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OFP1_ARATH
ID   OFP1_ARATH              Reviewed;         270 AA.
AC   Q9LZW2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Transcription repressor OFP1;
DE   AltName: Full=Ovate family protein 1;
DE            Short=AtOFP1;
GN   Name=OFP1; OrderedLocusNames=At5g01840; ORFNames=T20L15.110;
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   FUNCTION, INTERACTION WITH ATH1; BLH1; BLH2; BLH3; BLH4; BLH5; BLH10;
RP   KNAT1; KNAT3; KNAT4; KNAT5 AND KNAT7, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15781858; DOI=10.1073/pnas.0501181102;
RA   Hackbusch J., Richter K., Muller J., Salamini F., Uhrig J.F.;
RT   "A central role of Arabidopsis thaliana ovate family proteins in networking
RT   and subcellular localization of 3-aa loop extension homeodomain proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4908-4912(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17461792; DOI=10.1111/j.1365-313x.2007.03096.x;
RA   Wang S., Chang Y., Guo J., Chen J.G.;
RT   "Arabidopsis Ovate Family Protein 1 is a transcriptional repressor that
RT   suppresses cell elongation.";
RL   Plant J. 50:858-872(2007).
RN   [5]
RP   FUNCTION, INTERACTION WITH KU70, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20844935; DOI=10.1007/s11103-010-9685-5;
RA   Wang Y.K., Chang W.C., Liu P.F., Hsiao M.K., Lin C.T., Lin S.M., Pan R.L.;
RT   "Ovate family protein 1 as a plant Ku70 interacting protein involving in
RT   DNA double-strand break repair.";
RL   Plant Mol. Biol. 74:453-466(2010).
RN   [6]
RP   FUNCTION, INTERACTION WITH KNAT7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=21457372; DOI=10.1111/j.1365-313x.2011.04595.x;
RA   Li E., Wang S., Liu Y., Chen J.G., Douglas C.J.;
RT   "OVATE FAMILY PROTEIN4 (OFP4) interaction with KNAT7 regulates secondary
RT   cell wall formation in Arabidopsis thaliana.";
RL   Plant J. 67:328-341(2011).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND DISRUPTION PHENOTYPE.
RX   PubMed=21886836; DOI=10.1371/journal.pone.0023896;
RA   Wang S., Chang Y., Guo J., Zeng Q., Ellis B.E., Chen J.G.;
RT   "Arabidopsis ovate family proteins, a novel transcriptional repressor
RT   family, control multiple aspects of plant growth and development.";
RL   PLoS ONE 6:E23896-E23896(2011).
CC   -!- FUNCTION: Transcriptional repressor that regulates multiple aspects of
CC       plant growth and development through the regulation of BEL1-LIKE (BLH)
CC       and KNOX TALE (KNAT) homeodomain transcription factors. Controls the
CC       subcellular localization of the homeodomain protein BLH1. Plays a role
CC       in the regulation of cell elongation by controlling the expression of
CC       GA20OX1, a gene that encodes a key enzyme in gibberellin biosynthesis.
CC       May play a role in double-stranded DNA repair through the DNA non-
CC       homologous end joining (NHEJ) pathway along with KU70 and KU80 protein
CC       complex. Possesses DNA-binding activity towards double-stranded and
CC       single-stranded DNA in vitro. {ECO:0000269|PubMed:15781858,
CC       ECO:0000269|PubMed:17461792, ECO:0000269|PubMed:20844935,
CC       ECO:0000269|PubMed:21457372, ECO:0000269|PubMed:21886836}.
CC   -!- SUBUNIT: Interacts with ATH1, BLH1, BLH2, BLH3, BLH4, BLH5, BLH10,
CC       KNAT1, KNAT3, KNAT4, KNAT5, KNAT7 and KU70.
CC       {ECO:0000269|PubMed:15781858, ECO:0000269|PubMed:20844935,
CC       ECO:0000269|PubMed:21457372}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15781858,
CC       ECO:0000269|PubMed:17461792, ECO:0000269|PubMed:21457372}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, xylem of stems, flower buds and
CC       siliques. {ECO:0000269|PubMed:17461792, ECO:0000269|PubMed:21457372,
CC       ECO:0000269|PubMed:21886836}.
