AB7C_ARATH
ID AB7C_ARATH Reviewed; 1493 AA.
AC Q9LK62; Q8LGU0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ABC transporter C family member 7;
DE Short=ABC transporter ABCC.7;
DE Short=AtABCC7;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 7;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 7;
DE AltName: Full=Multidrug resistance-associated protein 7;
GN Name=ABCC7; Synonyms=MRP7; OrderedLocusNames=At3g13100; ORFNames=MJG19.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA Martinoia E., Schulz B.;
RT "Family business: the multidrug-resistance related protein (MRP) ABC
RT transporter genes in Arabidopsis thaliana.";
RL Planta 216:107-119(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [5]
RP GENE FAMILY.
RX PubMed=11855639; DOI=10.1007/s004250100661;
RA Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT "Multifunctionality of plant ABC transporters -- more than just
RT detoxifiers.";
RL Planta 214:345-355(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Pump for glutathione S-conjugates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12430019}.
CC -!- INDUCTION: By salicylic acid (SA). {ECO:0000269|PubMed:12430019}.
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; AJ507129; CAD45086.1; -; mRNA.
DR EMBL; AP000375; BAB01401.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75296.1; -; Genomic_DNA.
DR RefSeq; NP_187917.3; NM_112149.4.
DR AlphaFoldDB; Q9LK62; -.
DR SMR; Q9LK62; -.
DR STRING; 3702.AT3G13100.1; -.
DR iPTMnet; Q9LK62; -.
DR PaxDb; Q9LK62; -.
DR PRIDE; Q9LK62; -.
DR ProteomicsDB; 245082; -.
DR EnsemblPlants; AT3G13100.1; AT3G13100.1; AT3G13100.
DR GeneID; 820498; -.
DR Gramene; AT3G13100.1; AT3G13100.1; AT3G13100.
DR KEGG; ath:AT3G13100; -.
DR Araport; AT3G13100; -.
DR TAIR; locus:2090049; AT3G13100.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_0_1; -.
DR InParanoid; Q9LK62; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9LK62; -.
DR BioCyc; ARA:AT3G13100-MON; -.
DR PRO; PR:Q9LK62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK62; baseline and differential.
DR Genevisible; Q9LK62; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
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 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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1493
FT /note="ABC transporter C family member 7"
FT /id="PRO_0000226078"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 343..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 915..935
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 959..979
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1038..1055
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1059..1081
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 309..590
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 624..847
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 922..1204
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1241..1475
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 863..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 659..666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1275..1282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 32
FT /note="L -> V (in Ref. 1; CAD45086)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="K -> N (in Ref. 1; CAD45086)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="S -> A (in Ref. 1; CAD45086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1493 AA; 167805 MW; F8A781A6A26FF64C CRC64;
MKQSYAMDNP IVFFLLESNY FPMFSIFFNL LLLLVMFGSC VYKKRLGWEN SDAFTNERFK
DMSLTYNKLV VICCETLSAL NSVLLLLSCF NLHKNGWDRS ELMILLDLLF TALSWGAISF
YIRSQFTYSH DQKFPILLRV WWVLYFMFSC YRLLVDIALY KKQELVSVHL LLSDVLAVSV
GLFLCYSCLQ KQGQGERINL LLEEPLLNGA ESSAATSVQL DKAEDDEVVT PFSNAGFLSH
VSFSWMSPLI VLGNEKIIDS EDVPQVDNSD RAEKLFWIFR SKLEWDDGER RITTYKLIKA
LFFSVWRDIL LSTLFAFVYT VSCYVAPYLM DTFVQYLNGQ RQYSNQGVVL VTTFFVAKLV
ECQARRNWYF RLQKAGIGMR SVLVSMIYEK GLTLPCYSKQ GHTSGEIINL MTVDAERISA
FSWYMHDPWI LVLQISLALL ILYRSLGLGS IAAFAATFLV MLGNIPLAKL EEKFQGNLME
SKDNRMKKTS EALLNMRILK LQGWEMKFLH KILDLRGIEA GWLKKFVYNS AAISSVLWAA
PSFVSATAFG ACMLLKIPLE SGKIIAALAT FRILQTPIYK LPDTISMIVQ TKVSLDRIAT
FLCLDDLQQD GMERLPSGSS KMDVEVSNGA FSWDDSSPIP TLKDIRFKIP HGMNIAICGT
VGSGKSSLLS SILGEVPKIS GNLKVCGRKA YIAQSPWIQS GKVEENILFG KPMQREWYQR
VLEACSLNKD LEVFPFRDQT VIGERGINLS GGQKQRIQIA RALYQDADIY LFDDPFSAVD
AHTGSHLFKE VLLGLLRNKT VIYVTHQLEF LPEADLILVM KDGRITQAGK YNEILESGTD
FMELVGAHTD ALAAVDSYEK GSASAQSTTS KESKVSNDEE KQEEDLPSPK GQLVQEEERE
KGKVGFTVYQ KYMKLAYGGA LVPIILVVQI LFQVLNIGSN YWMAWVTPVS KDVKPLVSGS
TLILVYVFLA TASSFCILVR AMLSAMTGFK IATELFNQMH FRIFRASMSF FDATPIGRIL
NRASTDQSAV DLRLPSQFSN LAIAAVNILG IIGVMGQVAW QVLIVFIPVI AACTWYRQYY
ISAARELARL SGISRSPLVQ HFSETLSGIT TIRSFDQEPR FRTDIMRLND CYSRLRFHAI
SAMEWLCFRL DLLSTVAFAL SLVILVSVPE GVINPSFAGL AVTYALNLNS LQATLIWTLC
DLENKMISVE RMLQYIDIPS EPSLVIESTR PEKSWPCRGE ITICNLQVRY GPHLPMVLRG
LTCTFRGGLK TGIVGRTGCG KSTLIQTLFR IVEPAAGEIR IDGINILTIG LHDLRSRLSI
IPQEPTMFEG TVRSNLDPLE EYADDQIWEA LDKCQLGDEI RKKELKLDSP VSENGQNWSV
GQRQLVCLGR VLLKRSKVLI LDEATASVDT ATDTLIQETL RQHFSGCTVI TIAHRISSVI
DSDMVLLLDQ GLIEEHDSPA RLLEDKSSSF SKLVAEYTAS SDSRFKRSSM KTN
