PIE1_ARATH
ID PIE1_ARATH Reviewed; 2055 AA.
AC Q7X9V2; Q9LTV5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1;
DE EC=3.6.4.12;
DE AltName: Full=Independent early flowering 1 protein;
DE AltName: Full=Protein CHROMATIN REMODELING 13 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR13;
GN Name=PIE1; Synonyms=CHR13 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At3g12810; ORFNames=MBK21.19;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12837955; DOI=10.1105/tpc.012161;
RA Noh Y.-S., Amasino R.M.;
RT "PIE1, an ISWI family gene, is required for FLC activation and floral
RT repression in Arabidopsis.";
RL Plant Cell 15:1671-1682(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene family
RT in DNA damage response and recombination.";
RL Genetics 173:985-994(2006).
RN [5]
RP INTERACTION WITH ARP6; SWC6 AND H2A.F/Z PROTEINS.
RX PubMed=17470967; DOI=10.1242/dev.001891;
RA Choi K., Park C., Lee J., Oh M., Noh B., Lee I.;
RT "Arabidopsis homologs of components of the SWR1 complex regulate flowering
RT and plant development.";
RL Development 134:1931-1941(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN THE SWR1 COMPLEX.
RX PubMed=17220196; DOI=10.1105/tpc.106.048447;
RA Deal R.B., Topp C.N., McKinney E.C., Meagher R.B.;
RT "Repression of flowering in Arabidopsis requires activation of FLOWERING
RT LOCUS C expression by the histone variant H2A.Z.";
RL Plant Cell 19:74-83(2007).
RN [7]
RP INTERACTION WITH SWC6 AND ARP6.
RX PubMed=17142478; DOI=10.1104/pp.106.092270;
RA March-Diaz R., Garcia-Dominguez M., Florencio F.J., Reyes J.C.;
RT "SEF, a new protein required for flowering repression in Arabidopsis,
RT interacts with PIE1 and ARP6.";
RL Plant Physiol. 143:893-901(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH H2A.F/Z PROTEINS.
RX PubMed=17988222; DOI=10.1111/j.1365-313x.2007.03361.x;
RA March-Diaz R., Garcia-Dominguez M., Lozano-Juste J., Leon J.,
RA Florencio F.J., Reyes J.C.;
RT "Histone H2A.Z and homologues of components of the SWR1 complex are
RT required to control immunity in Arabidopsis.";
RL Plant J. 53:475-487(2008).
RN [9]
RP FUNCTION, INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
RX PubMed=19121105; DOI=10.1111/j.1365-313x.2008.03776.x;
RA Choi J., Hyun Y., Kang M.J., In Yun H., Yun J.Y., Lister C., Dean C.,
RA Amasino R.M., Noh B., Noh Y.S., Choi Y.;
RT "Resetting and regulation of Flowering Locus C expression during
RT Arabidopsis reproductive development.";
RL Plant J. 57:918-931(2009).
RN [10]
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: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant H2A.F/Z leading
CC to transcriptional regulation of selected genes (e.g. FLC) by chromatin
CC remodeling. Probable DNA-dependent ATPase. Not involved in the
CC repression of FLC in gametophytes, but required for the reactivation of
CC FLC in early embryos and for the maintenance of full activation of FLC
CC in late embryos. {ECO:0000269|PubMed:12837955,
CC ECO:0000269|PubMed:17220196, ECO:0000269|PubMed:17988222,
CC ECO:0000269|PubMed:19121105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex composed of
CC at least ARP6/ESD1/SUF3, PIE1, SWC6, SWC2 and H2AZs (HTA8, HTA9,
CC HTA11). Interacts (via c-terminus) with SWC6 and ARP6 and (via N-
CC terminus) with H2AZs. {ECO:0000269|PubMed:17142478,
CC ECO:0000269|PubMed:17220196, ECO:0000269|PubMed:17470967,
CC ECO:0000269|PubMed:17988222}.
