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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
 
 
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