FREE1_ARATH
ID FREE1_ARATH Reviewed; 601 AA.
AC Q9ASS2; Q940J6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein FREE1 {ECO:0000303|PubMed:25438943};
DE AltName: Full=FYVE domain protein required for endosomal sorting 1 {ECO:0000303|PubMed:24843126};
DE AltName: Full=FYVE domain-containing protein 1 {ECO:0000303|PubMed:24843126};
GN Name=FREE1 {ECO:0000303|PubMed:25438943};
GN Synonyms=FYVE1 {ECO:0000303|PubMed:24843126};
GN OrderedLocusNames=At1g20110 {ECO:0000312|Araport:AT1G20110};
GN ORFNames=T20H2.10 {ECO:0000312|EMBL:AAF79901.1};
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 {ECO:0000312|EMBL:AAK32902.1};
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].
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] OF 1-429.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [7]
RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, IDENTIFICATION IN THE ESCRT-I COMPLEX, INTERACTION WITH VPS23A
RP AND VPS23B, AND MUTAGENESIS OF PRO-32; PRO-33; PRO-35; PRO-83 AND PRO-86.
RX PubMed=25438943; DOI=10.1016/j.cub.2014.09.014;
RA Gao C., Luo M., Zhao Q., Yang R., Cui Y., Zeng Y., Xia J., Jiang L.;
RT "A unique plant ESCRT component, FREE1, regulates multivesicular body
RT protein sorting and plant growth.";
RL Curr. Biol. 24:2556-2563(2014).
RN [8]
RP FUNCTION, INTERACTION WITH IRT1, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24843126; DOI=10.1073/pnas.1402262111;
RA Barberon M., Dubeaux G., Kolb C., Isono E., Zelazny E., Vert G.;
RT "Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil
RT interface plays crucial role in metal homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8293-8298(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SH3P2 AND SH3P3.
RX PubMed=25699591; DOI=10.1104/pp.114.253377;
RA Kolb C., Nagel M.K., Kalinowska K., Hagmann J., Ichikawa M.,
RA Anzenberger F., Alkofer A., Sato M.H., Braun P., Isono E.;
RT "FYVE1 is essential for vacuole biogenesis and intracellular trafficking in
RT Arabidopsis.";
RL Plant Physiol. 167:1361-1373(2015).
RN [10]
RP FUNCTION, INTERACTION WITH SH3P2, AND IDENTIFICATION IN A PI3K COMPLEX.
RX PubMed=25624505; DOI=10.1073/pnas.1421271112;
RA Gao C., Zhuang X., Cui Y., Fu X., He Y., Zhao Q., Zeng Y., Shen J., Luo M.,
RA Jiang L.;
RT "Dual roles of an Arabidopsis ESCRT component FREE1 in regulating vacuolar
RT protein transport and autophagic degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1886-1891(2015).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PYL4 AND PYR1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27495812; DOI=10.1105/tpc.16.00178;
RA Belda-Palazon B., Rodriguez L., Fernandez M.A., Castillo M.-C.,
RA Anderson E.M., Gao C., Gonzalez-Guzman M., Peirats-Llobet M., Zhao Q.,
RA De Winne N., Gevaert K., De Jaeger G., Jiang L., Leon J., Mullen R.T.,
RA Rodriguez P.L.;
RT "FYVE1/FREE1 interacts with the PYL4 ABA receptor and mediates its delivery
RT to the vacuolar degradation pathway.";
RL Plant Cell 28:2291-2311(2016).
RN [12]
RP FUNCTION, INTERACTION WITH SNRK2D; SNRK2I; ABF4 AND ABI5, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT SER-530 AND SER-533, AND MUTAGENESIS OF
RP LEU-338; LEU-341; MET-343; SER-530 AND SER-533.
RX PubMed=30962512; DOI=10.1038/s41477-019-0400-5;
RA Li H., Li Y., Zhao Q., Li T., Wei J., Li B., Shen W., Yang C., Zeng Y.,
RA Rodriguez P.L., Zhao Y., Jiang L., Wang X., Gao C.;
RT "The plant ESCRT component FREE1 shuttles to the nucleus to attenuate
RT abscisic acid signalling.";
RL Nat. Plants 5:512-524(2019).
RN [13]
RP INTERACTION WITH SINAT1; SINAT2; SINAT3; SINAT4 AND SINAT5, SUBCELLULAR
RP LOCATION, AND UBIQUITINATION.
RX PubMed=32786047; DOI=10.1111/jipb.13005;
RA Xiao Z., Yang C., Liu C., Yang L., Yang S., Zhou J., Li F., Jiang L.,
RA Xiao S., Gao C., Shen W.;
RT "SINAT E3 ligases regulate the stability of the ESCRT component FREE1 in
RT response to iron deficiency in plants.";
RL J. Integr. Plant Biol. 62:1399-1417(2020).
