PIF3_ARATH
ID PIF3_ARATH Reviewed; 524 AA.
AC O80536; A5Y7A2; A5Y7A3; A5Y7A4; A5Y7A5; A5Y7A6; A5Y7A7; A5Y7A8; A5Y7A9;
AC A5Y7B0; A5Y7B1; A5Y7B2; A5Y7B3; A5Y7B4; A5Y7B5; A5Y7B6; Q9SBC5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 172.
DE RecName: Full=Transcription factor PIF3 {ECO:0000305};
DE AltName: Full=Basic helix-loop-helix protein 8 {ECO:0000303|PubMed:12679534};
DE Short=AtbHLH8 {ECO:0000303|PubMed:12679534};
DE Short=bHLH 8 {ECO:0000303|PubMed:12679534};
DE AltName: Full=Phytochrome-associated protein 3 {ECO:0000305};
DE AltName: Full=Phytochrome-interacting factor 3 {ECO:0000303|PubMed:9845368};
DE AltName: Full=Transcription factor EN 100 {ECO:0000305};
DE AltName: Full=bHLH transcription factor bHLH008 {ECO:0000305};
GN Name=PIF3 {ECO:0000303|PubMed:9845368};
GN Synonyms=BHLH8 {ECO:0000303|PubMed:12679534}, EN100 {ECO:0000305},
GN PAP3 {ECO:0000305};
GN OrderedLocusNames=At1g09530 {ECO:0000312|Araport:AT1G09530};
GN ORFNames=F14J9.19 {ECO:0000312|EMBL:AAC33213.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9845368; DOI=10.1016/s0092-8674(00)81636-0;
RA Ni M., Tepperman J.M., Quail P.H.;
RT "PIF3, a phytochrome-interacting factor necessary for normal photoinduced
RT signal transduction, is a novel basic helix-loop-helix protein.";
RL Cell 95:657-667(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY UV LIGHT, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lee J., Yi H., Shin B., Song P.-S., Choi G.;
RT "Identification and characterization of three phytochrome-associated
RT proteins.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-272, AND VARIANTS ASP-124; ASN-141;
RP HIS-176; LYS-186; LEU-209; ILE-220 AND ILE-236.
RC STRAIN=cv. An-2, cv. Bla-6, cv. Br-0, cv. Bu-2, cv. Columbia, cv. Di-1,
RC cv. Et-0, cv. Kl-1, cv. Li-5:3, cv. Ma-2, cv. Mt-0, cv. Pa-2, cv. Pi-0,
RC cv. Su-0, and cv. Tsu-1;
RX PubMed=17614917; DOI=10.1111/j.1365-294x.2007.03298.x;
RA Brock M.T., Tiffin P., Weinig C.;
RT "Sequence diversity and haplotype associations with phenotypic responses to
RT crowding: GIGANTEA affects fruit set in Arabidopsis thaliana.";
RL Mol. Ecol. 16:3050-3062(2007).
RN [8]
RP FUNCTION.
RX PubMed=10466729; DOI=10.1038/23500;
RA Ni M., Tepperman J.M., Quail P.H.;
RT "Binding of phytochrome B to its nuclear signalling partner PIF3 is
RT reversibly induced by light.";
RL Nature 400:781-784(1999).
RN [9]
RP FUNCTION.
RX PubMed=10797009; DOI=10.1126/science.288.5467.859;
RA Martinez-Garcia J.F., Huq E., Quail P.H.;
RT "Direct targeting of light signals to a promoter element-bound
RT transcription factor.";
RL Science 288:859-863(2000).
RN [10]
RP INTERACTION WITH APRR1.
RX PubMed=11828023; DOI=10.1093/pcp/pcf005;
RA Makino S., Matsushika A., Kojima M., Yamashino T., Mizuno T.;
RT "The APRR1/TOC1 quintet implicated in circadian rhythms of Arabidopsis
RT thaliana: I. Characterization with APRR1-overexpressing plants.";
RL Plant Cell Physiol. 43:58-69(2002).
RN [11]
RP GENE FAMILY, AND INTERACTION WITH PIF4.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [12]
RP FUNCTION.
RX PubMed=14508006; DOI=10.1105/tpc.014498;
RA Kim J., Yi H., Choi G., Shin B., Song P.S., Choi G.;
RT "Functional characterization of phytochrome interacting factor 3 in
RT phytochrome-mediated light signal transduction.";
RL Plant Cell 15:2399-2407(2003).
RN [13]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [14]
RP INTERACTION WITH APRR1.
