AB5C_ARATH
ID AB5C_ARATH Reviewed; 1514 AA.
AC Q7GB25; O65619; Q56ZX0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ABC transporter C family member 5;
DE Short=ABC transporter ABCC.5;
DE Short=AtABCC5;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 5;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 5;
DE AltName: Full=Multidrug resistance-associated protein 5;
GN Name=ABCC5; Synonyms=MRP5; OrderedLocusNames=At1g04120; ORFNames=F20D22.11;
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].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RA Weigmann N., Ansorge M., Meuller-Roeber B.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Ko J.-H., Kwon M.J., Yi H.C., Cho M.H.;
RT "Cloning and characterization of putative sulfonylurea receptor-like gene
RT from Arabidopsis thaliana.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 1438-1514.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
RX PubMed=11296221; DOI=10.1093/emboj/20.8.1875;
RA Gaedeke N., Klein M., Kolukisaoglu U.H., Forestier C., Mueller A.,
RA Ansorge M., Becker D., Mamnun Y., Kuchler K., Schulz B., Mueller-Roeber B.,
RA Martinoia E.;
RT "The Arabidopsis thaliana ABC transporter AtMRP5 controls root development
RT and stomata movement.";
RL EMBO J. 20:1875-1887(2001).
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 FUNCTION, AND 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.
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12943546; DOI=10.1046/j.1365-313x.2003.016012.x;
RA Klein M., Perfus-Barbeoch L., Frelet A., Gaedeke N., Reinhardt D.,
RA Mueller-Roeber B., Martinoia E., Forestier C.;
RT "The plant multidrug resistance ABC transporter AtMRP5 is involved in guard
RT cell hormonal signalling and water use.";
RL Plant J. 33:119-129(2003).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14684837; DOI=10.1104/pp.103.027045;
RA Lee E.K., Kwon M.J., Ko J.-H., Yi H.C., Hwang M.G., Chang S., Cho M.H.;
RT "Binding of sulfonylurea by AtMRP5, an Arabidopsis multidrug resistance-
RT related protein that functions in salt tolerance.";
RL Plant Physiol. 134:528-538(2004).
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).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19797057; DOI=10.1074/jbc.m109.030247;
RA Nagy R., Grob H., Weder B., Green P., Klein M., Frelet-Barrand A.,
RA Schjoerring J.K., Brearley C., Martinoia E.;
RT "The Arabidopsis ATP-binding cassette protein AtMRP5/AtABCC5 is a high
RT affinity inositol hexakisphosphate transporter involved in guard cell
RT signaling and phytate storage.";
RL J. Biol. Chem. 284:33614-33622(2009).
CC -!- FUNCTION: Pump for glutathione S-conjugates. Involved in regulation of
CC K(+) and Na(+) cell content. Mediates resistance to NaCl and Li(+),
CC confers sensitivity to sulfonylurea drugs such as glibenclamide
CC (inducer of stomatal opening), and required for stomatal opening
CC regulation by auxin, abscisic acid (ABA) and external Ca(2+).
CC Transports oestradiol-17-(beta-D-glucuronide) (E(2)17G). Involved in
CC the root auxin content regulation that controls the transition from
CC primary root elongation to lateral root formation. Plays a role in ABA-
CC mediated germination inhibition (PubMed:11296221, PubMed:11855639,
CC PubMed:12943546, PubMed:14684837). High-affinity inositol
CC hexakisphosphate transporter that plays a role in guard cell signaling
CC and phytic acid storage. Required for phytic acid accumulation in
CC developing seeds. Phytic acid is the primary storage form of phosphorus
CC in cereal grains and other plant seeds (PubMed:19797057).
CC {ECO:0000269|PubMed:11296221, ECO:0000269|PubMed:11855639,
CC ECO:0000269|PubMed:12943546, ECO:0000269|PubMed:14684837,
CC ECO:0000269|PubMed:19797057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- ACTIVITY REGULATION: (E(2)17G) transport activity in negatively
CC regulated by organic anions such as oestradiol-3-sulfate, luteolin-7-O-
CC diglucuronide-4'-O-glucuronide, glycocholate, vanadate and the
CC sulfonylurea glibenclamide, and, to a lower extent, by bafilomycin A1,
CC NH(4)Cl, GSH, GSSG and DNB-GS. {ECO:0000269|PubMed:11296221}.
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q7GB25-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in vascular tissues and
CC epidermis, including guard cells. {ECO:0000269|PubMed:11296221,
CC ECO:0000269|PubMed:12430019, ECO:0000269|PubMed:14684837}.
CC -!- DEVELOPMENTAL STAGE: In flowers, present in anthers central vascular
CC strand of the filament and in connecting tissues of the pollen sacs.
CC Also present at the silique attachment site of the pedicel.
CC {ECO:0000269|PubMed:11296221}.
CC -!- DISRUPTION PHENOTYPE: Increased water use efficiency (PubMed:12943546).
CC Low phytic acid levels in seed tissue (PubMed:19797057).
CC {ECO:0000269|PubMed:12943546, ECO:0000269|PubMed:19797057}.
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=AAC16754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y11250; CAA72120.1; -; mRNA.
DR EMBL; AF225908; AAG14965.1; -; mRNA.
DR EMBL; AC002411; AAC16754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27658.1; -; Genomic_DNA.
DR EMBL; AK220840; BAD94167.1; -; mRNA.
DR PIR; T00961; T00961.
