AB12C_ARATH
ID AB12C_ARATH Reviewed; 1495 AA.
AC Q9C8H0; F4I4U8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ABC transporter C family member 12;
DE Short=ABC transporter ABCC.12;
DE Short=AtABCC12;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 13;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 13;
DE AltName: Full=Multidrug resistance-associated protein 13;
GN Name=ABCC12; Synonyms=MRP12, MRP13; OrderedLocusNames=At1g30410;
GN ORFNames=T4K22.13;
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=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 [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 ---------------------------------------------------------------------------
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; AC025295; AAG51100.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60872.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60873.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60875.1; -; Genomic_DNA.
DR PIR; E86428; E86428.
DR RefSeq; NP_001323123.1; NM_001332893.1.
DR RefSeq; NP_001323124.1; NM_001332895.1.
DR RefSeq; NP_001323126.1; NM_001332897.1.
DR AlphaFoldDB; Q9C8H0; -.
DR SMR; Q9C8H0; -.
DR STRING; 3702.AT1G30410.1; -.
DR TCDB; 3.A.1.208.43; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9C8H0; -.
DR PRIDE; Q9C8H0; -.
DR ProteomicsDB; 245098; -.
DR EnsemblPlants; AT1G30410.2; AT1G30410.2; AT1G30410.
DR EnsemblPlants; AT1G30410.4; AT1G30410.4; AT1G30410.
DR EnsemblPlants; AT1G30410.6; AT1G30410.6; AT1G30410.
DR GeneID; 839921; -.
DR Gramene; AT1G30410.2; AT1G30410.2; AT1G30410.
DR Gramene; AT1G30410.4; AT1G30410.4; AT1G30410.
DR Gramene; AT1G30410.6; AT1G30410.6; AT1G30410.
DR KEGG; ath:AT1G30410; -.
DR Araport; AT1G30410; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9C8H0; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9C8H0; -.
DR BioCyc; ARA:AT1G30410-MON; -.
DR PRO; PR:Q9C8H0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8H0; baseline and differential.
DR Genevisible; Q9C8H0; 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 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; 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..1495
FT /note="ABC transporter C family member 12"
FT /id="PRO_0000226084"
FT TRANSMEM 38..58
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 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 907..927
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1140..1160
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 303..583
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 615..839
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 914..1198
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1235..1469
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 650..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1269..1276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1495 AA; 167956 MW; D29EF05C6D6BDE13 CRC64;
MGFEALNWYC KPVADGFWEK AVDGAFGAYT PCAIDSLVML VSHFVLLGLC FYRIWIIFHN
TKAQIYVLRK KYYNCVLGLL ACYCVVEPVL RLVMGISLFD MDEETDFPPF EVASLMVEAF
AWFSMLVLIG LETKQYVKEF RWYVRFGVLY VLVADAVLLD LVLPLKNSIN RTALYLFISS
RCSQALFGIL LLIYIPELDP YPGYHIVNNE PLDNVEYDAL RGGEHICPER HASIFSRIYF
GWITPLMQLG YRKPITEKDV WQLDKWDQTE TLIKRFQRCW TEESRRPKPW LLRALNNSLG
GRFWLAGIFK IGNDLSQFVG PVILSHLLRS MQEGDPAWVG YVYAFIIFVG VTLGVLCEAQ
YFQNVWRVGF RLRSTLVAAI FHKSLRLTHE ARKNFASGKV TNMITTDANA LQQISQQLHG
LWSAPFRIIV SMILLYQQLG VASLFGSLIL FLLIPLQTLI ISKMRKLTKE GLQWTDKRVG
ITNEILSSMD TVKCYAWEKS FESRIQGIRN EELSWFRKAQ LLSAFNSFIL NSIPVVVTVV
SFGVFVLLGG DLTPARAFTS LSLFAVLRFP LNMLPNLLSQ VVNANVSLQR IEELLLSEER
ILAQNPPLQP GTPAISIKNG YFSWDSKTTK PTLSDINLEI PVGTLVAIVG GTGEGKTSLI
SAMLGELSHA ETTSVVIRGS VAYVPQVSWI FNATVRENIL FGSDFESERY WRAIDATALQ
HDLDLLPGRD LTEIGERGVN ISGGQKQRVS MARAVYSNSD VYIFDDPLSA LDAHVAHQVF
DSCMKDELRG KTRVLVTNQL HFLPLMDKII LVSEGMIKEE GTFVELSKSG ILFKKLMENA
GKMDATQEVN TNDENILKLG PTVTVDVSER NLGSTKQGKR RRSVLIKQEE RETGIISWNV
LMRYKEAVGG LWVVMILLAC YLATEVLRVS SSTWLSIWTD QSTSKNYSPG FYIVVYALLG
FGQVAVTFTN SFWLITSSLH AARRLHDAML SSILRAPMLF FHTNPTGRVI NRFSKDIGDI
DRNVANLMNM FMNQLWQLLS TFALIGTVST ISLWAIMPLL ILFYAAYLYY QSTSREVRRL
DSVTRSPIYA QFGEALNGLS SIRAYKAYDR MAKINGKSMD NNIRFTLANT SSNRWLTIRL
ETLGGVMIWL TATFAVLQNG NTNNQAGFAS TMGLLLSYTL NITSLLSGVL RQASRAENSL
NSVERVGNYI DLPSEATDII ENNRPVCGWP SGGSIKFEDV HLRYRPGLPP VLHGLTFFVS
PSEKVGVVGR TGAGKSSMLN ALFRIVEVEK GRIMIDDCDV AKFGLTDVRR VLSIIPQSPV
LFSGTVRFNI DPFSEHNDAG LWEALHRAHI KDVISRNPFG LDAEVCEGGE NFSVGQRQLL
SLARALLRRS KILVLDEATA SVDVRTDSLI QRTIREEFKS CTMLVIAHRL NTIIDCDKIL
VLSSGQVLEY DSPQELLSRD TSAFFRMVHS TGPANAQYLS NLVFERRENG MSVGG