CC -!- INTERACTION:
CC Q7X9V2; Q8LGE3: ARP6; NbExp=4; IntAct=EBI-1537462, EBI-1537316;
CC Q7X9V2; Q9FHW2: SWC6; NbExp=4; IntAct=EBI-1537462, EBI-1537353;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
CC -!- TISSUE SPECIFICITY: Expressed in ovules, but not in stamens.
CC {ECO:0000269|PubMed:19121105}.
CC -!- INDUCTION: Not regulated by vernalization.
CC {ECO:0000269|PubMed:19121105}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. Loss of H2A.Z from chromatin.
CC {ECO:0000269|PubMed:12837955, ECO:0000269|PubMed:17220196}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY279398; AAP40633.1; -; mRNA.
DR EMBL; AB024033; BAB02425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75248.1; -; Genomic_DNA.
DR RefSeq; NP_187887.3; NM_112117.5.
DR AlphaFoldDB; Q7X9V2; -.
DR SMR; Q7X9V2; -.
DR BioGRID; 5797; 12.
DR IntAct; Q7X9V2; 6.
DR STRING; 3702.AT3G12810.1; -.
DR iPTMnet; Q7X9V2; -.
DR PaxDb; Q7X9V2; -.
DR PRIDE; Q7X9V2; -.
DR ProteomicsDB; 236732; -.
DR EnsemblPlants; AT3G12810.1; AT3G12810.1; AT3G12810.
DR GeneID; 820463; -.
DR Gramene; AT3G12810.1; AT3G12810.1; AT3G12810.
DR KEGG; ath:AT3G12810; -.
DR Araport; AT3G12810; -.
DR TAIR; locus:2087780; AT3G12810.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_13_1_1; -.
DR InParanoid; Q7X9V2; -.
DR OMA; VCWCSKS; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q7X9V2; -.
DR PRO; PR:Q7X9V2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7X9V2; baseline and differential.
DR Genevisible; Q7X9V2; AT.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0016514; C:SWI/SNF complex; ISS:TAIR.
DR GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 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.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; Developmental protein;
KW Differentiation; DNA-binding; Flowering; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..2055
FT /note="Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1"
FT /id="PRO_0000423729"
FT DOMAIN 35..107
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 548..713
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1076..1229
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1673..1727
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1843..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..147
FT /evidence="ECO:0000255"
FT COILED 229..250
FT /evidence="ECO:0000255"
FT COILED 392..416
FT /evidence="ECO:0000255"
FT COILED 1419..1492
FT /evidence="ECO:0000255"
FT COILED 2006..2029
FT /evidence="ECO:0000255"
FT MOTIF 29..36
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 664..667
