AB25G_ARATH
ID AB25G_ARATH Reviewed; 662 AA.
AC Q84TH5; C0Z3C6; Q949Y4; Q9C8W6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ABC transporter G family member 25 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.25 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG25 {ECO:0000303|PubMed:18299247};
DE AltName: Full=White-brown complex homolog protein 26 {ECO:0000303|PubMed:11346655};
DE Short=AtWBC26 {ECO:0000303|PubMed:11346655};
GN Name=ABCG25 {ECO:0000303|PubMed:18299247};
GN Synonyms=WBC26 {ECO:0000303|PubMed:11346655};
GN OrderedLocusNames=At1g71960 {ECO:0000312|Araport:AT1G71960};
GN ORFNames=F17M19.11 {ECO:0000312|EMBL:AAG52231.1};
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 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 REVIEW ON ABSCISIC ACID HOMEOSTASIS.
RX PubMed=20935463; DOI=10.4161/psb.5.9.12566;
RA Kuromori T., Shinozaki K.;
RT "ABA transport factors found in Arabidopsis ABC transporters.";
RL Plant Signal. Behav. 5:1124-1126(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta, and cv. No-0;
RX PubMed=20133881; DOI=10.1073/pnas.0912516107;
RA Kuromori T., Miyaji T., Yabuuchi H., Shimizu H., Sugimoto E., Kamiya A.,
RA Moriyama Y., Shinozaki K.;
RT "ABC transporter AtABCG25 is involved in abscisic acid transport and
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2361-2366(2010).
RN [9]
RP INDUCTION BY STRESS, AND TISSUE SPECIFICITY.
RX PubMed=22525244; DOI=10.1016/j.plantsci.2012.03.001;
RA Baron K.N., Schroeder D.F., Stasolla C.;
RT "Transcriptional response of abscisic acid (ABA) metabolism and transport
RT to cold and heat stress applied at the reproductive stage of development in
RT Arabidopsis thaliana.";
RL Plant Sci. 188:48-59(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=24521878; DOI=10.1104/pp.114.235556;
RA Kuromori T., Sugimoto E., Shinozaki K.;
RT "Intertissue signal transfer of abscisic acid from vascular cells to guard
RT cells.";
RL Plant Physiol. 164:1587-1592(2014).
RN [11]
RP REVIEW ON PHYTOHORMONE TRANSPORT.
RX PubMed=26517905; DOI=10.1042/bst20150106;
RA Borghi L., Kang J., Ko D., Lee Y., Martinoia E.;
RT "The role of ABCG-type ABC transporters in phytohormone transport.";
RL Biochem. Soc. Trans. 43:924-930(2015).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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: High affinity abscisic acid (ABA) transporter that mediates
CC the export of ABA, with a preference for (+)-ABA, through the plasma
CC membrane, especially in vascular tissues (e.g. phloem companion cells),
CC and is involved in the intercellular ABA signaling pathway
CC (PubMed:20133881, PubMed:20935463, PubMed:24521878, PubMed:26517905).
CC Together with ABCG31, export ABA from the endosperm to deliver it to
CC the embryo via ABCG30 and ABCG40-mediated import to suppress radicle
CC extension and subsequent embryonic growth (PubMed:26334616).
CC {ECO:0000269|PubMed:20133881, ECO:0000269|PubMed:24521878,
CC ECO:0000269|PubMed:26334616, ECO:0000303|PubMed:20935463,
CC ECO:0000303|PubMed:26517905}.
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:20133881, ECO:0000269|PubMed:24521878,
CC ECO:0000269|PubMed:26334616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63933;
CC Evidence={ECO:0000269|PubMed:20133881, ECO:0000269|PubMed:24521878,
CC ECO:0000269|PubMed:26334616};
CC -!- ACTIVITY REGULATION: ADP and vanadate (ABC transporters inhibitor)
CC inhibit the ATP-dependent abscisic acid (ABA) uptake.
CC {ECO:0000269|PubMed:20133881}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=260 nM for abscisic acid (in the presence of ATP)
CC {ECO:0000269|PubMed:20133881};
CC Vmax=6.9 pmol/min/mg enzyme with abscisic acid as substrate (in the
CC presence of ATP) {ECO:0000269|PubMed:20133881};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20133881};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84TH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84TH5-2; Sequence=VSP_060644;
CC -!- TISSUE SPECIFICITY: Mainly expressed in vascular tissues,predominantly
CC in phloem companion cells, with highest levels in roots and seeds, and
CC lower levels in seedlings, stems, leaves and flowers (PubMed:20133881,
CC PubMed:24521878). Mostly observed in inflorescence meristems relative
CC to cauline leaves and developing siliques (PubMed:22525244). In seeds,
CC mainly expressed in the endosperm and, to a lesser extent, in the
CC embryo (PubMed:26334616). {ECO:0000269|PubMed:20133881,
CC ECO:0000269|PubMed:22525244, ECO:0000269|PubMed:24521878,
CC ECO:0000269|PubMed:26334616}.
