ECO:0000313|EMBL:EEF39248.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034018};
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. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily.
CC {ECO:0000256|ARBA:ARBA00009726}.
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DR EMBL; EQ973909; EEF39248.1; -; Genomic_DNA.
DR RefSeq; XP_002523063.1; XM_002523017.2.
DR RefSeq; XP_015577230.1; XM_015721744.1.
DR STRING; 3988.B9SAP4; -.
DR GeneID; 8259848; -.
DR KEGG; rcu:8259848; -.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; B9SAP4; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF362; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR HOMOLOG; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000313|EMBL:EEF39248.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
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 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..963
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 984..1005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1017..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1081..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1175..1195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1207..1225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..607
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 641..864
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 949..1227
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1264..1498
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 877..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1506 AA; 168781 MW; 8EAE7B36698F36CD CRC64;
MASPPWITSL SCSSSVIQSD GDTSFPLLFQ WLRFVFLSPC PQRALLSSVD LLFLLVLLVF
VLQKLFSRFS SSGHSKSDID KPLIGNSRVL IRTTIWFKLS LIVTVFLTFG YTAVSILAFI
SESTELPWKI VDGSFWLVQA ITHAVISILI IHEKRFEAVT HPLSLRIYWV ANFIVITLFM
SSGIIRLVAQ QNIMVLDDII SIVSFPLSIV LLSVAIRGST GITVTRESEP VIDDETKLHD
SDSLSKGNVS GFASASRVSK AFWLWMNPLL SKGYKSPLKI DEVPTLSPEH RAERMSQLFA
AKWPKPHEKS KHPVRTTLLR CFWKEIAFTA FLAIMRLCVM YVGPLLIQSF VDYTSGKRTS
PYEGYYLVLI LLVAKFFEVL IVHQFNFNSQ KLGMLIRSTL ITSLYRKGLR LSCSARQSHG
VGQIVNYMAV DAQQLSDMML QLHAIWLMPL QVTVALVLLY NALGVSVIAA LIGIACVMVF
ALYGTRRNNR FQKNLMMNRD SRMKATNEML NYMRVIKFQA WEEHFNKRIQ NFRESEFEWL
SKFMYSVSGN IIVMWCTPLL ISTVTFGTAL LFGVPLDAGT VFTTTSIFKI LQDPIRSFPQ
SMISFSQAMI SLERLDRYML SKELVEQSVE RVDGCDGRIA VEIKDGSFSW DDESEDEVLK
NINFEIKKGE LTAIVGTVGS GKSSLLASVL GEMHKISGKV RVCGTTAYVA QTSWIQNGTI
QENILFGLPM DREKYNEVIR VCCLEKDLEM MDYGDQTEIG ERGINLSGGQ KQRIQLARAV
YQDCDIYLLD DVFSAVDAHT GSDIFKECVR GALKGKTILL VTHQVDFLHN IDLIMVMRDG
MIVQSGKYNN LVKSGMDFGA LVAAHDTAME LVEAGTAVPG ENSPRPPKSP QSSSNALEAN
GENKHLDQPK SEKGTSKLVE EEERETGKVG LHVYKQYCTA AFGWWGVTVA LLLSIVWQAS
LMAADYWLAY ETSEERASIF DPSLFISVYA VITAASLVLL TMRALFVNLM GLKTAQIFFM
GILHSILHAP MSFFDTTPSG RILSRASADQ SNVDLFIPFV LGLTVAMYIT LLSIIIITCQ
YAWPTVFLLV PLGWLNIWYR GYFLSTSREL TRLDSITKAP IIHHFSESIS GVLTIRSFRK
LERFSQENVN RVDANLRMDF HNNGSNEWLG FRLELMGSFI LCMSAMFLIV LPSSIIRPEN
VGLSLSYGLS LNGVLFWAIY MSCFVENRMV SVERIKQFTN IPSEAAWKIK DRIPPPSWPA
QGNVDLKDLQ VKYRPNTPLV LKGITLSIYG GEKIGVVGRT GSGKSTLIQV FFRLVEPTGG
KIIIDGIDIC MLGLQDLRSR FGIIPQEPVL FEGTVRSNID PIGQYTDEQI WKSLERCQLK
DVVAAKPEKL DALVADNGDN WSVGQRQLLC LGRVMLKRSR LLFMDEATAS VDSQTDGVIQ
KIIREDFAAC TIISIAHRIP TVMDCDRVLV IDAGKAKEFD KPSRLLERPS LFAALVQEYA
NRSAGL
//