RX PubMed=12826627; DOI=10.1093/pcp/pcg078;
RA Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S.,
RA Mizuno T.;
RT "A link between circadian-controlled bHLH factors and the APRR1/TOC1
RT quintet in Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:619-629(2003).
RN [15]
RP FUNCTION, INTERACTION WITH HDA15, AND SUBCELLULAR LOCATION.
RX PubMed=23548744; DOI=10.1105/tpc.113.109710;
RA Liu X., Chen C.Y., Wang K.C., Luo M., Tai R., Yuan L., Zhao M., Yang S.,
RA Tian G., Cui Y., Hsieh H.L., Wu K.;
RT "PHYTOCHROME INTERACTING FACTOR3 associates with the histone deacetylase
RT HDA15 in repression of chlorophyll biosynthesis and photosynthesis in
RT etiolated Arabidopsis seedlings.";
RL Plant Cell 25:1258-1273(2013).
RN [16]
RP INTERACTION WITH PIA2, AND PHOSPHORYLATION BY PHYA.
RC STRAIN=cv. Columbia;
RX PubMed=27143545; DOI=10.1093/jb/mvw031;
RA Yoo J., Cho M.-H., Lee S.-W., Bhoo S.H.;
RT "Phytochrome-interacting ankyrin repeat protein 2 modulates phytochrome A-
RT mediated PIF3 phosphorylation in light signal transduction.";
RL J. Biochem. 160:243-249(2016).
RN [17]
RP INTERACTION WITH TOPP4, AND PHOSPHORYLATION.
RX PubMed=26704640; DOI=10.1104/pp.15.01729;
RA Yue J., Qin Q., Meng S., Jing H., Gou X., Li J., Hou S.;
RT "TOPP4 regulates the stability of PHYTOCHROME INTERACTING FACTOR5 during
RT photomorphogenesis in Arabidopsis.";
RL Plant Physiol. 170:1381-1397(2016).
RN [18]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=29167353; DOI=10.1104/pp.17.01109;
RA Ma Q., Wang X., Sun J., Mao T.;
RT "Coordinated regulation of hypocotyl cell elongation by light and ethylene
RT through a microtubule destabilizing protein.";
RL Plant Physiol. 176:678-690(2018).
RN [19]
RP INTERACTION WITH FYPP1 AND FYPP3.
RX PubMed=31527236; DOI=10.1073/pnas.1907540116;
RA Yu X., Dong J., Deng Z., Jiang Y., Wu C., Qin X., Terzaghi W., Chen H.,
RA Dai M., Deng X.W.;
RT "Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress
RT photomorphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:20218-20225(2019).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, cv. En-2, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=31638649; DOI=10.1093/jxb/erz453;
RA Wang X., Ma Q., Wang R., Wang P., Liu Y., Mao T.;
RT "Submergence stress-induced hypocotyl elongation through ethylene
RT signaling-mediated regulation of cortical microtubules in Arabidopsis.";
RL J. Exp. Bot. 71:1067-1077(2020).
CC -!- FUNCTION: Transcription factor acting in the phytochrome signaling
CC pathway (PubMed:10466729, PubMed:14508006). Activates transcription by
CC binding to the G box (5'-CACGTG-3') (PubMed:10797009). Acts as a
CC negative regulator of phytochrome B signaling (PubMed:14508006).
CC Represses chlorophyll biosynthesis and photosynthesis in the dark
CC (PubMed:23548744). Recruits the histone deacetylase HDA15 to the
CC promoters of chlorophyll biosynthetic and photosynthetic genes
CC (PubMed:23548744). HDA15 represses their transcription by histone
CC deacetylation (PubMed:23548744). Promotes the expression of MDP60 to
CC modulate hypocotyl cell elongation in response to light and ethylene
CC signaling (PubMed:29167353). Required for submergence-induced and
CC ethylene-dependent underwater hypocotyl elongation (PubMed:31638649).
CC {ECO:0000269|PubMed:10466729, ECO:0000269|PubMed:10797009,
CC ECO:0000269|PubMed:14508006, ECO:0000269|PubMed:23548744,
CC ECO:0000269|PubMed:29167353, ECO:0000269|PubMed:31638649}.
CC -!- SUBUNIT: Homodimer (Probable). Can form a heterodimer with REP1 and
CC PIF4. Phytochrome B binds specifically to DNA-bound PIF3, but only upon
CC red light induced conversion to the Pfr form (PfrB). Reconversion to Pr
CC form causes rapid dissociation. Interacts with APRR1/TOC1. Binds to
CC PIA2; this interaction may trigger the repression of PHYA-mediated
CC phosphorylation (PubMed:27143545). Interacts with TOPP4
CC (PubMed:26704640, PubMed:11828023, PubMed:12826627, PubMed:12897250,
CC PubMed:27143545) (Probable). Interacts with FYPP1 AND FYPP3
CC (PubMed:31527236). Interacts with HDA15 in the dark (PubMed:23548744).
