AB31G_ARATH
ID AB31G_ARATH Reviewed; 1426 AA.
AC Q7PC88; O80878;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ABC transporter G family member 31 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.31 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG31 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 3 {ECO:0000303|PubMed:18299247};
DE Short=AtPDR3 {ECO:0000303|PubMed:18299247};
GN Name=ABCG31 {ECO:0000303|PubMed:18299247};
GN Synonyms=PDR3 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
GN OrderedLocusNames=At2g29940 {ECO:0000312|Araport:AT2G29940};
GN ORFNames=F23F1.14 {ECO:0000312|EMBL:AAC31858.1};
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 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 [4]
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 [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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24474628; DOI=10.1105/tpc.113.118935;
RA Choi H., Ohyama K., Kim Y.-Y., Jin J.-Y., Lee S.B., Yamaoka Y.,
RA Muranaka T., Suh M.C., Fujioka S., Lee Y.;
RT "The role of Arabidopsis ABCG9 and ABCG31 ATP binding cassette transporters
RT in pollen fitness and the deposition of steryl glycosides on the pollen
RT coat.";
RL Plant Cell 26:310-324(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26334616; DOI=10.1038/ncomms9113;
RA Kang J., Yim S., Choi H., Kim A., Lee K.P., Lopez-Molina L., Martinoia E.,
RA Lee Y.;
RT "Abscisic acid transporters cooperate to control seed germination.";
RL Nat. Commun. 6:8113-8113(2015).
CC -!- FUNCTION: Together with ABCG25, export abscisic acid (ABA) from the
CC endosperm to deliver it to the embryo via ABCG30 and ABCG40-mediated
CC import to suppress radicle extension and subsequent embryonic growth
CC (PubMed:26334616). Together with ABCG9, involved in pollen coat
CC deposition of steryl glycosides required for pollen fitness
CC (PubMed:24474628). May be a general defense protein (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:24474628,
CC ECO:0000269|PubMed:26334616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=abscisate(in) + ATP + H2O = abscisate(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:63932, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62432, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:26334616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63933;
CC Evidence={ECO:0000269|PubMed:26334616};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24474628,
CC ECO:0000269|PubMed:26334616}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, stems, leaves, siliques and
CC inflorescence (PubMed:12430018, PubMed:24474628). In seeds, confined to
CC the endosperm (PubMed:26334616). Highly expressed in the tapetum of
CC anthers (PubMed:24474628). {ECO:0000269|PubMed:12430018,
CC ECO:0000269|PubMed:24474628, ECO:0000269|PubMed:26334616}.
CC -!- DEVELOPMENTAL STAGE: Expressed transiently during flower develoment in
CC the anthers and developing siliques (specifically in the maternal
CC tissues), mostly in the pollen and the tapetal cell layer during pollen
CC maturation. {ECO:0000269|PubMed:24474628}.
CC -!- INDUCTION: Induced by cycloheximide (CHX).
CC {ECO:0000269|PubMed:12430018}.
CC -!- DISRUPTION PHENOTYPE: Early seeds germination on imbibition without
CC stratification, and reduced abscisic acid (ABA)-mediated inhibition of
CC stratified seeds germination (PubMed:26334616). Pollen grains of the
CC double mutant abcg9 abcg31 shrivel up and collapse upon exposure to dry
CC air, and exhibit an immature coat containing reduced levels of steryl
CC glycosides, thus leading to a low viability (PubMed:24474628).
CC {ECO:0000269|PubMed:24474628, ECO:0000269|PubMed:26334616}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC31858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004680; AAC31858.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08325.1; -; Genomic_DNA.
DR EMBL; BK001002; DAA00871.1; -; Genomic_DNA.
DR PIR; T02491; T02491.
DR RefSeq; NP_180555.2; NM_128548.4.
DR AlphaFoldDB; Q7PC88; -.
DR SMR; Q7PC88; -.
DR STRING; 3702.AT2G29940.1; -.
DR iPTMnet; Q7PC88; -.
DR PaxDb; Q7PC88; -.
DR PRIDE; Q7PC88; -.
DR ProteomicsDB; 244494; -.
DR EnsemblPlants; AT2G29940.1; AT2G29940.1; AT2G29940.
DR GeneID; 817544; -.
DR Gramene; AT2G29940.1; AT2G29940.1; AT2G29940.
DR KEGG; ath:AT2G29940; -.
DR Araport; AT2G29940; -.
DR TAIR; locus:2045683; AT2G29940.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_3_1; -.