CC   -!- INDUCTION: By the DNA-damaging agents methyl methanesulfonate (MMS) and
CC       menadione. {ECO:0000269|PubMed:20844935}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants are hypersensitive to the DNA-damaging
CC       agents methyl methanesulfonate (MMS) and menadione.
CC       {ECO:0000269|PubMed:15781858, ECO:0000269|PubMed:17461792,
CC       ECO:0000269|PubMed:20844935, ECO:0000269|PubMed:21457372,
CC       ECO:0000269|PubMed:21886836}.
CC   -!- MISCELLANEOUS: Plants over-expressing OFP1 show stunted growth with
CC       general delayed development and shortening and thickening of all aerial
CC       parts. Leaves are irregularly heart-shaped and lobed and display curved
CC       surfaces. Anthers are short with a thick filament and style and stigma
CC       protruded from the flower. Siliques are short and uneven and produce
CC       few seeds (PubMed:15781858 and PubMed:21886836).
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DR   EMBL; AL162351; CAB82754.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90399.1; -; Genomic_DNA.
DR   PIR; T48205; T48205.
DR   RefSeq; NP_195804.1; NM_120262.3.
DR   AlphaFoldDB; Q9LZW2; -.
DR   SMR; Q9LZW2; -.
DR   BioGRID; 17089; 16.
DR   IntAct; Q9LZW2; 13.
DR   STRING; 3702.AT5G01840.1; -.
DR   PaxDb; Q9LZW2; -.
DR   PRIDE; Q9LZW2; -.
DR   ProteomicsDB; 250887; -.
DR   EnsemblPlants; AT5G01840.1; AT5G01840.1; AT5G01840.
DR   GeneID; 831813; -.
DR   Gramene; AT5G01840.1; AT5G01840.1; AT5G01840.
DR   KEGG; ath:AT5G01840; -.
DR   Araport; AT5G01840; -.
DR   TAIR; locus:2180977; AT5G01840.
DR   eggNOG; ENOG502RTS2; Eukaryota.
DR   HOGENOM; CLU_036558_0_0_1; -.
DR   InParanoid; Q9LZW2; -.
DR   OMA; CLNSDEY; -.
DR   OrthoDB; 1209787at2759; -.
DR   PhylomeDB; Q9LZW2; -.
DR   PRO; PR:Q9LZW2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZW2; baseline and differential.
DR   Genevisible; Q9LZW2; AT.
DR   GO; GO:0005856; C:cytoskeleton; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:TAIR.
DR   InterPro; IPR025830; DNA_bnd_dom_ovate.
DR   InterPro; IPR038933; Ovate.
DR   InterPro; IPR006458; Ovate_C.
DR   PANTHER; PTHR33057; PTHR33057; 1.
DR   Pfam; PF13724; DNA_binding_2; 1.
DR   Pfam; PF04844; Ovate; 1.
DR   TIGRFAMs; TIGR01568; A_thal_3678; 1.
DR   PROSITE; PS51754; OVATE; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..270
FT                   /note="Transcription repressor OFP1"
FT                   /id="PRO_0000429670"
FT   DOMAIN          202..261
FT                   /note="OVATE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01090"
FT   REGION          25..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           28..45
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           260..264
FT                   /note="LxLxL"
FT   COMPBIAS        30..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30030 MW;  C2A2058809257C39 CRC64;
     MGNNYRFKLS ELIPNAWFYK LRDMSKSKKK NLQSQPNSTT SKKKHHAVPT PTSTTPLSPR
     PPRRPSHSSK APPSHPPRKS SGNRLRHRAT VDSKSSTTSG DSTTTETGSF SPDFRSDQVL
     LPDESLTGSW HSPCSSKLSK TATFTPPPEL ELRPIITKTA ATARKTAVNS PAGVRLRMRS
     PRISVSSSAR RSGSSARRSR AVVKASVDPK RDFKESMEEM IAENKIRATK DLEELLACYL
     CLNSDEYHAI IINVFKQIWL DLNLPPPHSK
 
 
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