CHR12_ARATH
ID CHR12_ARATH Reviewed; 1102 AA.
AC F4J9M5; Q9SFG5;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable ATP-dependent DNA helicase CHR12;
DE EC=3.6.4.12;
DE AltName: Full=Protein CHROMATIN REMODELING 12 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR12 {ECO:0000303|PubMed:17605754};
DE AltName: Full=Protein MINUSCULE 1 {ECO:0000303|PubMed:23062007};
GN Name=CHR12 {ECO:0000303|PubMed:16547115};
GN Synonyms=MINU1 {ECO:0000303|PubMed:23062007}; OrderedLocusNames=At3g06010;
GN ORFNames=F2O10.3;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17605754; DOI=10.1111/j.1365-313x.2007.03185.x;
RA Mlynarova L., Nap J.-P., Bisseling T.;
RT "The SWI/SNF chromatin-remodeling gene AtCHR12 mediates temporary growth
RT arrest in Arabidopsis thaliana upon perceiving environmental stress.";
RL Plant J. 51:874-885(2007).
RN [5]
RP FUNCTION, AND DISRUPTION 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=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 CHR23 in root and shoot stem cell initiation, and root
CC apical meristem (RAM) and shoot apical meristem (SAM) maintenance.
CC Plays an important role in mediating the temporary plant growth arrest
CC induced upon perception of stress (PubMed:17605754, PubMed:23062007).
CC May promote seed maturation and repress initiation of germination
CC (PubMed:24839909). {ECO:0000269|PubMed:17605754,
CC ECO:0000269|PubMed:23062007, 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:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in root endodermis, cotyledons, young
CC buds, developing cauline leaves, rosette and cauline leaf stipules,
CC sepals of young flower buds, stigma and seeds.
CC {ECO:0000269|PubMed:17605754}.
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:17605754, ECO:0000269|PubMed:23062007}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23228.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013454; AAF23228.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74329.1; -; Genomic_DNA.
DR RefSeq; NP_187252.2; NM_111475.3.
DR AlphaFoldDB; F4J9M5; -.
DR SMR; F4J9M5; -.
DR BioGRID; 5107; 12.
DR STRING; 3702.AT3G06010.1; -.
DR iPTMnet; F4J9M5; -.
DR PaxDb; F4J9M5; -.
DR PRIDE; F4J9M5; -.
DR ProteomicsDB; 246783; -.
DR EnsemblPlants; AT3G06010.1; AT3G06010.1; AT3G06010.
DR GeneID; 819772; -.
DR Gramene; AT3G06010.1; AT3G06010.1; AT3G06010.
DR KEGG; ath:AT3G06010; -.
DR Araport; AT3G06010; -.
DR TAIR; locus:2083033; AT3G06010.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; F4J9M5; -.
DR OMA; FNTSIQH; -.
DR OrthoDB; 685477at2759; -.
DR PRO; PR:F4J9M5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J9M5; baseline and differential.
DR Genevisible; F4J9M5; 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: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:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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..1102
FT /note="Probable ATP-dependent DNA helicase CHR12"
FT /id="PRO_0000429439"
FT DOMAIN 415..581
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 717..884
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 55..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..534
FT /note="DEAH box"
FT COMPBIAS 1010..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428..435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1102 AA; 126735 MW; 813A6CFB0EBA624D CRC64;
MVAQQLQERC GGTSQEDPVE TTKSLICALN YISRDLPLPP HLFTAVSSIY HGASSSSLSD
SDVSPPLPTS PPANKAPYGA DLMGEFEDAL LKQRPDCESG SRLIQLLDNR NKSHIQRRLS
ELEELPSTRG EDLQAKCLLE LYGLKLRELQ GKVRTAVSSE FWLRLNCADV SSQVFDWGMM
RLPRPFYGVG DPFAMEADDQ FRKKRDAERL SRLEEEEKNL IETAKRKFFA EVLNAVREFQ
LQIQATQKRR RQRNDGVQAW HGRQRQRATR AEKLRLMALK SDDQEAYMKL VKESKNERLT
TLLEETNKLL ANLGAAVQRQ KDAKLPEGID LLKDSESDLS ELDAPRSEPL QDLLPDQDID
ITESDNNDDS NDLLEGQRQY NSAIHSIQEK VTEQPSLLEG GELRSYQLEG LQWMVSLFNN
NLNGILADEM GLGKTIQTIS LIAYLLENKG VPGPYLIVAP KAVLPNWVNE FATWVPSIAA
FLYDGRLEER KAIREKIAGE GKFNVLITHY DLIMRDKAFL KKIEWYYMIV DEGHRLKNHE
SALAKTLLTG YRIKRRLLLT GTPIQNSLQE LWSLLNFLLP HIFNSVQNFE EWFNAPFADR
GNVSLTDEEE LLIIHRLHHV IRPFILRRKK DEVEKFLPGK TQVILKCDMS AWQKVYYKQV
TDMGRVGLQT GSGKSKSLQN LTMQLRKCCN HPYLFVGGDY NMWKKPEIVR ASGKFELLDR
LLPKLRKAGH RILLFSQMTR LIDVLEIYLT LNDYKYLRLD GTTKTDQRGL LLKQFNEPDS
PYFMFLLSTR AGGLGLNLQT ADTVIIFDSD WNPQMDQQAE DRAHRIGQKK EVRVFVLVSV
GSVEEVILER AKQKMGIDAK VIQAGLFNTT STAQDRREML EEIMRKGTSS LGTDVPSERE
INRLAARSED EFWMFERMDE ERRRKENYRA RLMQEQEVPE WAYTTQTQEE KLNNGKFHFG
SVTGKRKRKE IVYSDTLSEL QWLKAVESGE DLSKLSMRYN RREENASNTK TSTSKKVIES
IQTVSDGTSE EDEEEQEEER AKEMSGKQRV DKSEEEEEEG EEENDGKAIF KWNTHKKKRS
RYSFTCSSSD SRAQSSNGSR RK