DR InParanoid; Q7PC88; -.
DR OMA; GCTDPFE; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q7PC88; -.
DR PRO; PR:Q7PC88; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7PC88; baseline and differential.
DR Genevisible; Q7PC88; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0070505; C:pollen coat; IMP: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:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0080168; P:abscisic acid transport; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0140352; P:export from cell; IMP:UniProtKB.
DR GO; GO:1901656; P:glycoside transport; IMP:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; IMP:UniProtKB.
DR GO; GO:0048581; P:negative regulation of post-embryonic development; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
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 Abscisic acid signaling pathway; ATP-binding; Cell membrane; Glycoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1426
FT /note="ABC transporter G family member 31"
FT /id="PRO_0000234630"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1202..1222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1258..1278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1396..1416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 160..434
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 512..725
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 826..1078
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1151..1365
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255"
FT BINDING 193..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 871..878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1426 AA; 159872 MW; A91A3021F47A5BD1 CRC64;
MAAASNGSEY FEFDVETGRE SFARPSNAET VEQDEEDLRW AAIGRLPSQR QGTHNAILRR
SQTQTQTSGY ADGNVVQTID VKKLDRADRE MLVRQALATS DQDNFKLLSA IKERLDRVGM
EVPKIEVRFE NLNIEADVQA GTRALPTLVN VSRDFFERCL SSLRIIKPRK HKLNILKDIS
GIIKPGRMTL LLGPPGSGKS TLLLALAGKL DKSLKKTGNI TYNGENLNKF HVKRTSAYIS
QTDNHIAELT VRETLDFAAR CQGASEGFAG YMKDLTRLEK ERGIRPSSEI DAFMKAASVK
GEKHSVSTDY VLKVLGLDVC SDTMVGNDMM RGVSGGQRKR VTTGEMTVGP RKTLFMDEIS
TGLDSSTTFQ IVKCIRNFVH LMDATVLMAL LQPAPETFDL FDDLILLSEG YMVYQGPRED
VIAFFESLGF RLPPRKGVAD FLQEVTSKKD QAQYWADPSK PYQFIPVSDI AAAFRNSKYG
HAADSKLAAP FDKKSADPSA LCRTKFAISG WENLKVCFVR ELLLIKRHKF LYTFRTCQVG
FVGLVTATVF LKTRLHPTSE QFGNEYLSCL FFGLVHMMFN GFSELPLMIS RLPVFYKQRD
NSFHPAWSWS IASWLLRVPY SVLEAVVWSG VVYFTVGLAP SAGRFFRYML LLFSVHQMAL
GLFRMMASLA RDMVIANTFG SAAILIVFLL GGFVIPKADI KPWWVWGFWV SPLSYGQRAI
AVNEFTATRW MTPSAISDTT IGLNLLKLRS FPTNDYWYWI GIAVLIGYAI LFNNVVTLAL
AYLNPLRKAR AVVLDDPNEE TALVADANQV ISEKKGMILP FKPLTMTFHN VNYYVDMPKE
MRSQGVPETR LQLLSNVSGV FSPGVLTALV GSSGAGKTTL MDVLAGRKTG GYTEGDIRIS
GHPKEQQTFA RISGYVEQND IHSPQVTVEE SLWFSASLRL PKEITKEQKK EFVEQVMRLV
ELDTLRYALV GLPGTTGLST EQRKRLTIAV ELVANPSIIF MDEPTSGLDA RAAAIVMRTV
RNTVDTGRTV VCTIHQPSID IFEAFDELLL MKRGGQVIYG GKLGTHSQVL VDYFQGINGV
PPISSGYNPA TWMLEVTTPA LEEKYNMEFA DLYKKSDQFR EVEANIKQLS VPPEGSEPIS
FTSRYSQNQL SQFLLCLWKQ NLVYWRSPEY NLVRLVFTTI AAFILGTVFW DIGSKRTSSQ
DLITVMGALY SACLFLGVSN ASSVQPIVSI ERTVFYREKA AGMYAPIPYA AAQGLVEIPY
ILTQTILYGV ITYFTIGFER TFSKFVLYLV FMFLTFTYFT FYGMMAVGLT PNQHLAAVIS
SAFYSLWNLL SGFLVQKPLI PVWWIWFYYI CPVAWTLQGV ILSQLGDVES MINEPLFHGT
VKEFIEYYFG YKPNMIGVSA AVLVGFCALF FSAFALSVKY LNFQRR