RN [14]
RP INTERACTION WITH SINAT1; SINAT2; SINAT3 AND SINAT4, AND UBIQUITINATION.
RX PubMed=32753431; DOI=10.1105/tpc.20.00267;
RA Xia F.N., Zeng B., Liu H.S., Qi H., Xie L.J., Yu L.J., Chen Q.F., Li J.F.,
RA Chen Y.Q., Jiang L., Xiao S.;
RT "SINAT E3 ubiquitin ligases mediate FREE1 and VPS23A degradation to
RT modulate abscisic acid signaling.";
RL Plant Cell 32:3290-3310(2020).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=32540007; DOI=10.1016/j.plantsci.2020.110489;
RA Pan W., Zheng P., Zhang C., Wang W., Li Y., Fan T., Liu Y., Cao S.;
RT "The effect of ABRE BINDING FACTOR 4-mediated FYVE1 on salt stress
RT tolerance in Arabidopsis.";
RL Plant Sci. 296:110489-110489(2020).
CC -!- FUNCTION: Endosomal sorting complex required for transport (ESCRT)
CC component regulating multivesicular body (MVB) protein sorting and
CC plant growth (PubMed:25438943). Required for the formation of intra-
CC luminal vesicles (ILVs)in MVBs (PubMed:25438943). Binds to
CC phosphatidylinositol-3-phosphate (PI3P) and ubiquitin (PubMed:24843126,
CC PubMed:25438943). Controls IRT1 recycling to the plasma membrane and
CC impacts the polar delivery of this transporter to the outer plasma
CC membrane domain (PubMed:24843126). Regulates ubiquitin-dependent
CC membrane protein degradation, vacuolar transport, autophagy, and
CC vacuole biogenesis (PubMed:25624505, PubMed:25699591). ESCRT component
CC that binds ubiquitin and regulates vacuolar sorting of proteins
CC (PubMed:27495812). Attenuates abscisic acid (ABA) signaling through
CC RSL1-triggered degradation of the ABA receptors PYR1 and PYL4
CC (PubMed:27495812). Interacts with PYL4 and PYR1, and delivers the
CC ubiquitinated ABA receptors as cargo to the vacuolar degradation
CC pathway (PubMed:27495812). In response to ABA, is phosphorylated by
CC SnRK2 kinases which mediate FREE1 nuclear import (PubMed:30962512). In
CC the nucleus, interacts with the ABA-responsive transcription factors
CC ABF4 and ABI5 to reduce their ability to bind to their cis-regulatory
CC sequences of downstream genes, thus leading to transcriptional
CC inhibition of ABA signaling pathway (PubMed:30962512). Negatively
CC regulates salt stress tolerance via a negative feedback loop involving
CC ABA signaling pathway (PubMed:32540007). {ECO:0000269|PubMed:24843126,
CC ECO:0000269|PubMed:25438943, ECO:0000269|PubMed:25624505,
CC ECO:0000269|PubMed:25699591, ECO:0000269|PubMed:27495812,
CC ECO:0000269|PubMed:30962512, ECO:0000269|PubMed:32540007}.
CC -!- SUBUNIT: Part of the ESCRT-I complex (PubMed:25438943). Interacts with
CC VPS23A and VPS23B, but not with VPS28 or VPS37 (PubMed:25438943).
CC Interacts with IRT1 (PubMed:24843126). Interacts with SH3P2
CC (PubMed:25699591, PubMed:25624505). Interacts with SH3P3, but not with
CC SH3P1 (PubMed:25699591). Interacts (via N-terminus) with PYL4 and PYR3
CC (PubMed:27495812). Interacts (via C-terminus) with SNRK2D/SNRK2.2,
CC SNRK2I/SNRK2.3, ABF4 and ABI5 (PubMed:30962512). Interacts with SINAT1,
CC SINAT2, SINAT3 and SINAT4 (PubMed:32786047, PubMed:32753431). Interacts
CC with SINAT5 (PubMed:32786047). Component of a phosphoinositide 3-kinase
CC (PI3K) complex containing ATG6, SH3P2 and FREE1 (PubMed:25624505).
