AB4C_ARATH
ID AB4C_ARATH Reviewed; 1516 AA.
AC Q7DM58; O24525; Q0WVT4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ABC transporter C family member 4;
DE Short=ABC transporter ABCC.4;
DE Short=AtABCC4;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 4;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 4;
DE AltName: Full=Multidrug resistance-associated protein 4;
GN Name=ABCC4; Synonyms=EST3, MRP4; OrderedLocusNames=At2g47800;
GN ORFNames=F17A22.19;
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 [GENOMIC DNA], AND INDUCTION.
RX PubMed=9671034; DOI=10.1007/s004380050779;
RA Sanchez-Fernandez R., Ardiles-Diaz W., Van Montagu M., Inze D., May M.J.;
RT "Cloning and expression analyses of the AtMRP4, a novel MRP-like gene from
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 258:655-662(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Sanchez-Fernandez R., Rea P.A.;
RT "AtMRP4 gene of Arabidopsis encodes a glutathione S-conjugate pump.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1272-1516, AND INDUCTION.
RX PubMed=9271206; DOI=10.1016/s0014-5793(97)00702-3;
RA Tommasini R., Vogt E., Schmid J., Fromentau M., Amrhein N., Martinoia E.;
RT "Differential expression of genes coding for ABC transporters after
RT treatment of Arabidopsis thaliana with xenobiotics.";
RL FEBS Lett. 411:206-210(1997).
RN [7]
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 [8]
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 [9]
RP 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 [10]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, FUNCTION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15225287; DOI=10.1111/j.1365-313x.2004.02125.x;
RA Klein M., Geisler M., Suh S.J., Kolukisaoglu U.H., Azevedo L., Plaza S.,
RA Curtis M.D., Richter A., Weder B., Schulz B., Martinoia E.;
RT "Disruption of AtMRP4, a guard cell plasma membrane ABCC-type ABC
RT transporter, leads to deregulation of stomatal opening and increased
RT drought susceptibility.";
RL Plant J. 39:219-236(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [12]
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).
CC -!- FUNCTION: Involved in the regulation of stomatal aperture. May function
CC as a high-capacity pump for folates. {ECO:0000269|PubMed:15225287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- ACTIVITY REGULATION: Inhibited by methotrexate.
CC {ECO:0000269|PubMed:15225287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15225287};
CC Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:17151019}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression in the guard cells.
CC {ECO:0000269|PubMed:12430019, ECO:0000269|PubMed:15225287}.
CC -!- INDUCTION: By salicylic acid (SA), menadione and, to a lower extent, by
CC 1-chloro-2,4-dinitrobenzene (CDNB), benoxacor, cloquintocet,
CC fenchlorazol and fluorazol. {ECO:0000269|PubMed:12430019,
CC ECO:0000269|PubMed:9271206, ECO:0000269|PubMed:9671034}.
CC -!- DISRUPTION PHENOTYPE: Plants have larger stomatal aperture and
CC increased drought susceptibility, but are not affected by the ABA
CC signal transduction pathway. {ECO:0000269|PubMed:15225287}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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; AJ002584; CAA05625.1; -; Genomic_DNA.
DR EMBL; AF243509; AAF68441.1; -; mRNA.
DR EMBL; AC005309; AAC63634.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10889.1; -; Genomic_DNA.
DR EMBL; AK226656; BAE98764.1; -; mRNA.
DR EMBL; U96399; AAC49797.1; -; mRNA.
DR PIR; F84919; F84919.
DR RefSeq; NP_182301.1; NM_130347.5.
DR AlphaFoldDB; Q7DM58; -.
DR SMR; Q7DM58; -.
DR BioGRID; 4727; 1.
DR IntAct; Q7DM58; 1.
DR STRING; 3702.AT2G47800.1; -.
DR iPTMnet; Q7DM58; -.
DR PaxDb; Q7DM58; -.
DR PRIDE; Q7DM58; -.
DR ProteomicsDB; 244376; -.
DR EnsemblPlants; AT2G47800.1; AT2G47800.1; AT2G47800.
DR GeneID; 819392; -.
DR Gramene; AT2G47800.1; AT2G47800.1; AT2G47800.
DR KEGG; ath:AT2G47800; -.
DR Araport; AT2G47800; -.
DR TAIR; locus:2043268; AT2G47800.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q7DM58; -.
