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SYD_ARATH
ID   SYD_ARATH               Reviewed;        3574 AA.
AC   F4IHS2; F4IHS3; F4IHS4; Q5BN47; Q8L9D7; Q9AUB4; Q9SL27;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Chromatin structure-remodeling complex protein SYD;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SYD;
DE   AltName: Full=Protein CHROMATIN REMODELING 3;
DE   AltName: Full=Protein SPLAYED;
GN   Name=SYD; Synonyms=CHR3; OrderedLocusNames=At2g28290; ORFNames=T3B23;
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP   MUTAGENESIS OF GLY-1153, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11818058; DOI=10.1016/s0960-9822(01)00651-0;
RA   Wagner D., Meyerowitz E.M.;
RT   "SPLAYED, a novel SWI/SNF ATPase homolog, controls reproductive development
RT   in Arabidopsis.";
RL   Curr. Biol. 12:85-94(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=16640604; DOI=10.1111/j.1365-313x.2006.02734.x;
RA   Su Y., Kwon C.S., Bezhani S., Huvermann B., Chen C., Peragine A.,
RA   Kennedy J.F., Wagner D.;
RT   "The N-terminal ATPase AT-hook-containing region of the Arabidopsis
RT   chromatin-remodeling protein SPLAYED is sufficient for biological
RT   activity.";
RL   Plant J. 46:685-699(2006).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3252-3574 (ISOFORM 3).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=15833920; DOI=10.1101/gad.1276305;
RA   Kwon C.S., Chen C., Wagner D.;
RT   "WUSCHEL is a primary target for transcriptional regulation by SPLAYED in
RT   dynamic control of stem cell fate in Arabidopsis.";
RL   Genes Dev. 19:992-1003(2005).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=16854978; DOI=10.1242/dev.02508;
RA   Kwon C.S., Hibara K., Pfluger J., Bezhani S., Metha H., Aida M., Tasaka M.,
RA   Wagner D.;
RT   "A role for chromatin remodeling in regulation of CUC gene expression in
RT   the Arabidopsis cotyledon boundary.";
RL   Development 133:3223-3230(2006).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17293567; DOI=10.1105/tpc.106.048272;
RA   Bezhani S., Winter C., Hershman S., Wagner J.D., Kennedy J.F., Kwon C.S.,
RA   Pfluger J., Su Y., Wagner D.;
RT   "Unique, shared, and redundant roles for the Arabidopsis SWI/SNF chromatin
RT   remodeling ATPases BRAHMA and SPLAYED.";
RL   Plant Cell 19:403-416(2007).
RN   [9]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [10]
RP   INTERACTION WITH BARD1/ROW1.
RX   PubMed=18591352; DOI=10.1105/tpc.108.058867;
RA   Han P., Li Q., Zhu Y.-X.;
RT   "Mutation of Arabidopsis BARD1 causes meristem defects by failing to
RT   confine WUSCHEL expression to the organizing center.";
RL   Plant Cell 20:1482-1493(2008).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY WOUNDING.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=19079584; DOI=10.1371/journal.ppat.1000237;
RA   Walley J.W., Rowe H.C., Xiao Y., Chehab E.W., Kliebenstein D.J., Wagner D.,
RA   Dehesh K.;
RT   "The chromatin remodeler SPLAYED regulates specific stress signaling
RT   pathways.";
RL   PLoS Pathog. 4:E1000237-E1000237(2008).
RN   [12]
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   [13]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH LFY.
RX   PubMed=22323601; DOI=10.1073/pnas.1113409109;
RA   Wu M.F., Sang Y., Bezhani S., Yamaguchi N., Han S.K., Li Z., Su Y.,
RA   Slewinski T.L., Wagner D.;
RT   "SWI2/SNF2 chromatin remodeling ATPases overcome polycomb repression and
RT   control floral organ identity with the LEAFY and SEPALLATA3 transcription
RT   factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3576-3581(2012).