CC -!- INDUCTION: By abscisic acid (ABA) (PubMed:20133881). In cauline leaves,
CC activated by cold stress, but repressed by heat stress
CC (PubMed:22525244). Within inflorescence meristems, down-regulated by
CC both cold and heat stress treatments (PubMed:22525244). In developing
CC siliques, activated by cold stress, but unaffected by heat stress
CC (PubMed:22525244). {ECO:0000269|PubMed:20133881,
CC ECO:0000269|PubMed:22525244}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid (ABA).
CC {ECO:0000269|PubMed:20133881}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52231.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021665; AAG52231.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35258.1; -; Genomic_DNA.
DR EMBL; AY050810; AAK92745.1; -; mRNA.
DR EMBL; BT005795; AAO64197.1; -; mRNA.
DR EMBL; AK319090; BAH57205.1; -; mRNA.
DR PIR; E96742; E96742.
DR RefSeq; NP_565030.1; NM_105854.1. [Q84TH5-1]
DR AlphaFoldDB; Q84TH5; -.
DR SMR; Q84TH5; -.
DR STRING; 3702.AT1G71960.1; -.
DR TCDB; 3.A.1.204.28; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q84TH5; -.
DR PRIDE; Q84TH5; -.
DR ProteomicsDB; 243302; -. [Q84TH5-1]
DR EnsemblPlants; AT1G71960.1; AT1G71960.1; AT1G71960. [Q84TH5-1]
DR GeneID; 843527; -.
DR Gramene; AT1G71960.1; AT1G71960.1; AT1G71960. [Q84TH5-1]
DR KEGG; ath:AT1G71960; -.
DR Araport; AT1G71960; -.
DR TAIR; locus:2016089; AT1G71960.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_10_1; -.
DR InParanoid; Q84TH5; -.
DR OMA; RVRPWWD; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q84TH5; -.
DR PRO; PR:Q84TH5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84TH5; baseline and differential.
DR Genevisible; Q84TH5; 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: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:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0080168; P:abscisic acid transport; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0140352; P:export from cell; IDA:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; IDA:UniProtKB.
DR GO; GO:0048581; P:negative regulation of post-embryonic development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IDA: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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; ATP-binding;
KW Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..662
FT /note="ABC transporter G family member 25"
FT /id="PRO_0000240697"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..308
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 388..594
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /id="VSP_060644"
FT CONFLICT 118
FT /note="L -> F (in Ref. 4; BAH57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="L -> I (in Ref. 3; AAK92745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 72903 MW; AA84BD738D2D488A CRC64;
MSAFDGVENQ MNGPDSSPRL SQDPREPRSL LSSSCFPITL KFVDVCYRVK IHGMSNDSCN
IKKLLGLKQK PSDETRSTEE RTILSGVTGM ISPGEFMAVL GPSGSGKSTL LNAVAGRLHG
SNLTGKILIN DGKITKQTLK RTGFVAQDDL LYPHLTVRET LVFVALLRLP RSLTRDVKLR
AAESVISELG LTKCENTVVG NTFIRGISGG ERKRVSIAHE LLINPSLLVL DEPTSGLDAT
AALRLVQTLA GLAHGKGKTV VTSIHQPSSR VFQMFDTVLL LSEGKCLFVG KGRDAMAYFE
SVGFSPAFPM NPADFLLDLA NGVCQTDGVT EREKPNVRQT LVTAYDTLLA PQVKTCIEVS
HFPQDNARFV KTRVNGGGIT TCIATWFSQL CILLHRLLKE RRHESFDLLR IFQVVAASIL
CGLMWWHSDY RDVHDRLGLL FFISIFWGVL PSFNAVFTFP QERAIFTRER ASGMYTLSSY
FMAHVLGSLS MELVLPASFL TFTYWMVYLR PGIVPFLLTL SVLLLYVLAS QGLGLALGAA
IMDAKKASTI VTVTMLAFVL TGGYYVNKVP SGMVWMKYVS TTFYCYRLLV AIQYGSGEEI
LRMLGCDSKG KQGASAATSA GCRFVEEEVI GDVGMWTSVG VLFLMFFGYR VLAYLALRRI
KH
