AB10C_ARATH
ID AB10C_ARATH Reviewed; 1453 AA.
AC Q9LYS2; F4J869;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ABC transporter C family member 10;
DE Short=ABC transporter ABCC.10;
DE Short=AtABCC10;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 14;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 14;
DE AltName: Full=Multidrug resistance-associated protein 14;
GN Name=ABCC10; Synonyms=MRP10, MRP14; OrderedLocusNames=At3g59140;
GN ORFNames=F17J16.190;
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86942.1; Type=Erroneous gene model prediction; Evidence={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; AL163527; CAB86942.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79882.1; -; Genomic_DNA.
DR PIR; T47796; T47796.
DR RefSeq; NP_191473.2; NM_115776.4.
DR AlphaFoldDB; Q9LYS2; -.
DR SMR; Q9LYS2; -.
DR STRING; 3702.AT3G59140.1; -.
DR iPTMnet; Q9LYS2; -.
DR PaxDb; Q9LYS2; -.
DR PRIDE; Q9LYS2; -.
DR ProteomicsDB; 245128; -.
DR EnsemblPlants; AT3G59140.1; AT3G59140.1; AT3G59140.
DR GeneID; 825083; -.
DR Gramene; AT3G59140.1; AT3G59140.1; AT3G59140.
DR KEGG; ath:AT3G59140; -.
DR Araport; AT3G59140; -.
DR TAIR; locus:2077750; AT3G59140.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9LYS2; -.
DR OMA; IKGFIFT; -.
DR OrthoDB; 138195at2759; -.
DR BioCyc; ARA:AT3G59140-MON; -.
DR PRO; PR:Q9LYS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYS2; baseline and differential.
DR Genevisible; Q9LYS2; AT.
DR GO; GO:0005829; C:cytosol; 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: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 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1453
FT /note="ABC transporter C family member 10"
FT /id="PRO_0000226085"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 290..310
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 415..435
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 889..909
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 925..945
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 993..1013
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1020..1040
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 285..566
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 603..825
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 886..1170
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1207..1441
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 637..644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1241..1248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1453 AA; 162813 MW; CB663426426A9970 CRC64;
MIENYWTSFC GNHHTSSNCT VRFLQICFGI TLSFLTLCIC LFHKEPPKRI HQFFCLRLVS
ALFNGIIGSL DLVLGIWVLR ENHSKPLILW LVILIQGFTW LFINLIICVR GTRIRKSSLR
LLSIFSFFYG LVSSCLSVNN AVFGDELAVR TILDVLLLPG SVLLLLSAYK GYRFDESGES
SLYEPLNAGD SNGFSEKADF DNRVSQFAKA GLFSTLSFWW LNSLIKRGNV KDLEEEDIPE
LRKEERAETC YSLFEENLIE QKRRLGSSCQ PSILKVTVLC VWRELLTSGF FAFMKIVAVS
AGPLLLNAFI LVAEGNASFR YEGLVLAVLL FFSKMIESLS QRQWYFRCRI VGLRVRSLLT
AAINKKQLRL NNSSRLIHSG SEIMNYATVD AYRIGEFPYW FHQLWTTSFQ LLIALGILFH
SVGVATFSAL AVIILTVLCN APIAKLQNKF QSELMTSQDE RLKACNESLV NMKVLKLYAW
ESHFKKVIEK LRNIELKSLK AVQMRKAYNA VLFWSSPVFV SAATFATCYF LDIPLRASNV
FTFVATLRLV QDPVRMIPDV IGVTIQAKVA FSRIATFLEA PELQGGERRR KQRSEGNQNA
IIIKSASFSW EEKGSTKPNL RNVSLEVKFG EKVAVCGEVG SGKSTLLAAI LGETPCVSGT
IDFYGTIAYV SQTAWIQTGT IRDNILFGGV MDEHRYRETI QKSSLDKDLE LLPDGDQTEI
GERGVNLSGG QKQRIQLARA LYQDADIYLL DDPFSAVDAH TASSLFQEYV MDALAGKAVL
LVTHQVDFLP AFDSVLLMSD GEITEADTYQ ELLARSRDFQ DLVNAHRETA GSERVVAVEN
PTKPVKEINR VISSQSKVLK PSRLIKQEER EKGDTGLRPY IQYMNQNKGY IFFFIASLAQ
VTFAVGQILQ NSWMAANVDN PQVSTLKLIL VYLLIGLCSV LCLMVRSVCV VIMCMKSSAS
LFSQLLNSLF RAPMSFYDST PLGRILSRVS SDLSIVDLDV PFGLIFVVAS SVNTGCSLGV
LAIVTWQVLF VSVPMVYLAF RLQKYYFQTA KELMRINGTT RSYVANHLAE SVAGAITIRA
FDEEERFFKK SLTLIDTNAS PFFHSFAANE WLIQRLETVS AIVLASTAFC MILLPTGTFS
SGFIGMALSY GLSLNMGLVY SVQNQCYLAN WIISVERLNQ YTHLTPEAPE VIEETRPPVN
WPVTGRVEIS DLQIRYRRES PLVLKGISCT FEGGHKIGIV GRTGSGKTTL ISALFRLVEP
VGGKIVVDGV DISKIGVHDL RSRFGIIPQD PTLFNGTVRF NLDPLCQHSD AEIWEVLGKC
QLKEVVQEKE NGLDSLVVED GSNWSMGQRQ LFCLGRAVLR RSRVLVLDEA TASIDNATDL
ILQKTIRREF ADCTVITVAH RIPTVMDCTM VLSISDGRIV EYDEPMKLMK DENSLFGKLV
KEYWSHYNSA DSR