RN   [14]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: Catalytic component of the chromatin structure-remodeling
CC       complex (RSC), which is involved in transcription regulation and
CC       nucleosome positioning. Controls stem cell fate via the transcription
CC       regulation of WUS in the shoot apical meristem, by modulating its
CC       promoter. LFY-dependent repressor of the meristem identity switch from
CC       vegetative to reproductive development probably by modulating chromatin
CC       state. Involved in the regulation of floral homeotic gene expression in
CC       response to environmental stimuli. Required for carpel and ovule
CC       development, and for cotyledon separation via the regulation of CUC2
CC       transcription. Regulates the promoters of several genes downstream of
CC       the jasmonate (JA) and ethylene (ET) signaling pathways. Required for
CC       resistance against the necrotrophic pathogen B.cinerea but not the
CC       biotrophic pathogen P.syringae. {ECO:0000269|PubMed:11818058,
CC       ECO:0000269|PubMed:15833920, ECO:0000269|PubMed:16640604,
CC       ECO:0000269|PubMed:16854978, ECO:0000269|PubMed:17293567,
CC       ECO:0000269|PubMed:19079584, ECO:0000269|PubMed:22323601}.
CC   -!- SUBUNIT: Interacts with LFY (PubMed:22323601). Binds to BARD1/ROW1
CC       (PubMed:18591352). {ECO:0000269|PubMed:18591352,
CC       ECO:0000269|PubMed:22323601}.
CC   -!- INTERACTION:
CC       F4IHS2; Q00958: LFY; NbExp=4; IntAct=EBI-15967899, EBI-1644366;
CC       F4IHS2; O22456: SEP3; NbExp=2; IntAct=EBI-15967899, EBI-592020;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=F4IHS2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4IHS2-2; Sequence=VSP_046250;
CC       Name=3;
CC         IsoId=F4IHS2-3; Sequence=VSP_046249;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in rapidly dividing cells in the
CC       vegetative, inflorescence, and root meristems, as well as in young leaf
CC       and flower primordia. Isoform 1 is predominantly found in seedlings
CC       whereas isoform 2 is present in both seedlings and inflorescences (at
CC       protein level). {ECO:0000269|PubMed:11818058,
CC       ECO:0000269|PubMed:16640604}.
CC   -!- INDUCTION: By wounding. {ECO:0000269|PubMed:19079584}.
CC   -!- PTM: Phosphorylated.
CC   -!- DISRUPTION PHENOTYPE: Precocious transition from inflorescence to
CC       flower formation and impaired maintenance of the shoot apical meristem
CC       (SAM) during the reproductive phase. Abnormal flowers with splayed open
CC       first-whorl sepals due to outward bending of the pointy sepal tips.
CC       Reduced male fertility and reduced anther dehiscence. Partially unfused
CC       at the tip fourth-whorl carpels, with stigmatic tissue missing or
CC       placed internal to the carpel tip, leading to funnel shaped carpels.
CC       Female sterility ovule growth arrest at megagametogenesis. Fused
CC       cotyledons. Impaired expression of PDF1.2a, leading to reduced ethylene
CC       (ET) and jasmonic acid (JA) signaling. Reduced resistance toward B.
CC       cinerea. {ECO:0000269|PubMed:11818058, ECO:0000269|PubMed:15833920,
CC       ECO:0000269|PubMed:16854978, ECO:0000269|PubMed:17293567,
CC       ECO:0000269|PubMed:19079584, ECO:0000269|PubMed:22323601}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD29835.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAM66026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF247809; AAK31908.1; -; mRNA.
DR   EMBL; AY927849; AAX22009.1; -; mRNA.
DR   EMBL; AC006202; AAD29835.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08099.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08100.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08101.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM63245.1; -; Genomic_DNA.
DR   EMBL; AY088490; AAM66026.1; ALT_INIT; mRNA.
DR   PIR; A84683; A84683.
DR   RefSeq; NP_001077971.1; NM_001084502.2. [F4IHS2-2]
DR   RefSeq; NP_001325347.1; NM_001336158.1. [F4IHS2-2]
DR   RefSeq; NP_850116.1; NM_179785.3. [F4IHS2-1]
DR   RefSeq; NP_850117.1; NM_179786.2. [F4IHS2-3]
DR   SMR; F4IHS2; -.
