AB3C_ARATH
ID AB3C_ARATH Reviewed; 1514 AA.
AC Q9LK64; O24510; Q3EB73;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ABC transporter C family member 3;
DE Short=ABC transporter ABCC.3;
DE Short=AtABCC3;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 3;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 3;
DE AltName: Full=Multidrug resistance-associated protein 3;
GN Name=ABCC3; Synonyms=EST2, MRP3; OrderedLocusNames=At3g13080;
GN ORFNames=MJG19.3;
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] (ISOFORM 1), AND INDUCTION.
RC STRAIN=cv. Columbia;
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 [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 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 [5]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=9681016; DOI=10.1046/j.1365-313x.1998.00076.x;
RA Tommasini R., Vogt E., Fromenteau M., Hoertensteiner S., Matile P.,
RA Amrhein N., Martinoia E.;
RT "An ABC-transporter of Arabidopsis thaliana has both glutathione-conjugate
RT and chlorophyll catabolite transport activity.";
RL Plant J. 13:773-780(1998).
RN [6]
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 [7]
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 [8]
RP TISSUE SPECIFICITY.
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 [9]
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: Pump for glutathione S-conjugates. Mediates the transport of
CC glutathione conjugates such as chlorodinitrobenzene-GS (DNB-GS), and of
CC chlorophyll catabolites such as Bn-NCC-1. Transports also heavy metals
CC such as cadmium (Cd). {ECO:0000269|PubMed:9681016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- ACTIVITY REGULATION: Glutathione-conjugate transport is inhibited by
CC decyl-glutathione and, to a lower extent, by GS-GS, but not by GSH. All
CC transports are inhibited by vanadate. {ECO:0000269|PubMed:9681016}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for DNB-GS (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9681016};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LK64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LK64-2; Sequence=VSP_018099;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12430019,
CC ECO:0000269|PubMed:9681016}.
CC -!- INDUCTION: By 1-chloro-2,4-dinitrobenzene (CDNB), primisulfuron (PS),
CC aminotriazole, benoxacor, oxabetrinil and IRL 1803, and, to a lower
CC extent, by cloquintocet, fenchlorazol and fluorazol.
CC {ECO:0000269|PubMed:9271206, ECO:0000269|PubMed:9671034}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49791.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U92650; AAC49791.1; ALT_FRAME; mRNA.
DR EMBL; AP000375; BAB01399.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75291.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75292.1; -; Genomic_DNA.
DR PIR; T52081; T52081.
DR RefSeq; NP_187915.1; NM_112147.3. [Q9LK64-1]
DR RefSeq; NP_850575.1; NM_180244.1. [Q9LK64-2]
DR AlphaFoldDB; Q9LK64; -.
DR SMR; Q9LK64; -.
DR STRING; 3702.AT3G13080.1; -.
DR TCDB; 3.A.1.208.17; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9LK64; -.
DR PRIDE; Q9LK64; -.
DR ProteomicsDB; 244605; -. [Q9LK64-1]
DR EnsemblPlants; AT3G13080.1; AT3G13080.1; AT3G13080. [Q9LK64-1]
DR EnsemblPlants; AT3G13080.2; AT3G13080.2; AT3G13080. [Q9LK64-2]
DR GeneID; 820496; -.
DR Gramene; AT3G13080.1; AT3G13080.1; AT3G13080. [Q9LK64-1]
DR Gramene; AT3G13080.2; AT3G13080.2; AT3G13080. [Q9LK64-2]
DR KEGG; ath:AT3G13080; -.
DR Araport; AT3G13080; -.
DR TAIR; locus:2090029; AT3G13080.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9LK64; -.
DR OMA; MDLMTFL; -.
DR PhylomeDB; Q9LK64; -.
DR BioCyc; ARA:AT3G13080-MON; -.
DR PRO; PR:Q9LK64; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK64; baseline and differential.
DR Genevisible; Q9LK64; AT.
DR GO; GO:0048046; C:apoplast; 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: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:0015431; F:ABC-type glutathione S-conjugate transporter activity; IDA: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; IDA:TAIR.