FT /note="DEAH box"
FT MOTIF 1506..1513
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1570..1577
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 21..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 561..568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2055 AA; 234048 MW; ED38EC3C67D7F776 CRC64;
MASKGGKSKP DIVMASKSGK SKPDNESRAK RQKTLEAPKE PRRPKTHWDH VLEEMAWLSK
DFESERKWKL AQAKKVALRA SKGMLDQASR EERKLKEEEQ RLRKVALNIS KDMKKFWMKV
EKLVLYKHQL VRNEKKKKAM DKQLEFLLGQ TERYSTMLAE NLVEPYKQGQ NTPSKPLLTI
ESKSDEERAE QIPPEINSSA GLESGSPELD EDYDLKSEDE TEDDEDTIEE DEKHFTKRER
QEELEALQNE VDLPVEELLR RYTSGRVSRE TSPVKDENED NLTSVSRVTS PVKDENQDNL
ASVGQDHGED KNNLAASEET EGNPSVRRSN DSYGHLAISE THSHDLEPGM TTASVKSRKE
DHTYDFNDEQ EDVDFVLANG EEKDDEATLA VEEELAKADN EDHVEEIALL QKESEMPIEV
LLARYKEDFG GKDISEDESE SSFAVSEDSI VDSDENRQQA DLDDDNVDLT ECKLDPEPCS
ENVEGTFHEV AEDNDKDSSD KIADAAAAAR SAQPTGFTYS TTKVRTKLPF LLKHSLREYQ
HIGLDWLVTM YEKKLNGILA DEMGLGKTIM TIALLAHLAC DKGIWGPHLI VVPTSVMLNW
ETEFLKWCPA FKILTYFGSA KERKLKRQGW MKLNSFHVCI TTYRLVIQDS KMFKRKKWKY
LILDEAHLIK NWKSQRWQTL LNFNSKRRIL LTGTPLQNDL MELWSLMHFL MPHVFQSHQE
FKDWFCNPIA GMVEGQEKIN KEVIDRLHNV LRPFLLRRLK RDVEKQLPSK HEHVIFCRLS
KRQRNLYEDF IASTETQATL TSGSFFGMIS IIMQLRKVCN HPDLFEGRPI VSSFDMAGID
VQLSSTICSL LLESPFSKVD LEALGFLFTH LDFSMTSWEG DEIKAISTPS ELIKQRVNLK
DDLEAIPLSP KNRKNLQGTN IFEEIRKAVF EERIQESKDR AAAIAWWNSL RCQRKPTYST
SLRTLLTIKG PLDDLKANCS SYMYSSILAD IVLSPIERFQ KMIELVEAFT FAIPAARVPS
PTCWCSKSDS PVFLSPSYKE KVTDLLSPLL SPIRPAIVRR QVYFPDRRLI QFDCGKLQEL
AMLLRKLKFG GHRALIFTQM TKMLDVLEAF INLYGYTYMR LDGSTPPEER QTLMQRFNTN
PKIFLFILST RSGGVGINLV GADTVIFYDS DWNPAMDQQA QDRCHRIGQT REVHIYRLIS
ESTIEENILK KANQKRVLDN LVIQNGEYNT EFFKKLDPME LFSGHKALTT KDEKETSKHC
GADIPLSNAD VEAALKQAED EADYMALKRV EQEEAVDNQE FTEEPVERPE DDELVNEDDI
KADEPADQGL VAAGPAKEEM SLLHSDIRDE RAVITTSSQE DDTDVLDDVK QMAAAAADAG
QAISSFENQL RPIDRYAIRF LELWDPIIVE AAMENEAGFE EKEWELDHIE KYKEEMEAEI
DDGEEPLVYE KWDADFATEA YRQQVEVLAQ HQLMEDLENE AREREAAEVA EMVLTQNESA
HVLKPKKKKK AKKAKYKSLK KGSLAAESKH VKSVVKIEDS TDDDNEEFGY VSSSDSDMVT
PLSRMHMKGK KRDLIVDTDE EKTSKKKAKK HKKSLPNSDI KYKQTSALLD ELEPSKPSDS
MVVDNELKLT NRGKTVGKKF ITSMPIKRVL MIKPEKLKKG NLWSRDCVPS PDSWLPQEDA
ILCAMVHEYG PNWNFVSGTL YGMTAGGAYR GRYRHPAYCC ERYRELIQRH ILSASDSAVN
EKNLNTGSGK ALLKVTEENI RTLLNVAAEQ PDTEMLLQKH FSCLLSSIWR TSTRTGNDQM
LSLNSPIFNR QFMGSVNHTQ DLARKPWQGM KVTSLSRKLL ESALQDSGPS QPDNTISRSR
LQETQPINKL GLELTLEFPR GNDDSLNQFP PMISLSIDGS DSLNYVNEPP GEDVLKGSRV
AAENRYRNAA NACIEDSFGW ASNTFPANDL KSRTGTKAQS LGKHKLSASD SAKSTKSKHR
KLLAEQLEGA WVRPNDPNLK FDFTPGDREE EEEQEVDEKA NSAEIEMISC SQWYDPFFTS
GLDDCSLASD ISEIE
