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Database: UniProt
Entry: F4K128
LinkDB: F4K128
Original site: F4K128 
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   31-JUL-2019, entry version 59.
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};
GN   OrderedLocusNames=At5g19310; ORFNames=F7K24.60;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   family 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
RT   remodeling ATPases cause embryogenesis and stem cell maintenance
RT   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
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza 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
RT   results 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
RT   ATPase genes.";
RL   Physiol. Plantarum 153:318-326(2015).
CC   -!- FUNCTION: Probable chromatin-remodeling factor that is
CC       functionally redundant with CHR12 in root and shoot stem cell
CC       initiation and root apical meristem (RAM) and shoot apical
CC       meristem (SAM) maintenance. Can associate with the promoter region
CC       of WOX5 (PubMed:23062007). May promote seed maturation and repress
CC       initiation of germination (PubMed:24839909). May repress plant
CC       growth (PubMed:24666886). {ECO:0000269|PubMed:23062007,
CC       ECO:0000269|PubMed:24666886, 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
CC       (RAM) and shoot apical meristem (SAM).
CC       {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}.
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   SMR; F4K128; -.
DR   BioGrid; 17327; 2.
DR   IntAct; F4K128; 1.
DR   STRING; 3702.AT5G19310.1; -.
DR   iPTMnet; F4K128; -.
DR   PaxDb; F4K128; -.
DR   PRIDE; F4K128; -.
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; ENOG410IUMP; Eukaryota.
DR   eggNOG; ENOG410XNUT; LUCA.
DR   InParanoid; F4K128; -.
DR   KO; K11647; -.
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: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:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
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   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_N; 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; Complete proteome;
KW   Developmental protein; Growth regulation; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1064       Probable ATP-dependent DNA helicase
FT                                CHR23.
FT                                /FTId=PRO_0000429440.
FT   DOMAIN      398    563       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      699    866       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     411    418       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       513    516       DEAH box.
FT   COMPBIAS    860   1027       Glu-rich.
FT   CONFLICT    118    118       G -> V (in Ref. 3; AY080694).
FT                                {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
//
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