DR OMA; ICMATPV; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q7DM58; -.
DR BioCyc; ARA:AT2G47800-MON; -.
DR PRO; PR:Q7DM58; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7DM58; baseline and differential.
DR Genevisible; Q7DM58; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C: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:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP: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; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1516
FT /note="ABC transporter C family member 4"
FT /id="PRO_0000226075"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1186..1206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1211..1231
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 326..607
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 641..864
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 957..1237
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1274..1508
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 879..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 676..683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1308..1315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 1234
FT /note="F -> L (in Ref. 5; BAE98764)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295
FT /note="T -> I (in Ref. 5; BAE98764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1516 AA; 169080 MW; 047751628C58431E CRC64;
MWLLSSSPWL SELSCSYSAV VEHTSSVPVP IQWLRFVLLS PCPQRALFSA VDFIFLLCFA
LHKLFSSPSS SSEINGHAEI RKPLIGIRGR TPTRTTAWFK TTVAVTVLLS FCSVVLCVLA
FTGKRRTQRP WNLIDPLFWL IHAVTHLVIA VLVLHQKRFA ALNHPLSLRI YWISSFVLTS
LFAVTGIFHF LSDAATSLRA EDVASFFSFP LTAFLLIASV RGITGLVTAE TNSPTKPSDA
VSVEKSDNVS LYASASVFSK TFWLWMNPLL SKGYKSPLTL EQVPTLSPEH KAERLALLFE
SSWPKPSENS SHPIRTTLLR CFWKEILFTA ILAIVRLGVM YVGPVLIQSF VDFTSGKRSS
PWQGYYLVLI LLVAKFVEVL TTHQFNFDSQ KLGMLIRSTL ITALYKKGLK LTGSARQNHG
VGQIVNYMAV DAQQLSDMML QLHAIWLMPL QVTVALVLLY GSLGASVITA VIGLTGVFVF
ILLGTQRNNG YQFSLMGNRD SRMKATNEML NYMRVIKFQA WENHFNKRIL KFRDMEFGWL
SKFLYSIAGN IIVLWSTPVL ISALTFATAL ALGVKLDAGT VFTTTTIFKI LQEPIRTFPQ
SMISLSQAMI SLGRLDSYMM SKELSEDAVE RALGCDGNTA VEVRDGSFSW DDEDNEPALS
DINFKVKKGE LTAIVGTVGS GKSSLLASVL GEMHRISGQV RVCGSTGYVA QTSWIENGTV
QDNILFGLPM VREKYNKVLN VCSLEKDLQM MEFGDKTEIG ERGINLSGGQ KQRIQLARAV
YQECDVYLLD DVFSAVDAHT GSDIFKKCVR GALKGKTVLL VTHQVDFLHN VDCILVMRDG
KIVESGKYDE LVSSGLDFGE LVAAHETSME LVEAGADSAA VATSPRTPTS PHASSPRTSM
ESPHLSDLND EHIKSFLGSH IVEDGSKLIK EEERETGQVS LGVYKQYCTE AYGWWGIVLV
LFFSLTWQGS LMASDYWLAY ETSAKNAISF DASVFILGYV IIALVSIVLV SIRSYYVTHL
GLKTAQIFFR QILNSILHAP MSFFDTTPSG RILSRASTDQ TNVDILIPFM LGLVVSMYTT
LLSIFIVTCQ YAWPTAFFVI PLGWLNIWYR NYYLASSREL TRMDSITKAP IIHHFSESIA
GVMTIRSFRK QELFRQENVK RVNDNLRMDF HNNGSNEWLG FRLELVGSWV LCISALFMVL
LPSNVIRPEN VGLSLSYGLS LNSVLFFAIY MSCFVENKMV SVERIKQFTD IPSESEWERK
ETLPPSNWPF HGNVHLEDLK VRYRPNTPLV LKGITLDIKG GEKVGVVGRT GSGKSTLIQV
LFRLVEPSGG KIIIDGIDIS TLGLHDLRSR FGIIPQEPVL FEGTVRSNID PTEQYSDEEI
WKSLERCQLK DVVATKPEKL DSLVVDNGEN WSVGQRQLLC LGRVMLKRSR LLFLDEATAS
VDSQTDAVIQ KIIREDFASC TIISIAHRIP TVMDGDRVLV IDAGKAKEFD SPARLLERPS
LFAALVQEYA LRSAGI
