AB14C_ARATH
ID AB14C_ARATH Reviewed; 1539 AA.
AC Q9LZJ5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ABC transporter C family member 14;
DE Short=ABC transporter ABCC.14;
DE Short=AtABCC14;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 10;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 10;
DE AltName: Full=Multidrug resistance-associated protein 10;
GN Name=ABCC14; Synonyms=MRP10, MRP14; OrderedLocusNames=At3g62700;
GN ORFNames=F26K9.130;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [5]
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 [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-894, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(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 -!- 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; AL162651; CAB83120.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80381.1; -; Genomic_DNA.
DR PIR; T48059; T48059.
DR RefSeq; NP_191829.1; NM_116135.3.
DR AlphaFoldDB; Q9LZJ5; -.
DR SMR; Q9LZJ5; -.
DR BioGRID; 10758; 2.
DR STRING; 3702.AT3G62700.1; -.
DR iPTMnet; Q9LZJ5; -.
DR SwissPalm; Q9LZJ5; -.
DR PaxDb; Q9LZJ5; -.
DR PRIDE; Q9LZJ5; -.
DR ProteomicsDB; 244529; -.
DR EnsemblPlants; AT3G62700.1; AT3G62700.1; AT3G62700.
DR GeneID; 825444; -.
DR Gramene; AT3G62700.1; AT3G62700.1; AT3G62700.
DR KEGG; ath:AT3G62700; -.
DR Araport; AT3G62700; -.
DR TAIR; locus:2081755; AT3G62700.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9LZJ5; -.
DR OMA; DFFANIW; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9LZJ5; -.
DR BioCyc; ARA:AT3G62700-MON; -.
DR PRO; PR:Q9LZJ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZJ5; baseline and differential.
DR Genevisible; Q9LZJ5; 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: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: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..1539
FT /note="ABC transporter C family member 14"
FT /id="PRO_0000226081"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 131..151
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 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1015..1035
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1088..1108
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1112..1132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1209..1229
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 324..605
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 639..862
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 980..1260
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1297..1531
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 896..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 674..681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1331..1338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1539 AA; 172137 MW; BF953EC320330648 CRC64;
MRWLSSTWLS DLSCSSSSVI EPSSSLPAPI QWLRFILLSP CPQRLLSSTV DVLFLLILFF
FAIQKLCSSS SSRTNGEADI TKPLLGRRTR TRTTGLFKTT VVVTIVLSFC SLVLCVSAFF
TTRTKLKLVD TLFWLIHAVT NVVIAVLVLH LKRFASPSHP LTLRIYWVFN FVVTTLFTVS
GILHLLSDDP AAASLRADDV ASFISFPLTA VLLLVSIKGS TGVVVTTSNV TAPAKSNDVV
VEKSENVSLY ASASFISKTF WLWMNPLLRK GYKSPLNLDQ VPTLSPEHRA EKLATLFESK
WPKPQENSRN PVRTTLIRCF WKEIAFTAVL AIIRLSVIYV GPVLIQSFVD FTSGKRSSPS
QGYYLVLILL IAKFVEVLST HQFNFNSQKL GMLIRSTLIT ALYKKGLKLT GSARQNHGVG
QIVNYMAVDA QQLSDMMLQL HAIWLMPLQV AAAIVLLYNT LGPSVVTTVI GLTGIFVFIL
LGTKRNNRYQ FSLMMNRDSR MKATNEMLNY MRVIKFQAWE DHFNERILKF REMEFGWLSK
FLYSIAGNII VLWSTPVLIS ALTFTTAVFL GVKLDAGTVF TTTTIFKILQ EPIRTFPQSM
ISLSQAMISL GRLDAYMMSR ELSEETVERS QGCDGNVAVE IKDGSFSWDD EDDEPAIENI
NFEVKKGELA AIVGTVGSGK SSLLASVLGE MHKLSGKVRV CGTTAYVAQT SWIQNGTVQD
NILFGLPMNR SKYNEVLKVC CLEKDMQIME FGDQTEIGER GINLSGGQKQ RIQLARAVYQ
ESDVYLLDDV FSAVDAHTGS DIFKKCVRGA LKGKTILLVT HQVDFLHNVD RILVMRDGMI
VQSGKYDELV SSGLDFGELV AAHETSMELV EAGSASATAA NVPMASPITQ RSISIESPRQ
PKSPKVHRTT SMESPRVLRT TSMESPRLSE LNDESIKSFL GSNIPEDGSR LIKEEEREVG
QVSFQVYKLY STEAYGWWGM ILVVFFSVAW QASLMASDYW LAYETSAKNE VSFDATVFIR
VYVIIAAVSI VLVCLRAFYV THLGLKTAQI FFKQILNSLV HAPMSFFDTT PSGRILSRAS
TDQTNVDIFI PFMIGLVATM YTTLLSIFIV TCQYAWPTVF FIIPLGWLNI WYRGYYLASS
RELTRLDSIT KAPVIHHFSE SIAGVMTIRA FKKQPMFRQE NVKRVNANLR MDFHNNGSNE
WLGFRLELIG SWVLCISALF MVMLPSNIIK PENVGLSLSY GLSLNGVLFW AIYLSCFIEN
KMVSVERIKQ FTDIPAEAKW EIKESRPPPN WPYKGNIRLE DVKVRYRPNT PLVLKGLTID
IKGGEKIGVV GRTGSGKSTL IQVLFRLVEP SGGKIIIDGI DICTLGLHDL RSRFGIIPQE
PVLFEGTVRS NIDPTEKYSD EEIWKSLERC QLKDVVASKP EKLDSLVADN GENWSVGQRQ
LLCLGRVMLK RSRILFLDEA TASVDSQTDA MIQKIIREDF SDCTIISIAH RIPTVMDCDR
VLVIDAGKAK EYDSPVRLLE RQSLFAALVQ EYALRSAGI