DR PIR; T52080; T52080.
DR RefSeq; NP_171908.1; NM_100293.3. [Q7GB25-1]
DR AlphaFoldDB; Q7GB25; -.
DR SMR; Q7GB25; -.
DR BioGRID; 24512; 7.
DR IntAct; Q7GB25; 7.
DR STRING; 3702.AT1G04120.1; -.
DR TCDB; 3.A.1.208.21; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q7GB25; -.
DR PaxDb; Q7GB25; -.
DR PRIDE; Q7GB25; -.
DR ProteomicsDB; 245093; -. [Q7GB25-1]
DR EnsemblPlants; AT1G04120.1; AT1G04120.1; AT1G04120. [Q7GB25-1]
DR GeneID; 839277; -.
DR Gramene; AT1G04120.1; AT1G04120.1; AT1G04120. [Q7GB25-1]
DR KEGG; ath:AT1G04120; -.
DR Araport; AT1G04120; -.
DR TAIR; locus:2020235; AT1G04120.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q7GB25; -.
DR PhylomeDB; Q7GB25; -.
DR BioCyc; ARA:AT1G04120-MON; -.
DR PRO; PR:Q7GB25; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7GB25; baseline and differential.
DR Genevisible; Q7GB25; 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: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:0008281; F:sulfonylurea receptor activity; IDA:TAIR.
DR GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:TAIR.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1514
FT /note="ABC transporter C family member 5"
FT /id="PRO_0000226076"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1155..1175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1180..1200
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 307..588
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 622..845
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 949..1231
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1268..1502
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT COILED 899..927
FT /evidence="ECO:0000255"
FT BINDING 657..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1302..1309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1514 AA; 168574 MW; 35351F361D101783 CRC64;
MDFIEISLIF REHLPLLELC SVIINLLLFL VFLFAVSARQ ILVCVRRGRD RLSKDDTVSA
SNLSLEREVN HVSVGFGFNL SLLCCLYVLG VQVLVLVYDG VKVRREVSDW FVLCFPASQS
LAWFVLSFLV LHLKYKSSEK LPFLVRIWWF LAFSICLCTM YVDGRRLAIE GWSRCSSHVV
ANLAVTPALG FLCFLAWRGV SGIQVTRSSS DLQEPLLVEE EAACLKVTPY STAGLVSLIT
LSWLDPLLSA GSKRPLELKD IPLLAPRDRA KSSYKVLKSN WKRCKSENPS KPPSLARAIM
KSFWKEAACN AVFAGLNTLV SYVGPYLISY FVDYLGGKEI FPHEGYVLAG IFFTSKLIET
VTTRQWYMGV DILGMHVRSA LTAMVYRKGL KLSSIAKQNH TSGEIVNYMA VDVQRIGDYS
WYLHDIWMLP MQIVLALAIL YKSVGIAAVA TLVATIISIL VTIPLAKVQE DYQDKLMTAK
DERMRKTSEC LRNMRVLKLQ AWEDRYRVRL EEMREEEYGW LRKALYSQAF VTFIFWSSPI
FVAAVTFATS IFLGTQLTAG GVLSALATFR ILQEPLRNFP DLVSMMAQTK VSLDRISGFL
QEEELQEDAT VVIPRGLSNI AIEIKDGVFC WDPFSSRPTL SGIQMKVEKG MRVAVCGTVG
SGKSSFISCI LGEIPKISGE VRICGTTGYV SQSAWIQSGN IEENILFGSP MEKTKYKNVI
QACSLKKDIE LFSHGDQTII GERGINLSGG QKQRVQLARA LYQDADIYLL DDPFSALDAH
TGSDLFRDYI LSALAEKTVV FVTHQVEFLP AADLILVLKE GRIIQSGKYD DLLQAGTDFK
ALVSAHHEAI EAMDIPSPSS EDSDENPIRD SLVLHNPKSD VFENDIETLA KEVQEGGSAS
DLKAIKEKKK KAKRSRKKQL VQEEERVKGK VSMKVYLSYM GAAYKGALIP LIILAQAAFQ
FLQIASNWWM AWANPQTEGD ESKVDPTLLL IVYTALAFGS SVFIFVRAAL VATFGLAAAQ
KLFLNMLRSV FRAPMSFFDS TPAGRILNRV SIDQSVVDLD IPFRLGGFAS TTIQLCGIVA
VMTNVTWQVF LLVVPVAVAC FWMQKYYMAS SRELVRIVSI QKSPIIHLFG ESIAGAATIR
GFGQEKRFIK RNLYLLDCFV RPFFCSIAAI EWLCLRMELL STLVFAFCMV LLVSFPHGTI
DPSMAGLAVT YGLNLNGRLS RWILSFCKLE NKIISIERIY QYSQIVGEAP AIIEDFRPPS
SWPATGTIEL VDVKVRYAEN LPTVLHGVSC VFPGGKKIGI VGRTGSGKST LIQALFRLIE
PTAGKITIDN IDISQIGLHD LRSRLGIIPQ DPTLFEGTIR ANLDPLEEHS DDKIWEALDK
SQLGDVVRGK DLKLDSPVLE NGDNWSVGQR QLVSLGRALL KQAKILVLDE ATASVDTATD
NLIQKIIRTE FEDCTVCTIA HRIPTVIDSD LVLVLSDGRV AEFDTPARLL EDKSSMFLKL
VTEYSSRSTG IPEL