CC {ECO:0000269|PubMed:24843126, ECO:0000269|PubMed:25438943,
CC ECO:0000269|PubMed:25624505, ECO:0000269|PubMed:25699591,
CC ECO:0000269|PubMed:27495812, ECO:0000269|PubMed:30962512,
CC ECO:0000269|PubMed:32753431, ECO:0000269|PubMed:32786047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24843126,
CC ECO:0000269|PubMed:25438943, ECO:0000269|PubMed:25699591,
CC ECO:0000269|PubMed:30962512}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:25438943, ECO:0000269|PubMed:27495812}; Peripheral
CC membrane protein {ECO:0000269|PubMed:25438943}. Late endosome
CC {ECO:0000269|PubMed:24843126, ECO:0000269|PubMed:25699591,
CC ECO:0000269|PubMed:27495812}. Endosome, multivesicular body
CC {ECO:0000269|PubMed:32786047}. Nucleus {ECO:0000269|PubMed:24843126,
CC ECO:0000269|PubMed:30962512}. Note=In response to abscisic acid (ABA),
CC SnRK2 kinases phosphorylate FREE1, a step requisite for ABA-induced
CC FREE1 nuclear import. {ECO:0000269|PubMed:30962512}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Lowest expression in mature seeds.
CC {ECO:0000269|PubMed:25438943}.
CC -!- INDUCTION: Not regulated by iron starvation (PubMed:24843126). Induced
CC by abscisic acid (ABA), salt stress and osmotic stress
CC (PubMed:32540007). {ECO:0000269|PubMed:24843126,
CC ECO:0000269|PubMed:32540007}.
CC -!- DOMAIN: The FYVE domain is required for PI3P binding (PubMed:25438943).
CC The N-terminal domain (31-86) is required for the interaction with
CC VPS23A and B (PubMed:25438943). The C-terminal domain (515-601) is
CC required for the binding to ubiquitin (PubMed:25438943). The C-terminal
CC coiled-coil region is required for the interaction with SH3P2
CC (PubMed:25624505). {ECO:0000269|PubMed:25438943,
CC ECO:0000269|PubMed:25624505}.
CC -!- PTM: Phosphorylated at Ser-530 and Ser-533 by SNRK2D/SNRK2.2 and
CC SNRK2I/SNRK2.3 in response to abscisic acid (ABA) (PubMed:30962512).
CC Phosphorylation is necessary for ABA-induced FREE1 nuclear import
CC (PubMed:30962512). {ECO:0000269|PubMed:30962512}.
CC -!- PTM: Ubiquitinated by SINAT1, SINAT2, SINAT3 and SINAT4 for subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:32753431,
CC ECO:0000269|PubMed:32786047}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality when homozygous
CC (PubMed:25438943, PubMed:25699591). Degenerated root surface structures
CC and vacuoles with altered morphology (PubMed:25699591). Accumulation of
CC ubiquitinated membrane-associated proteins (PubMed:25699591).
CC Hypersensitivity to abscisic acid (ABA) due to impaired targeting of
CC ABA receptors (e.g. PYL4 and PYR1) for vacuolar degradation, thus
CC leading to their accumulation and an enhanced response to ABA
CC (PubMed:27495812). {ECO:0000269|PubMed:25438943,
CC ECO:0000269|PubMed:25699591, ECO:0000269|PubMed:27495812}.
CC -!- MISCELLANEOUS: Reduction-of-function FREE1 alleles exhibit enhanced
CC sensitivity to abscisic acid-mediated inhibition of seedling
CC establishment (PubMed:27495812). Seedlings overexpressing FREE1 exhibit
CC increased sensitivity to salt stress (PubMed:32540007).
CC {ECO:0000269|PubMed:27495812, ECO:0000269|PubMed:32540007}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79901.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g20110 has been split into 2 genes: At1g20110 and At1g20120.; Evidence={ECO:0000305};
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DR EMBL; AC022472; AAF79901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29937.1; -; Genomic_DNA.
DR EMBL; AF367315; AAK32902.1; -; mRNA.
DR EMBL; AF428277; AAL16109.1; -; mRNA.
DR EMBL; AY143942; AAN28881.1; -; mRNA.
DR EMBL; AY054543; AAK96734.1; -; mRNA.
DR EMBL; AK221672; BAD95359.1; -; mRNA.
DR RefSeq; NP_564103.1; NM_101865.4.
DR AlphaFoldDB; Q9ASS2; -.
DR SMR; Q9ASS2; -.
DR IntAct; Q9ASS2; 1.
DR STRING; 3702.AT1G20110.1; -.
DR iPTMnet; Q9ASS2; -.
DR PaxDb; Q9ASS2; -.
DR PRIDE; Q9ASS2; -.
DR ProteomicsDB; 228943; -.
DR EnsemblPlants; AT1G20110.1; AT1G20110.1; AT1G20110.
DR GeneID; 838600; -.
DR Gramene; AT1G20110.1; AT1G20110.1; AT1G20110.
DR KEGG; ath:AT1G20110; -.
