AB12G_ARATH
ID AB12G_ARATH Reviewed; 687 AA.
AC Q9C8K2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ABC transporter G family member 12 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.12 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG12 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Protein ECERIFERUM 5 {ECO:0000303|PubMed:11336252, ECO:0000303|PubMed:15499022};
DE AltName: Full=White-brown complex homolog protein 12 {ECO:0000303|PubMed:15499022};
DE Short=AtWBC12 {ECO:0000303|PubMed:15499022};
GN Name=ABCG12 {ECO:0000303|PubMed:18299247};
GN Synonyms=CER5 {ECO:0000303|PubMed:11336252, ECO:0000303|PubMed:15499022},
GN D3, WBC12 {ECO:0000303|PubMed:15499022};
GN OrderedLocusNames=At1g51500 {ECO:0000312|Araport:AT1G51500};
GN ORFNames=F5D21.6 {ECO:0000312|EMBL:AAG52619.1};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLY-171.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15499022; DOI=10.1126/science.1102331;
RA Pighin J.A., Zheng H., Balakshin L.J., Goodman I.P., Western T.L.,
RA Jetter R., Kunst L., Samuels A.L.;
RT "Plant cuticular lipid export requires an ABC transporter.";
RL Science 306:702-704(2004).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=11336252; DOI=10.1016/s0031-9422(00)00513-6;
RA Rashotte A.M., Jenks M.A., Feldmann K.A.;
RT "Cuticular waxes on eceriferum mutants of Arabidopsis thaliana.";
RL Phytochemistry 57:115-123(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SALT AND ABSCISIC ACID.
RX PubMed=17951461; DOI=10.1104/pp.107.105676;
RA Panikashvili D., Savaldi-Goldstein S., Mandel T., Yifhar T., Franke R.B.,
RA Hoefer R., Schreiber L., Chory J., Aharoni A.;
RT "The Arabidopsis DESPERADO/AtWBC11 transporter is required for cutin and
RT wax secretion.";
RL Plant Physiol. 145:1345-1360(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, 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).
RN [10]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH ABCG11.
RC STRAIN=cv. Columbia;
RX PubMed=20870961; DOI=10.1105/tpc.110.077974;
RA McFarlane H.E., Shin J.J.H., Bird D.A., Samuels A.L.;
RT "Arabidopsis ABCG transporters, which are required for export of diverse
RT cuticular lipids, dimerize in different combinations.";
RL Plant Cell 22:3066-3075(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=26965486; DOI=10.1016/j.bbalip.2016.03.002;
RA Sadler C., Schroll B., Zeisler V., Wassmann F., Franke R., Schreiber L.;
RT "Wax and cutin mutants of Arabidopsis: Quantitative characterization of the
RT cuticular transport barrier in relation to chemical composition.";
RL Biochim. Biophys. Acta 1861:1336-1344(2016).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=28346494; DOI=10.1371/journal.pone.0174014;
RA Maxwell D.J., Partridge J.C., Roberts N.W., Boonham N., Foster G.D.;
RT "The effects of surface structure mutations in Arabidopsis thaliana on the
RT polarization of reflections from virus-infected leaves.";
RL PLoS ONE 12:e0174014-e0174014(2017).
CC -!- FUNCTION: Involved in the secretion of cuticular wax from epidermal
CC cells to the cuticle, especially in the transport of aldehydes,
CC alcohols and acids. {ECO:0000269|PubMed:11336252,
CC ECO:0000269|PubMed:15499022, ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:26965486}.
CC -!- FUNCTION: (Microbial infection) Required for the polarization of
CC reflected light on both adaxial and abaxial leaves surfaces upon viral
CC infection by Turnip vein clearing virus (TVCV), probably by regulating
CC cuticular wax compounds deposition, thus influencing visual
CC attractiveness of infected plants for insect vectors.
CC {ECO:0000269|PubMed:28346494}.
CC -!- SUBUNIT: Forms heterodimers with ABCG11 in epidermal cells.
CC {ECO:0000269|PubMed:20870961}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15499022,
CC ECO:0000269|PubMed:20870961}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15499022}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:20870961}. Note=Trafficking to the plasma membrane
CC is dependent of ABCG11. {ECO:0000269|PubMed:20870961}.
CC -!- TISSUE SPECIFICITY: Exclusively and constitutively expressed in
CC epidermal cells. {ECO:0000269|PubMed:15499022}.
CC -!- INDUCTION: By NaCl and abscisic acid (ABA).
CC {ECO:0000269|PubMed:17951461}.
