AB13C_ARATH
ID AB13C_ARATH Reviewed; 1410 AA.
AC Q9SKX0; F4INF8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ABC transporter C family member 13;
DE Short=ABC transporter ABCC.13;
DE Short=AtABCC13;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 11;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 11;
DE AltName: Full=Multidrug resistance-associated protein 11;
GN Name=ABCC13; Synonyms=MRP11, MRP13; OrderedLocusNames=At2g07680;
GN ORFNames=T5E7.1;
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=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 [2]
RP GENE REANNOTATION.
RA Ducos E.;
RL Unpublished observations (MAY-2010).
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 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 [5]
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 [6]
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 [7]
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=AAD37023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEC06127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006225; AAD37023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06127.1; ALT_SEQ; Genomic_DNA.
DR PIR; F84487; F84487.
DR RefSeq; NP_178811.7; NM_126770.8.
DR AlphaFoldDB; Q9SKX0; -.
DR SMR; Q9SKX0; -.
DR STRING; 3702.AT2G07680.1; -.
DR PaxDb; Q9SKX0; -.
DR PRIDE; Q9SKX0; -.
DR ProteomicsDB; 245144; -.
DR GeneID; 815414; -.
DR KEGG; ath:AT2G07680; -.
DR Araport; AT2G07680; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q9SKX0; -.
DR PhylomeDB; Q9SKX0; -.
DR PRO; PR:Q9SKX0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKX0; baseline and differential.
DR Genevisible; Q9SKX0; 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: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; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; 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; 2.
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..1410
FT /note="ABC transporter C family member 13"
FT /id="PRO_0000226082"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 844..864
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 963..985
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 990..1009
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1087..1107
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 255..530
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 564..791
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 852..1139
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1174..1407
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 602..609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1208..1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1410 AA; 157870 MW; AB05CE5DF255A1AE CRC64;
MAITLTNFTF LYMDANLKRL GDIVLGFGAN VVTLLLILIL TITRRNGRCN RRKSYIEKCL
LYVTPALGAC LSCVDLVLLV RTNRRREVIL CFVPLSGFVM WIAVILSLKF ACCACHVFTS
QILCFWWIFR FLTDALHLNM IFTLQRVQEI CLIMLDIAFG ISINVLRIKQ AHPKIIPLED
PLIEDDDDQK RIVRRLFLEK NGSWWDLFTF GYIGSIMKHG SVKQLELENL LTLPPEMDPF
TCCENLLRCW QLQECNNYST PSLIWSIYGV YGWPYFRLGL LKVFNDCIGF AGPLLLNRLI
KSFLDTQYTF RLSKLKLKLR SSIMSVIYRK CLWVNTANRS GFSEGEIQTF MSVDADRIVN
LCNSLHDLWS LPLQIGIALY LLYTQVKFAF LSGLAITILL IPVNKWISVL IASATEKMMK
LKDERIRKTG ELLTNIRTLK MYGWDNWFAD WLKETRATEV THLATRKYLD AWCVFFWATT
PTLFSLCTFG LFALMGHQLD AATVFTCLAL FNSLISPLNS FPWVINGLID AFISTRRVSK
FLCCLEHSRD FSIDSGFTSE DLAVCVEDAS CTWSSNVEED YNLTIKQVSL RVPKGSFVAV
IGEVGSGKTS LLNSLLGEMR CVHGSILLNG SVAYVPQVPW LLSGTVRENI LFGKPFDSKR
YFETLSACAL DVDISLMVGG DMACIGDKGL NLSGGQRARF ALARAVYHGS DMYLLDDVLS
AVDSQVGCWI LQRALLGPLL NKKTRVMCTH NIQAISCADM IVVMDKGKVN WSGSVTDMPK
SISPTFSLTN EFDMSSPNHL TKRKETLSIK EDGVDEISEA AADIVKLEER KEGRVEMMVY
RNYAVFSGWF ITIVILVSAV LMQGSRNGND LWLSYWVDKT GKGVSHYSTS FYLMVLCIFC
IINSILTLVR AFSFAFGGLK AAVHVHNALI SKLINAPTQF FDQTPSGRIL NRFSSDLYTI
DDSLPFILNI LLANFVGLLG IIVVLSYVQV LFLLLLLPFW YIYSKLQVFY RSTSRELRRL
DSVSRSPIYA SFTETLDGSS TIRAFKSEEH FVGRFIEHLT LYQRTSYSEI IASLWLSLRL
QLLGSMIVLF VAVMAVLGSG GNFPISFGTP GLVGLALSYA APLVSLLGSL LTSFTETEKE
MVSVERVLQY MDVPQEEVSG PQSLSDKWPV HGLVEFHNVT MRYISTLPPA LTQISFTIQG
GMHVGVIGRT GAGKSSILNA LFRLTPVCSG EILVDGKNIS HLPIRELRSC LAVVPQSPFL
FQGSLRDNLD PLGLSEDWRI WEILDKCKVK AAVESVGGLD SYVKESGCSF SVGQRQLLCL
ARALLKSSKI LCLDECTANI DVHTASLLHN TISSECKGVT VITIAHRIST VVDLDSILIL
DRGILVEQGK PQHLLQDDSS TFSSFVRASQ
