CHR23_ARATH
ID CHR23_ARATH Reviewed; 1064 AA.
AC F4K128;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable ATP-dependent DNA helicase CHR23;
DE EC=3.6.4.12;
DE AltName: Full=Protein CHROMATIN REMODELING 23 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR23 {ECO:0000303|PubMed:24666886};
DE AltName: Full=Protein MINUSCULE 2 {ECO:0000303|PubMed:23062007};
GN Name=CHR23 {ECO:0000303|PubMed:16547115};
GN Synonyms=MINU2 {ECO:0000303|PubMed:23062007}; OrderedLocusNames=At5g19310;
GN ORFNames=F7K24.60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] OF 1-612.
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 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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23062007; DOI=10.1111/tpj.12009;
RA Sang Y., Silva-Ortega C.O., Wu S., Yamaguchi N., Wu M.F., Pfluger J.,
RA Gillmor C.S., Gallagher K.L., Wagner D.;
RT "Mutations in two non-canonical Arabidopsis SWI2/SNF2 chromatin remodeling
RT ATPases cause embryogenesis and stem cell maintenance defects.";
RL Plant J. 72:1000-1014(2012).
RN [6]
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).
RN [7]
RP FUNCTION.
RX PubMed=24666886; DOI=10.1186/1471-2229-14-76;
RA Folta A., Severing E.I., Krauskopf J., van de Geest H., Verver J.,
RA Nap J.P., Mlynarova L.;
RT "Over-expression of Arabidopsis AtCHR23 chromatin remodeling ATPase results
RT in increased variability of growth and gene expression.";
RL BMC Plant Biol. 14:76-76(2014).
RN [8]
RP FUNCTION.
RX PubMed=24839909; DOI=10.1111/ppl.12231;
RA Leeggangers H.A., Folta A., Muras A., Nap J.P., Mlynarova L.;
RT "Reduced seed germination in Arabidopsis over-expressing SWI/SNF2 ATPase
RT genes.";
RL Physiol. Plantarum 153:318-326(2015).
CC -!- FUNCTION: Probable chromatin-remodeling factor that is functionally
CC redundant with CHR12 in root and shoot stem cell initiation and root
CC apical meristem (RAM) and shoot apical meristem (SAM) maintenance. Can
CC associate with the promoter region of WOX5 (PubMed:23062007). May
CC promote seed maturation and repress initiation of germination
CC (PubMed:24839909). May repress plant growth (PubMed:24666886).
CC {ECO:0000269|PubMed:23062007, ECO:0000269|PubMed:24666886,
CC ECO:0000269|PubMed:24839909}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23062007}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, root apical meristem (RAM)
CC and shoot apical meristem (SAM). {ECO:0000269|PubMed:23062007}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but double mutant plants chr12 and chr23 are embryonic
CC lethal. {ECO:0000269|PubMed:23062007}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92683.1; -; Genomic_DNA.
DR EMBL; AY080694; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_197432.2; NM_121936.3.
DR AlphaFoldDB; F4K128; -.
DR SMR; F4K128; -.
DR BioGRID; 17327; 12.
DR IntAct; F4K128; 1.
DR STRING; 3702.AT5G19310.1; -.
DR iPTMnet; F4K128; -.
DR PaxDb; F4K128; -.
DR PRIDE; F4K128; -.
DR ProteomicsDB; 247001; -.
DR EnsemblPlants; AT5G19310.1; AT5G19310.1; AT5G19310.
DR GeneID; 832051; -.
DR Gramene; AT5G19310.1; AT5G19310.1; AT5G19310.
DR KEGG; ath:AT5G19310; -.
DR Araport; AT5G19310; -.
DR TAIR; locus:2150270; AT5G19310.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; F4K128; -.
DR OrthoDB; 685477at2759; -.
DR PhylomeDB; F4K128; -.
DR PRO; PR:F4K128; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K128; baseline and differential.
DR Genevisible; F4K128; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0010231; P:maintenance of seed dormancy; IMP:UniProtKB.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IMP: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; 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; SM01314; SnAC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromatin regulator; Developmental protein; Growth regulation;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1064
FT /note="Probable ATP-dependent DNA helicase CHR23"
FT /id="PRO_0000429440"
FT DOMAIN 398..563
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 699..866
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 924..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 513..516
FT /note="DEAH box"
FT COMPBIAS 927..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1018
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 118
FT /note="G -> V (in Ref. 3; AY080694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 122887 MW; BEDFFEC4815B0BED CRC64;
MVKQLQEQEE NDPVEKTKSL ISALNYLSRD LLLPSHLYAS VSSIYHASVS DLSPSPPLRG
NSYTPNRGDL MSEFEDALLQ QRLNYESGSR LAELKETRYK NRIHNRLSQL EGLPSNRGED
LQEKCLLELY GLKLQELQCR VRGEVSAEYW LRLNCADPER QLYDWGMMRL PRRMYGVGDS
FVMEADDQFR NKRDAERLLR LEEEEKNLIE TTQRKFFAEV LNAVREFQLQ IQASHRRCKQ
RNDGVQAWHG KQRQRATRAE KLRIMALKSD DQEEYMKLAK ESKNEKLTLF LEETNKIFVS
LGAAVQRQKD AKLSENTKLL KGSESDLSDV DAPEDVLPAQ DIEIIDSDNN DDSNDLLEGE
RQFNLAIHSI QEKVTKQPSL LQGGELRSYQ LEGLQWMVSL YNNDYNGILA DEMGLGKTIQ
TIALIAYLLE SKDLHGPHLI LAPKAVLPNW ENEFALWAPS ISAFLYDGSK EKRTEIRARI
AGGKFNVLIT HYDLIMRDKA FLKKIDWNYM IVDEGHRLKN HECALAKTLG TGYRIKRRLL
LTGTPIQNSL QELWSLLNFL LPHIFNSIHN FEEWFNTPFA ECGSASLTDE EELLIINRLH
HVIRPFLLRR KKSEVEKFLP GKTQVILKCD MSAWQKLYYK QVTDVGRVGL HSGNGKSKSL
QNLTMQLRKC CNHPYLFVGA DYNMCKKPEI VRASGKFELL DRLLPKLKKA GHRILLFSQM
TRLIDLLEIY LSLNDYMYLR LDGSTKTDQR GILLKQFNEP DSPYFMFLLS TRAGGLGLNL
QTADTIIIFD SDWNPQMDQQ AEDRAHRIGQ KKEVRVFVLV SIGSIEEVIL ERAKQKMGID
AKVIQAGLFN TTSTAQDRRE MLEEIMSKGT SSLGEDVPSE REINRLAART EEEFWMFEQM
DEERRKKENY KTRLMEEKEV PEWAYTSETQ EDKTNAKNHF GSLTGKRKRK EAVYSDSLSD
LQWMKAMESE DEDASKVSQK RKRTDTKTRM SNGSKAEAVL SESDEEKEEE EEERKEESGK
ESEEENEKPL HSWKTNKKKR SRYPVMTSSP NSRGKGSSKG SKRN