DR Araport; AT1G20110; -.
DR TAIR; locus:2198646; AT1G20110.
DR eggNOG; KOG1729; Eukaryota.
DR HOGENOM; CLU_012981_2_0_1; -.
DR InParanoid; Q9ASS2; -.
DR OMA; WSSSFDD; -.
DR OrthoDB; 900019at2759; -.
DR PhylomeDB; Q9ASS2; -.
DR PRO; PR:Q9ASS2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ASS2; baseline and differential.
DR Genevisible; Q9ASS2; AT.
DR GO; GO:0000813; C:ESCRT I complex; IPI:TAIR.
DR GO; GO:0031902; C:late endosome membrane; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0036258; P:multivesicular body assembly; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045893; FREE1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46977; PTHR46977; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Coiled coil; Cytoplasm; Endosome;
KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="Protein FREE1"
FT /id="PRO_0000434149"
FT ZN_FING 455..515
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..344
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:30962512"
FT REGION 542..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 527..552
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30962512,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 32
FT /note="P->A: Loss of interactions with VPS23A and VPS23B;
FT when associated with A-33; A-35; A-83 and A-86."
FT /evidence="ECO:0000269|PubMed:25438943"
FT MUTAGEN 33
FT /note="P->A: Loss of interactions with VPS23A and VPS23B;
FT when associated with A-32; A-35; A-83 and A-86."
FT /evidence="ECO:0000269|PubMed:25438943"
FT MUTAGEN 35
FT /note="P->A: Loss of interactions with VPS23A and VPS23B;
FT when associated with A-32; A-33; A-83 and A-86."
FT /evidence="ECO:0000269|PubMed:25438943"
FT MUTAGEN 83
FT /note="P->A: Loss of interactions with VPS23A and VPS23B;
FT when associated with A-32; A-33; A-35 and A-86."
FT /evidence="ECO:0000269|PubMed:25438943"
FT MUTAGEN 86
FT /note="P->A: Loss of interactions with VPS23A and VPS23B;
FT when associated with A-32; A-33; A-35 and A-83."
FT /evidence="ECO:0000269|PubMed:25438943"
FT MUTAGEN 341
FT /note="L->A: Localizes predominantly to the nucleus; when
FT associated with A-338 and A-343."
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 343
FT /note="M->A: Localizes predominantly to the nucleus; when
FT associated with A-338 and A-341."
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 530
FT /note="S->A: Abolishes phosphorylation; abolishes abscisic
FT acid-induced nuclear import; when associated with A-533."
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 530
FT /note="S->D: Mimicks constitutive phosphorylation;
FT accumulates in the nucleus in the absence of abscisic acid
FT treatment; when associated with D-533."
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 533
FT /note="S->A: Abolishes phosphorylation; abolishes abscisic
FT acid-induced nuclear import; when associated with A-530."
FT /evidence="ECO:0000269|PubMed:30962512"
FT MUTAGEN 533
FT /note="S->D: Mimicks constitutive phosphorylation;
FT accumulates in the nucleus in the absence of abscisic acid
FT treatment; when associated with D-530."
SQ SEQUENCE 601 AA; 65396 MW; 919CD7FC2B8E3489 CRC64;
MQQGDYNSYY HHQYSQFQNP TPNPNPNPNP SPPAPATVAG PTDLTRNTYA SAPPFTGGYG
SADYSNYSQN YTPYGQNSEH VPPSAPSFTS PSQPPPSPPA TSLNPNSYST FNQPPPPPTI
HPQPLSSYGS FDSTAPYQQP TSQHMYYSPY DQHQTSGYSS APPPSSAPAP NPNPAPYSSS
LYSAPPYSSG GSSIPPSYEK PSVKFDQSGY DGYNRSRSDL GSDLYGKRSD SGEYPAFEDS
YGDGVYAYQG GKVEPYGSRG TAPKSSNSTL FDDYGRSISF SSSGRDSSVS SNSAKIVRAV
PKADVQEDST GGVQKFRVKL LAETYGQTTT DVLCQIGLDG LRMLDPSTSR TLRIYPLENI
TRCEKLDSSI LAFWSKTPVD IEAKRIRLQS NSYTTNTLLD TVTAAMFQAK EIGGSSRPPT
SGKLIEQTAE KKKGLGDWMN IIKPVNEEKD HWVPDEAVSK CTSCGSDFGA FIRRHHCRNC
GDVFCDKCTQ GRIALTAEDN APQVRVCDRC MAEVSQRLSN AKETTGRNVS LQSHEDLARK
LQEEMERNRK SSSGLREGSG RRMKEVACPT CTVHLQVQVP VSGSETIECG VCQNPFLVSA
H