CC {ECO:0000269|PubMed:11828023, ECO:0000269|PubMed:12826627,
CC ECO:0000269|PubMed:12897250, ECO:0000269|PubMed:23548744,
CC ECO:0000269|PubMed:26704640, ECO:0000269|PubMed:27143545,
CC ECO:0000269|PubMed:31527236, ECO:0000305}.
CC -!- INTERACTION:
CC O80536; Q9FE22: HFR1; NbExp=6; IntAct=EBI-625701, EBI-626001;
CC O80536; P14712: PHYA; NbExp=8; IntAct=EBI-625701, EBI-624446;
CC O80536; P14713: PHYB; NbExp=22; IntAct=EBI-625701, EBI-300727;
CC O80536; Q8GZM7: PIF1; NbExp=6; IntAct=EBI-625701, EBI-630400;
CC O80536; O80536: PIF3; NbExp=3; IntAct=EBI-625701, EBI-625701;
CC O80536; Q8W2F3-2: PIF4; NbExp=3; IntAct=EBI-625701, EBI-625732;
CC O80536; Q9SLH3: RGA; NbExp=6; IntAct=EBI-625701, EBI-963624;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23548744}.
CC -!- INDUCTION: By UV treatment. {ECO:0000269|PubMed:12679534}.
CC -!- PTM: Phosphorylated by PHYA; this phosphorylation is repressed by PIA2.
CC {ECO:0000269|PubMed:27143545}.
CC -!- PTM: Dephosphorylated by TOPP4 during photomorphogenesis, leading to
CC subsequent degradation of PIF3 by the proteasomal pathway.
CC {ECO:0000269|PubMed:26704640}.
CC -!- DISRUPTION PHENOTYPE: Inhibited submergence-induced and ethylene-
CC dependent underwater hypocotyl elongation.
CC {ECO:0000269|PubMed:31638649}.
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DR EMBL; AF100166; AAC95156.1; -; mRNA.
DR EMBL; AF251693; AAL55715.1; -; mRNA.
DR EMBL; AF088280; AAC99771.1; -; mRNA.
DR EMBL; AC003970; AAC33213.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28457.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28458.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60410.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60411.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60412.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60413.1; -; Genomic_DNA.
DR EMBL; AK117255; BAC41930.1; -; mRNA.
DR EMBL; EF193482; ABP96435.1; -; Genomic_DNA.
DR EMBL; EF193483; ABP96436.1; -; Genomic_DNA.
DR EMBL; EF193484; ABP96437.1; -; Genomic_DNA.
DR EMBL; EF193485; ABP96438.1; -; Genomic_DNA.
DR EMBL; EF193486; ABP96439.1; -; Genomic_DNA.
DR EMBL; EF193487; ABP96440.1; -; Genomic_DNA.
DR EMBL; EF193488; ABP96441.1; -; Genomic_DNA.
DR EMBL; EF193489; ABP96442.1; -; Genomic_DNA.
DR EMBL; EF193490; ABP96443.1; -; Genomic_DNA.
DR EMBL; EF193491; ABP96444.1; -; Genomic_DNA.
DR EMBL; EF193492; ABP96445.1; -; Genomic_DNA.
DR EMBL; EF193493; ABP96446.1; -; Genomic_DNA.
DR EMBL; EF193494; ABP96447.1; -; Genomic_DNA.
DR EMBL; EF193495; ABP96448.1; -; Genomic_DNA.
DR EMBL; EF193496; ABP96449.1; -; Genomic_DNA.
DR PIR; H86228; H86228.
DR RefSeq; NP_001318964.1; NM_001331836.1.
DR RefSeq; NP_001318965.1; NM_001331837.1.
DR RefSeq; NP_001322700.1; NM_001331838.1.
DR RefSeq; NP_001322701.1; NM_001331839.1.
DR RefSeq; NP_172424.1; NM_100824.3.
DR RefSeq; NP_849626.1; NM_179295.3.
DR AlphaFoldDB; O80536; -.
DR SMR; O80536; -.
DR BioGRID; 22720; 34.
DR DIP; DIP-33892N; -.
DR IntAct; O80536; 18.
DR STRING; 3702.AT1G09530.2; -.
DR PaxDb; O80536; -.