DR GO; GO:0010290; F:chlorophyll catabolite transmembrane transporter activity; IDA: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 Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1514
FT /note="ABC transporter C family member 3"
FT /id="PRO_0000226074"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 364..386
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 940..960
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1077..1097
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1181..1201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1205..1225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 325..606
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 640..863
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 950..1232
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1271..1503
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 675..682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1303..1310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT VAR_SEQ 1347..1372
FT /note="SIIPQDPTMFEGTMRSNLDPLEEYTD -> N (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018099"
SQ SEQUENCE 1514 AA; 168971 MW; 455575FCD3DA5115 CRC64;
MDFLGSTTGS GTLAMLFSFS ESILPLDSRS FLLKPLFLRW LSGFLHSVLL LVLFFSWVRK
KIRGDSGVTE SLKDRRDFGF KSALFCSLAL SLLNLVLMSL SGFYWYESGW LDNEQLVSSL
GFLLGMVSWG VLSICLHRCR DCEHKKAPFL LRLWLVFYLV VSCYSLVVDF VMYERRETVP
VHLLVFDIVA FIAAVFLGYV AVLKKDRSNS NGVLEEPLLN GGDSRVGGDD SVELNKTNGS
GEATPYSRAG ILSLLTFSWM SPLIDIGNKK TLDLEDVPQL HDTDSVVGLA PKFRSMLESP
DGGERSGVTT FKLIKALYFT AQWEILVTAF FAFIYTVASY VGPALIDTFV QYLNGRRQYN
HEGYVLVITF FAAKIVECLS QRHWFFRLQK VGIRMRSALV AMIYEKGLTL SCQSKQGRTS
GEIINFMTVD AERIGNFSWY MHDPWMVLLQ VGLALWILYR NLGLASIAAL VATIIVMLIN
FPFGRMQERF QEKLMEAKDS RMKSTSEILR NMRILKLQGW EMKFLSKIFD LRKSEEGWLK
KYVYNSAVIS FVFWGAPTLV SVSTFGACIL LGIPLESGKI LSALATFRIL QEPIYNLPDT
ISMIVQTKVS LDRLASYLCL DNLQPDIVER LPKGSSDVAV EVINSTLSWD VSSSNPTLKD
INFKVFPGMK VAVCGTVGSG KSSLLSSLLG EVPKVSGSLK VCGTKAYVAQ SPWIQSGKIE
DNILFGKPME RERYDKVLEA CSLSKDLEIL SFGDQTVIGE RGINLSGGQK QRIQIARALY
QDADIYLFDD PFSAVDAHTG SHLFKEVLLG LLCSKSVIYV THQVEFLPAA DLILVMKDGR
ISQAGKYNDI LNSGTDFMEL IGAHQEALAV VDSVDANSVS EKSALGQENV IVKDAIAVDE
KLESQDLKND KLESVEPQRQ IIQEEEREKG SVALDVYWKY ITLAYGGALV PFILLGQVLF
QLLQIGSNYW MAWATPVSED VQAPVKLSTL MIVYVALAFG SSLCILLRAT LLVTAGYKTA
TELFHKMHHC IFRSPMSFFD STPSGRIMSR ASTDQSAVDL ELPYQFGSVA ITVIQLIGII
GVMSQVSWLV FLVFIPVVAA SIWYQRYYIA AARELSRLVG VCKAPLIQHF SETISGATTI
RSFSQEFRFR SDNMRLSDGY SRPKFYTAGA MEWLCFRLDM LSSLTFVFSL VFLVSIPTGV
IDPSLAGLAV TYGLSLNTLQ AWLIWTLCNL ENKIISVERI LQYASVPSEP PLVIESNRPE
QSWPSRGEVE IRDLQVRYAP HMPLVLRGIT CTFKGGLRTG IVGRTGSGKS TLIQTLFRIV
EPSAGEIRID GVNILTIGLH DLRLRLSIIP QDPTMFEGTM RSNLDPLEEY TDDQIWEALD
KCQLGDEVRK KEQKLDSSVS ENGDNWSMGQ RQLVCLGRVL LKRSKILVLD EATASVDTAT
DNLIQKTLRE HFSDCTVITI AHRISSVIDS DMVLLLSNGI IEEYDTPVRL LEDKSSSFSK
LVAEYTSRSS SSFD