DR   BioGRID; 2725; 33.
DR   DIP; DIP-60019N; -.
DR   IntAct; F4IHS2; 2.
DR   STRING; 3702.AT2G28290.1; -.
DR   iPTMnet; F4IHS2; -.
DR   PaxDb; F4IHS2; -.
DR   PRIDE; F4IHS2; -.
DR   ProteomicsDB; 232978; -. [F4IHS2-1]
DR   EnsemblPlants; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
DR   EnsemblPlants; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
DR   EnsemblPlants; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
DR   EnsemblPlants; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
DR   GeneID; 817375; -.
DR   Gramene; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
DR   Gramene; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
DR   Gramene; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
DR   Gramene; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
DR   KEGG; ath:AT2G28290; -.
DR   Araport; AT2G28290; -.
DR   TAIR; locus:2062840; AT2G28290.
DR   eggNOG; KOG0386; Eukaryota.
DR   eggNOG; KOG1181; Eukaryota.
DR   InParanoid; F4IHS2; -.
DR   OMA; ITDHTTI; -.
DR   PRO; PR:F4IHS2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IHS2; baseline and differential.
DR   Genevisible; F4IHS2; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:TAIR.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI:TAIR.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR   GO; GO:0010104; P:regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR   GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; DNA-binding;
KW   Ethylene signaling pathway; Helicase; Hydrolase;
KW   Jasmonic acid signaling pathway; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Plant defense; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..3574
FT                   /note="Chromatin structure-remodeling complex protein SYD"
FT                   /id="PRO_0000421936"
FT   DOMAIN          573..647
FT                   /note="HSA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT   DOMAIN          766..933
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1077..1223
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          76..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1342..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1500..1575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1588..1637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1690..1811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1830..1868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2040..2068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2089..2115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2143..2162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2179..2220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2235..2338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2350..2451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2517..2538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2684..2703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2718..2759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2865..2884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3017..3045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3189..3208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3316..3337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3512..3574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           884..887
FT                   /note="DEAH box"
FT   MOTIF           1266..1273
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        79..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1356..1382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1436..1451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1500..1515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1554..1573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1593..1614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1690..1756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1772..1786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1795..1811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1836..1865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2040..2061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2089..2105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2179..2196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2285..2312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2322..2336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2371..2394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2403..2420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2432..2451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2517..2531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2718..2740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2741..2758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3316..3330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3519..3537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3538..3562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         779..786
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VAR_SEQ         3339..3383
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_046249"
FT   VAR_SEQ         3339..3369
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16640604"
FT                   /id="VSP_046250"
FT   MUTAGEN         1153
FT                   /note="G->E: In syd-1; precocious transition from
FT                   inflorescence to flower formation, abnormal flowers
FT                   exhibiting variable petals and stamens number and position
FT                   as well as some mosaic organs (stamenoid petals)."
