AB15C_ARATH
ID AB15C_ARATH Reviewed; 1053 AA.
AC Q7FB56; F4JD20;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative ABC transporter C family member 15;
DE Short=ABC transporter ABCC.15;
DE Short=AtABCC15;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 15;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 15;
DE AltName: Full=Putative multidrug resistance-associated protein 15;
GN Name=ABCC15; Synonyms=MRP15; OrderedLocusNames=At3g60970;
GN ORFNames=T27I15.60;
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 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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks some conserved transmembrane domains, which are one of
CC the features of the ABC conjugate transporter subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB94133.1; 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; AL358732; CAB94133.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80133.1; -; Genomic_DNA.
DR PIR; T50518; T50518.
DR RefSeq; NP_191656.2; NM_115961.3.
DR AlphaFoldDB; Q7FB56; -.
DR SMR; Q7FB56; -.
DR STRING; 3702.AT3G60970.1; -.
DR PaxDb; Q7FB56; -.
DR PRIDE; Q7FB56; -.
DR ProteomicsDB; 243297; -.
DR EnsemblPlants; AT3G60970.1; AT3G60970.1; AT3G60970.
DR GeneID; 825269; -.
DR Gramene; AT3G60970.1; AT3G60970.1; AT3G60970.
DR KEGG; ath:AT3G60970; -.
DR Araport; AT3G60970; -.
DR TAIR; locus:2100987; AT3G60970.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_0_1; -.
DR InParanoid; Q7FB56; -.
DR OMA; RITCFTD; -.
DR OrthoDB; 138195at2759; -.
DR BioCyc; ARA:AT3G60970-MON; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7FB56; baseline and differential.
DR Genevisible; Q7FB56; 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; 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 5: Uncertain;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1053
FT /note="Putative ABC transporter C family member 15"
FT /id="PRO_0000226086"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 481..503
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1..180
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 214..437
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 483..765
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 804..1036
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 836..843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1053 AA; 117251 MW; 4E88EB0FA9F51CA9 CRC64;
MSVDVQRITD FIWYVNSIWM LPIQIFSAIY ILQKHLGLGA LAALVTTLMV MACNYPLTRL
QRNYQSDIMN AKDDRMKATS EILKNMKILK LQAWDNQFLN KVKTLRKKEY DCLWKSLRLQ
DFTTFILWGA PSLISVVTFV TCMLMGVKLT AGAVLSALAT FQMLQSPIFG LPDLLSALVQ
SKVSADRIAS YLQQSETQKD AVEYCSNDHT EFSVEIENGA FSWEPESSRP TLDDIELKVK
SGMKVAICGA VGSGKSSLPS SILGEIQKLK GTVRVSGKQA YVPQSPWILS GTIRDNILFG
SIYESEKYER TVKACALIKD FELFSNGDLT EIGERGINMS GGQKQRIQIA RAVYQNADIY
LLDDPFSAVD AHTGRELFED CLMGILKDKT VLYVTHQVEF LPAADLILVM QNGRVMQAGK
FEELLKQNIG FEVLTQCDSE HNISTENKKK EAKLVQDEET EKGVIGKEVY LTYLTTVKGG
LLVPFIILAQ SCFQMLQIAS NYWMAWTAPP TAESIPKLGM GRILLVYALL AAGSSLCVLA
RTILVAIGGL STAETFFSRM LCSIFRAPMS YFDSTPTGRI LNRASTDQSV LDLEMAVKLG
WCAFSIIQIV GTIFVMSQVA WQVCVIFIPV AVACVFYQRY YTPTERELSR MSGVERAPIL
HHFAESLAGA TTIRAFDQRD RFISSNLVLI DSHSRPWFHV ASAMEWLSFR LNLLSHFVFA
FSLVLLVTLP EGVINPSIAG LGVTYGLSLN VLQATVIWNI CNAENKMISV ERILQHSKIP
SEAPLVIDDQ RPLDNWPNVG SIVFRDLQVR YAEHFPAVLK NITCAFPGGK KIGVVGRTGS
GKSTLIQALF RIVEPSHGTI VIDNVDITKI GLHDLRSRLG IIPQDNALFD GTIRLNLDPL
AQYTDREIWE ALDKCQLGDV IRAKDEKLDA TVVENGENWS VGQRQLVCLG RVLLKKSNIL
VLDEATASVD SATDGVIQKI INQEFKDRTV VTIAHRIHTV IESDLVLVLS DGRIAEFDSP
AKLLQREDSF FSKLIKEYSL RSNHFAGSND LLS
