AB32G_ARATH
ID AB32G_ARATH Reviewed; 1420 AA.
AC O81016;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ABC transporter G family member 32 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.32;
DE Short=AtABCG32 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 4 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
DE AltName: Full=Protein PERMEABLE CUTICLE 1 {ECO:0000303|PubMed:21628525};
GN Name=ABCG32 {ECO:0000303|PubMed:18299247};
GN Synonyms=PDR4 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311},
GN PEC1 {ECO:0000303|PubMed:21628525};
GN OrderedLocusNames=At2g26910 {ECO:0000312|Araport:AT2G26910};
GN ORFNames=F12C20.5 {ECO:0000312|EMBL:AAC32236.1};
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1355-1420.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12430018; DOI=10.1007/s00425-002-0889-z;
RA van den Brule S., Smart C.C.;
RT "The plant PDR family of ABC transporters.";
RL Planta 216:95-106(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
RA Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
RT "Organization and function of the plant pleiotropic drug resistance ABC
RT transporter family.";
RL FEBS Lett. 580:1123-1130(2006).
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).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21628525; DOI=10.1105/tpc.111.083121;
RA Bessire M., Borel S., Fabre G., Carraca L., Efremova N., Yephremov A.,
RA Cao Y., Jetter R., Jacquat A.C., Metraux J.P., Nawrath C.;
RT "A member of the PLEIOTROPIC DRUG RESISTANCE family of ATP binding cassette
RT transporters is required for the formation of a functional cuticle in
RT Arabidopsis.";
RL Plant Cell 23:1958-1970(2011).
CC -!- FUNCTION: May be a general defense protein (By similarity). Required
CC for the formation of the cuticle layer of the cell wall
CC (PubMed:21628525). {ECO:0000250, ECO:0000269|PubMed:21628525}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21628525};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21628525}.
CC -!- TISSUE SPECIFICITY: Ubiquitous in aerial organs (PubMed:12430018,
CC PubMed:21628525). Higher expression levels in young, expanding tissues
CC than in older tissues. Detected in the epidermal layer
CC (PubMed:21628525). {ECO:0000269|PubMed:12430018,
CC ECO:0000269|PubMed:21628525}.
CC -!- INDUCTION: Repressed by cycloheximide (CHX) and abscisic acid (ABA).
CC {ECO:0000269|PubMed:12430018}.
CC -!- DISRUPTION PHENOTYPE: Chemical composition modifications and structural
CC alterations of the cuticular layer of the cell wall leading to
CC increased permeability of the cuticle, increased sensitivity to
CC herbicide (glufosidate), increased cuticular transpiration and
CC increased resistance to Botrytis cinerea.
CC {ECO:0000269|PubMed:21628525}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AC005168; AAC32236.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07906.1; -; Genomic_DNA.
DR EMBL; BX821941; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK001003; DAA00872.1; -; Genomic_DNA.
DR PIR; T02644; T02644.
DR RefSeq; NP_180259.1; NM_128248.2.
DR AlphaFoldDB; O81016; -.
DR SMR; O81016; -.
DR BioGRID; 2584; 1.
DR STRING; 3702.AT2G26910.1; -.
DR TCDB; 3.A.1.205.16; the atp-binding cassette (abc) superfamily.
DR iPTMnet; O81016; -.
DR PaxDb; O81016; -.
DR PRIDE; O81016; -.
DR ProteomicsDB; 245084; -.
DR EnsemblPlants; AT2G26910.1; AT2G26910.1; AT2G26910.
DR GeneID; 817232; -.
DR Gramene; AT2G26910.1; AT2G26910.1; AT2G26910.
DR KEGG; ath:AT2G26910; -.
DR Araport; AT2G26910; -.
DR TAIR; locus:2039523; AT2G26910.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; O81016; -.
DR OMA; SSWGQWI; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; O81016; -.
DR PRO; PR:O81016; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81016; baseline and differential.