CC -!- DISRUPTION PHENOTYPE: Abnormal cuticle and unusual lipidic
CC cytoplasmatic inclusions in epidermal cells associated with a reduced
CC secretion of aldehydes, alcohols and acids (PubMed:17951461,
CC PubMed:26965486). The double mutant abcg11 abcg12 exhibits ABCG12-
CC containing membrane inclusions protruded into the vacuole and
CC contiguous with the endoplasmic reticulum (PubMed:20870961). Reduced
CC polarizing on the adaxial and abaxial leaves surfaces, and impaired
CC impact of viral infection by Turnip vein clearing virus (TVCV) on the
CC polarization of reflected light leading to high light reflections; this
CC phenotype is not visible upon viral infection by Cucumber mosaic virus
CC (CMV) (PubMed:28346494). {ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:20870961, ECO:0000269|PubMed:26965486,
CC ECO:0000269|PubMed:28346494}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) 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; AY734542; AAU44368.1; -; Genomic_DNA.
DR EMBL; AC024261; AAG52619.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32674.1; -; Genomic_DNA.
DR EMBL; AF412079; AAL06532.1; -; mRNA.
DR EMBL; AY093162; AAM13161.1; -; mRNA.
DR EMBL; BT008427; AAP37786.1; -; mRNA.
DR PIR; D96553; D96553.
DR RefSeq; NP_175561.1; NM_104028.5.
DR AlphaFoldDB; Q9C8K2; -.
DR SMR; Q9C8K2; -.
DR BioGRID; 26800; 27.
DR IntAct; Q9C8K2; 24.
DR STRING; 3702.AT1G51500.1; -.
DR TCDB; 3.A.1.204.4; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9C8K2; -.
DR PaxDb; Q9C8K2; -.
DR PRIDE; Q9C8K2; -.
DR ProteomicsDB; 244598; -.
DR EnsemblPlants; AT1G51500.1; AT1G51500.1; AT1G51500.
DR GeneID; 841575; -.
DR Gramene; AT1G51500.1; AT1G51500.1; AT1G51500.
DR KEGG; ath:AT1G51500; -.
DR Araport; AT1G51500; -.
DR TAIR; locus:2033899; AT1G51500.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_7_1; -.
DR InParanoid; Q9C8K2; -.
DR OMA; CKRENIY; -.
DR OrthoDB; 806939at2759; -.
DR PhylomeDB; Q9C8K2; -.
DR PRO; PR:Q9C8K2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8K2; baseline and differential.
DR Genevisible; Q9C8K2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0140352; P:export from cell; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..687
FT /note="ABC transporter G family member 12"
FT /id="PRO_0000240684"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..269
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 361..573
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT REGION 649..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RXN0"
FT MUTAGEN 171
FT /note="G->D: In cer5-1; accumulation of wax in epidermal
FT cells cytoplasm, and reduction of cuticular wax
FT deposition."
FT /evidence="ECO:0000269|PubMed:15499022"
SQ SEQUENCE 687 AA; 76451 MW; 030F0031DEBC8B8F CRC64;
MELESTSNGR RPPPPAEIGR GAYLAWEDLT VVIPNFSGGP TRRLLDGLNG HAEPGRIMAI
MGPSGSGKST LLDSLAGRLA RNVIMTGNLL LNGKKARLDY GLVAYVTQED ILMGTLTVRE
TITYSAHLRL SSDLTKEEVN DIVEGTIIEL GLQDCADRVI GNWHSRGVSG GERKRVSVAL
EILTRPQILF LDEPTSGLDS ASAFFVIQAL RNIARDGGRT VVSSIHQPSS EVFALFDDLF
LLSSGETVYF GESKFAVEFF AEAGFPCPKK RNPSDHFLRC INSDFDTVTA TLKGSQRIRE
TPATSDPLMN LATSEIKARL VENYRRSVYA KSAKSRIREL ASIEGHHGME VRKGSEATWF
KQLRTLTKRS FVNMCRDIGY YWSRIVIYIV VSFCVGTIFY DVGHSYTSIL ARVSCGGFIT
GFMTFMSIGG FPSFIEEMKV FYKERLSGYY GVSVYIISNY VSSFPFLVAI ALITGSITYN
MVKFRPGVSH WAFFCLNIFF SVSVIESLMM VVASLVPNFL MGLITGAGII GIIMMTSGFF
RLLPDLPKVF WRYPISFMSY GSWAIQGAYK NDFLGLEFDP MFAGEPKMTG EQVINKIFGV
QVTHSKWWDL SAIVLILVCY RILFFIVLKL KERAEPALKA IQAKRTMKSL KKRPSFKKVP
SLSSLSSRRH QPLHSLSSQE GLTSPIN