FT                   /evidence="ECO:0000269|PubMed:11818058"
FT   CONFLICT        757
FT                   /note="Y -> E (in Ref. 1; AAK31908 and 2; AAX22009)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3574 AA;  389864 MW;  14209D18F717A69B CRC64;
     MTSSSHNIEL EAAKFLHKLI QDSKDEPAKL ATKLYVILQH MKTSGKENTM PYQVISRAMD
     TVVNQHGLDI EALKSSCLPH PGGTQTEDSG SAHLAGSSQA VGVSNEGKAT LVENEMTKYD
     AFTSGRQLGG SNSASQTFYQ GSGTQSNRSF DRESPSNLDS TSGISQPHNR SETMNQRDVK
     SSGKRKRGES SLSWDQNMDN SQIFDSHKID DQTGEVSKIE MPGNSGDIRN LHVGLSSDAF
     TTPQCGWQSS EATAIRPAIH KEPGNNVAGE GFLPSGSPFR EQQLKQLRAQ CLVFLALRNG
     LVPKKLHVEI ALRNTFREED GFRGELFDPK GRTHTSSDLG GIPDVSALLS RTDNPTGRLD
     EMDFSSKETE RSRLGEKSFA NTVFSDGQKL LASRIPSSQA QTQVAVSHSQ LTFSPGLTKN
     TPSEMVGWTG VIKTNDLSTS AVQLDEFHSS DEEEGNLQPS PKYTMSQKWI MGRQNKRLLV
     DRSWSLKQQK ADQAIGSRFN ELKESVSLSD DISAKTKSVI ELKKLQLLNL QRRLRSEFVY
     NFFKPIATDV EHLKSYKKHK HGRRIKQLEK YEQKMKEERQ RRIRERQKEF FGGLEVHKEK
     LEDLFKVRRE RLKGFNRYAK EFHKRKERLH REKIDKIQRE KINLLKINDV EGYLRMVQDA
     KSDRVKQLLK ETEKYLQKLG SKLKEAKLLT SRFENEADET RTSNATDDET LIENEDESDQ
     AKHYLESNEK YYLMAHSIKE NINEQPSSLV GGKLREYQMN GLRWLVSLYN NHLNGILADE
     MGLGKTVQVI SLICYLMETK NDRGPFLVVV PSSVLPGWQS EINFWAPSIH KIVYCGTPDE
     RRKLFKEQIV HQKFNVLLTT YEYLMNKHDR PKLSKIHWHY IIIDEGHRIK NASCKLNADL
     KHYVSSHRLL LTGTPLQNNL EELWALLNFL LPNIFNSSED FSQWFNKPFQ SNGESSAEEA
     LLSEEENLLI INRLHQVLRP FVLRRLKHKV ENELPEKIER LIRCEASAYQ KLLMKRVEDN
     LGSIGNAKSR AVHNSVMELR NICNHPYLSQ LHSEEVNNII PKHFLPPIVR LCGKLEMLDR
     MLPKLKATDH RVLFFSTMTR LLDVMEDYLT LKGYKYLRLD GQTSGGDRGA LIDGFNKSGS
     PFFIFLLSIR AGGVGVNLQA ADTVILFDTD WNPQVDLQAQ ARAHRIGQKK DVLVLRFETV
     NSVEEQVRAS AEHKLGVANQ SITAGFFDNN TSAEDRKEYL ESLLRESKKE EDAPVLDDDA
     LNDLIARRES EIDIFESIDK QRKENEMETW NTLVHGPGSD SFAHIPSIPS RLVTEDDLKL
     LYETMKLNDV PMVAKESTVG MKRKDGSMGG LDTHQYGRGK RAREVRSYEE KLTEEEFEKL
     CQTESPDSPQ GKGEGSERSL ANDTSNIPVE NSSDTLLPTS PTQAITVQPM EPVRPQSHTL
     KEETQPIKRG RGRPKRTDKA LTPVSLSAVS RTQATGNAIS SAATGLDFVS SDKRLEAASH
     PTSSLALTSP DLSGPPGFQS LPASPAPTPI RGRGRGRSRG RGAGRGRRVE GVLHGSNSSI
     TQRTETATSL ASDAEATKFA LPRSASEIVS RVPKANEGST SNPDQVSPVH SATTALRSDK
     AADKDLDAPP GFDSGSHVQT LNVLENSSER KAFAVKKRPL IQGVSSQHPG PNKQPLDLPV