DR Genevisible; O81016; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0080051; P:cutin transport; IMP:TAIR.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1420
FT /note="ABC transporter G family member 32"
FT /id="PRO_0000234631"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1162..1182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1202..1222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1235..1255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1277..1297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1307..1327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1334..1354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1392..1412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 135..408
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 486..699
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 818..1070
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1143..1357
FT /note="ABC transmembrane type-2 2"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 863..870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1420 AA; 161265 MW; 9E192A9D5A46A601 CRC64;
MWNSAENAFS RSTSFKDEIE DEEELRWAAL QRLPTYSRIR RGIFRDMVGE PKEIQIGNLE
ASEQRLLLDR LVNSVENDPE QFFARVRKRF DAVDLKFPKI EVRFQNLMVE SFVHVGSRAL
PTIPNFIINM AEGLLRNIHV IGGKRNKLTI LDGISGVIRP SRLTLLLGPP SSGKTTLLLA
LAGRLGTNLQ TSGKITYNGY DLKEIIAPRT SAYVSQQDWH VAEMTVRQTL EFAGRCQGVG
FKYDMLLELA RREKLAGIVP DEDLDIFMKS LALGGMETSL VVEYVMKILG LDTCADTLVG
DEMIKGISGG QKKRLTTGEL LVGPARVLFM DEISNGLDSS TTHQIIMYMR HSTHALEGTT
VISLLQPSPE TYELFDDVIL MSEGQIIYQG PRDEVLDFFS SLGFTCPDRK NVADFLQEVT
SKKDQQQYWS VPFRPYRYVP PGKFAEAFRS YPTGKKLAKK LEVPFDKRFN HSAALSTSQY
GVKKSELLKI NFAWQKQLMK QNAFIYVFKF VQLLLVALIT MTVFCRTTMH HNTIDDGNIY
LGSLYFSMVI ILFNGFTEVP MLVAKLPVLY KHRDLHFYPS WAYTLPSWLL SIPTSIIESA
TWVAVTYYTI GYDPLFSRFL QQFLLYFSLH QMSLGLFRVM GSLGRHMIVA NTFGSFAMLV
VMTLGGFIIS RDSIPSWWIW GYWISPLMYA QNAASVNEFL GHNWQKTAGN HTSDSLGLAL
LKERSLFSGN YWYWIGVAAL LGYTVLFNIL FTLFLAHLNP WGKFQAVVSR EELDEREKKR
KGDEFVVELR EYLQHSGSIH GKYFKNRGMV LPFQPLSLSF SNINYYVDVP LGLKEQGILE
DRLQLLVNIT GAFRPGVLTA LVGVSGAGKT TLMDVLAGRK TGGTIEGDVY ISGFPKRQET
FARISGYCEQ NDVHSPCLTV VESLLFSACL RLPADIDSET QRAFVHEVME LVELTSLSGA
LVGLPGVDGL STEQRKRLTI AVELVANPSI VFMDEPTSGL DARAAAIVMR TVRNIVNTGR
TIVCTIHQPS IDIFESFDEL LFMKRGGELI YAGPLGQKSC ELIKYFESIE GVQKIKPGHN
PAAWMLDVTA STEEHRLGVD FAEIYRNSNL CQRNKELIEV LSKPSNIAKE IEFPTRYSQS
LYSQFVACLW KQNLSYWRNP QYTAVRFFYT VVISLMLGTI CWKFGSKRDT QQQLFNAMGS
MYAAVLFIGI TNATAAQPVV SIERFVSYRE RAAGMYSALP FAFAQVFIEF PYVLAQSTIY
STIFYAMAAF EWSAVKFLWY LFFMYFSIMY FTFYGMMTTA ITPNHNVASI IAAPFYMLWN
LFSGFMIPYK RIPLWWRWYY WANPVAWTLY GLLVSQYGDD ERSVKLSDGI HQVMVKQLLE
DVMGYKHDFL GVSAIMVVAF CVFFSLVFAF AIKAFNFQRR