DR PRIDE; O80536; -.
DR EnsemblPlants; AT1G09530.1; AT1G09530.1; AT1G09530.
DR EnsemblPlants; AT1G09530.2; AT1G09530.2; AT1G09530.
DR EnsemblPlants; AT1G09530.3; AT1G09530.3; AT1G09530.
DR EnsemblPlants; AT1G09530.4; AT1G09530.4; AT1G09530.
DR EnsemblPlants; AT1G09530.5; AT1G09530.5; AT1G09530.
DR EnsemblPlants; AT1G09530.6; AT1G09530.6; AT1G09530.
DR GeneID; 837479; -.
DR Gramene; AT1G09530.1; AT1G09530.1; AT1G09530.
DR Gramene; AT1G09530.2; AT1G09530.2; AT1G09530.
DR Gramene; AT1G09530.3; AT1G09530.3; AT1G09530.
DR Gramene; AT1G09530.4; AT1G09530.4; AT1G09530.
DR Gramene; AT1G09530.5; AT1G09530.5; AT1G09530.
DR Gramene; AT1G09530.6; AT1G09530.6; AT1G09530.
DR KEGG; ath:AT1G09530; -.
DR Araport; AT1G09530; -.
DR TAIR; locus:2012345; AT1G09530.
DR eggNOG; ENOG502QV9I; Eukaryota.
DR HOGENOM; CLU_014289_0_0_1; -.
DR InParanoid; O80536; -.
DR OMA; MVDEIPM; -.
DR OrthoDB; 583799at2759; -.
DR PhylomeDB; O80536; -.
DR PRO; PR:O80536; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80536; baseline and differential.
DR Genevisible; O80536; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009704; P:de-etiolation; IMP:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0031539; P:positive regulation of anthocyanin metabolic process; IMP:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0042548; P:regulation of photosynthesis, light reaction; IDA:UniProtKB.
DR GO; GO:1905421; P:regulation of plant organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR GO; GO:1990785; P:response to water-immersion restraint stress; IEP:UniProtKB.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR044273; PIF3-like.
DR PANTHER; PTHR46807; PTHR46807; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Phytochrome signaling pathway;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..524
FT /note="Transcription factor PIF3"
FT /id="PRO_0000127428"
FT DOMAIN 343..392
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 38..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 124
FT /note="E -> D (in strain: cv. An-2 and cv. Su-0)"
FT VARIANT 141
FT /note="K -> N (in strain: cv. An-2 and cv. Su-0)"
FT VARIANT 176
FT /note="Q -> H (in strain: cv. An-2 and cv. Su-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 186
FT /note="Q -> K (in strain: cv. An-2 and cv. Su-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 209
FT /note="F -> L (in strain: cv. An-2 and cv. Su-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 220
FT /note="T -> I (in strain: cv. An-2 and cv. Su-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 236
FT /note="V -> I (in strain: cv. An-2 and cv. Su-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT CONFLICT 15
FT /note="E -> D (in Ref. 3; AAC99771)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT CONFLICT 344
FT /note="S -> L (in Ref. 3; AAC99771)"
FT /evidence="ECO:0000269|PubMed:17614917"
SQ SEQUENCE 524 AA; 56990 MW; 1044AC01D598DE7C CRC64;
MPLFELFRLT KAKLESAQDR NPSPPVDEVV ELVWENGQIS TQSQSSRSRN IPPPQANSSR
AREIGNGSKT TMVDEIPMSV PSLMTGLSQD DDFVPWLNHH PSLDGYCSDF LRDVSSPVTV
NEQESDMAVN QTAFPLFQRR KDGNESAPAA SSSQYNGFQS HSLYGSDRAR DLPSQQTNPD
RFTQTQEPLI TSNKPSLVNF SHFLRPATFA KTTNNNLHDT KEKSPQSPPN VFQTRVLGAK
DSEDKVLNES VASATPKDNQ KACLISEDSC RKDQESEKAV VCSSVGSGNS LDGPSESPSL
SLKRKHSNIQ DIDCHSEDVE EESGDGRKEA GPSRTGLGSK RSRSAEVHNL SERRRRDRIN
EKMRALQELI PNCNKVDKAS MLDEAIEYLK SLQLQVQIMS MASGYYLPPA VMFPPGMGHY
PAAAAAMAMG MGMPYAMGLP DLSRGGSSVN HGPQFQVSGM QQQPVAMGIP RVSGGGIFAG
SSTIGNGSTR DLSGSKDQTT TNNNSNLKPI KRKQGSSDQF CGSS