     STSSTLLGGG PVQNQNAVSS VCDGSKSPSE GRTYTALQGV TTAPSDATLP MSSQPSDATL
     PMSSQPVGST VEAQEANVPS LPAALPAKRR VRNLPSRGET PKRQGKRRGQ PLPATDASSA
     RSTGLTPQIE VKVGNLSGTK AKFDAVAKEQ PHFSQSVAPD IHSSGSLSQE IRRDTSGTGG
     SARKQTADVT DVARVMKEIF SETSLLKHKV GEPSATTRTN VPDAQSPGEM NLHTVETHKA
     EDSSGLKNQE ALYNLSKADK LVSDIPHPVP GDLTTSGSVA NKDVDIGSSK VAAENELVKI
     PGGDVDSSVI QLSLGNTLTA KSSLEKCTAD QLLGEKLSQE GETTPASDGE TCHLAEETAS
     SLSYVRSEPT ASASTTAEPL PTDKLEKNIS FQDEVKTLNG DKREAILLSS EEQTNVNSKI
     ETNSEELQAS RTDEVPHVDG KSVDVANQTV KEDEAKHSVE IQSSMLEPDE LPNAGQKGHS
     SIDLQPLVLV TSNENAMSLD DKDYDPISKS ADIEQDPEES VFVQGVGRPK VGTADTQMED
     TNDAKLLVGC SVESEEKEKT LQSLIPGDDA DTEQDPEESV SDQRPKVGSA YTQMEDTDEA
     KLLMGCSVES EEKEKTLQSH IPGDDADTEK NPEESVSVQG VDRPKVGTTD TQMEDTNDAK
     LLVGCSVASE EKEKTLQSHI PGDDADTEQN PEESVSVQGV NRPKVGNANT QMEDTDEAKV
     LVGCSVESEE KEKTLQSHIP GDDADTEQNP EESVSNFDRP KDGTADTHME DIDDAKLLVG
     CSVESEEKEK SLQSHMPSDD AVLHAPFENT KDSKGDDLHG ESLVSCPTME VMEQKGFESE
     THARTDSGGI DRGNEVSENM SDGVKMNISS VQVPDASHDL NVSQDQTDIP LVGGIDPEHV
     QENVDVPASP HGAAPNIVIF QSEGHLSPSI LPDDVAGQLE SMSNDEKTNI SSEQVPDVSH
     DLKVSQDQTD IPPVGGIVPE NLQEIVDVPA SPHGVVPDVV VSQSEEIQSP SILPDDVPGQ
     PDDGNCEKMD TMQNNTSIDI GITSGKTCQP SSSTQPEDEN RNSLSHCEPS EVVEQRDSRD
     QVCIGSVESQ VEISSAILEN RSADIQPPQS ILVDQKDIEE SKEPGIESAD VSLHQLADIQ
     AEPSNLVDQM DIEESKEPGT ESADVSLHQL ADIQPGPSIL VDQMDTEKSK EPGTESADVS
     LHQLADIQPG PSILVDQMDT EKSKEPGTES ADVSLHQLAD IQPGPSILVD QMDTEEFKNP
     DVSLHQLADI EPSLSISAVQ KNIEDKDQSH VETAGSELVD VSAECSTEPQ VQLPPSSEPV
     GDMHVHLGAS KSEIVAEGTD FSSSLPKTEE ENAKSQLADT EPSSSLTAVQ KNIEDQVETA
     GCEFVVVSTG CSTEPQVQLP PSAEPVVAEG TEFPSSLLMT GVDNSSHLMT GVDNAKTHLA
     DVVPSSSPTT MEKNIEAQDQ DQVTTGGCGL VDVLTECSSE PQLQLPPSAE PVISEGTELA
     TLPLTEEENA DSQLANIEPS SSPSVVEKNI EAQDQDQVKT AGCELVSTGC SSEPQVHLPP
     SAEPDGDIHV HLKETEKSES MVVVGEGTAF PSSLPVTEEG NAESQLADTE PFTSPTVVEK
     NIKDQEQVET TGCGLVDDST GCSSEPQVQL PPSAEPMEGT HMHLEETKKS ETVVTEIQLA
     DIDPSFSLIV VQTNIEDQDQ IETGGCDLIN VPSGCSTEPQ IQLSSSAEPE EGMHIHLEAA
     MNSETVVTEG SELPSSLPMT EDENADGQLA EVEPSVSLTV EQTNIEEKDH IETAECELVD
     VSPGCSSQPE VKFPPSPDAV GGMDVHLETV VTEDTDSNSS LPKTEEKDAE NPSDRLDGES
     DGTTVATVEG TCVESNSLVA EESNIEVPKD NEDV
 
 
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