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AHL27_ARATH
ID   AHL27_ARATH             Reviewed;         311 AA.
AC   Q9S7C9; Q0WRK9;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=AT-hook motif nuclear-localized protein 27 {ECO:0000312|EMBL:FAA00298.1};
DE   AltName: Full=DNA-binding protein ESCAROLA {ECO:0000303|PubMed:10759496};
DE   AltName: Full=Protein ORESARA 7 {ECO:0000303|PubMed:17971039};
GN   Name=AHL27 {ECO:0000303|PubMed:15604740};
GN   Synonyms=ESC {ECO:0000312|EMBL:AAF07197.1},
GN   ORE7 {ECO:0000303|PubMed:17971039};
GN   OrderedLocusNames=At1g20900 {ECO:0000312|Araport:AT1G20900};
GN   ORFNames=F9H16.12 {ECO:0000312|EMBL:AAD30602.1};
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 [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10759496; DOI=10.1104/pp.122.4.1003;
RA   Weigel D., Ahn J.H., Blazquez M.A., Borevitz J.O., Christensen S.K.,
RA   Fankhauser C., Ferrandiz C., Kardailsky I., Malancharuvil E.J., Neff M.M.,
RA   Nguyen J.T., Sato S., Wang Z.Y., Xia Y., Dixon R.A., Harrison M.J.,
RA   Lamb C.J., Yanofsky M.F., Chory J.;
RT   "Activation tagging in Arabidopsis.";
RL   Plant Physiol. 122:1003-1013(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=15604740; DOI=10.1007/s11103-004-3249-5;
RA   Fujimoto S., Matsunaga S., Yonemura M., Uchiyama S., Azuma T., Fukui K.;
RT   "Identification of a novel plant MAR DNA binding protein localized on
RT   chromosomal surfaces.";
RL   Plant Mol. Biol. 56:225-239(2004).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17971039; DOI=10.1111/j.1365-313x.2007.03317.x;
RA   Lim P.O., Kim Y., Breeze E., Koo J.C., Woo H.R., Ryu J.S., Park D.H.,
RA   Beynon J., Tabrett A., Buchanan-Wollaston V., Nam H.G.;
RT   "Overexpression of a chromatin architecture-controlling AT-hook protein
RT   extends leaf longevity and increases the post-harvest storage life of
RT   plants.";
RL   Plant J. 52:1140-1153(2007).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18088311; DOI=10.1111/j.1365-313x.2007.03393.x;
RA   Street I.H., Shah P.K., Smith A.M., Avery N., Neff M.M.;
RT   "The AT-hook-containing proteins SOB3/AHL29 and ESC/AHL27 are negative
RT   modulators of hypocotyl growth in Arabidopsis.";
RL   Plant J. 54:1-14(2008).
RN   [10]
RP   FUNCTION.
RX   PubMed=19517252; DOI=10.1007/s11103-009-9507-9;
RA   Xiao C., Chen F., Yu X., Lin C., Fu Y.F.;
RT   "Over-expression of an AT-hook gene, AHL22, delays flowering and inhibits
RT   the elongation of the hypocotyl in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 71:39-50(2009).
RN   [11]
RP   FUNCTION.
RX   PubMed=20738724; DOI=10.1111/j.1744-7909.2010.00969.x;
RA   Lu H., Zou Y., Feng N.;
RT   "Overexpression of AHL20 negatively regulates defenses in Arabidopsis.";
RL   J. Integr. Plant Biol. 52:801-808(2010).
RN   [12]
RP   GENE FAMILY, MUTAGENESIS OF ARG-91, SUBUNIT, INTERACTION WITH AHL12; AHL25;
RP   AHL29; TCP4; TCP13; EF114; ATAF2/NAC081; H2B.1; H3.3 AND H4, AND DOMAIN
RP   PPC.
RX   PubMed=24218605; DOI=10.1073/pnas.1219277110;
RA   Zhao J., Favero D.S., Peng H., Neff M.M.;
RT   "Arabidopsis thaliana AHL family modulates hypocotyl growth redundantly by
RT   interacting with each other via the PPC/DUF296 domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E4688-E4697(2013).
CC   -!- FUNCTION: Transcription factor that specifically binds AT-rich DNA
CC       sequences related to the nuclear matrix attachment regions (MARs)
CC       (PubMed:17971039, PubMed:19517252). Negatively regulates plant innate
CC       immunity (PTI) to pathogens through the down-regulation of the PAMP-
CC       triggered FRK1 expression (PubMed:20738724). Acts redundantly with
CC       AHL18, AHL22 and AHL29 in the regulation of flowering and regulation of
CC       the hypocotyl elongation (PubMed:19517252). Acts as a chromatin
CC       remodeling factor that negatively regulates the leaf senescence
CC       (PubMed:17971039). Acts redundantly with AHL29/SOB3 to modulate
CC       hypocotyl growth inhibition in response to light (PubMed:18088311).
CC       {ECO:0000269|PubMed:17971039, ECO:0000269|PubMed:18088311,
CC       ECO:0000269|PubMed:19517252, ECO:0000269|PubMed:20738724}.
CC   -!- SUBUNIT: Homodimer. Interacts with AHL12, AHL25, AHL29, TCP4, TCP13,
CC       EF114, ATAF2/NAC081, histone H2B.1, histone H3.3 and histone H4.
CC       {ECO:0000269|PubMed:24218605}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17971039,
CC       ECO:0000269|PubMed:18088311}.
CC   -!- TISSUE SPECIFICITY: Expressed in the hypocotyl and the vascular tissue
CC       of seedling. {ECO:0000269|PubMed:18088311}.
CC   -!- DOMAIN: The PPC domain mediates interactions between AHL proteins.
CC       {ECO:0000269|PubMed:24218605}.
CC   -!- DISRUPTION PHENOTYPE: AHL27 and AHL29 double mutant exhibit a long
CC       hypocotyl phenotype in the light. {ECO:0000269|PubMed:18088311}.
CC   -!- MISCELLANEOUS: Overexpression of AHL27 results in a decreased flg22-
CC       induced expression of FRK1 (PubMed:20738724). Overexpression causes
CC       also delay of leaf senescence, late flowering and modified leaf
CC       development (PubMed:10759496, PubMed:17971039).
CC       {ECO:0000269|PubMed:10759496, ECO:0000269|PubMed:17971039,
CC       ECO:0000269|PubMed:20738724}.
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DR   EMBL; AF194974; AAF07197.1; -; mRNA.
DR   EMBL; AC007369; AAD30602.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30038.1; -; Genomic_DNA.
DR   EMBL; BT006460; AAP21268.1; -; mRNA.
DR   EMBL; AK228296; BAF00240.1; -; mRNA.
DR   EMBL; AB493469; BAH30307.1; -; mRNA.
DR   EMBL; BR000363; FAA00298.1; -; mRNA.
DR   PIR; F86341; F86341.
DR   RefSeq; NP_173514.1; NM_101943.2.
DR   AlphaFoldDB; Q9S7C9; -.
DR   SMR; Q9S7C9; -.
DR   BioGRID; 23922; 17.
DR   STRING; 3702.AT1G20900.1; -.
DR   PaxDb; Q9S7C9; -.
DR   PRIDE; Q9S7C9; -.
DR   ProteomicsDB; 244845; -.
DR   EnsemblPlants; AT1G20900.1; AT1G20900.1; AT1G20900.
DR   GeneID; 838683; -.
DR   Gramene; AT1G20900.1; AT1G20900.1; AT1G20900.
DR   KEGG; ath:AT1G20900; -.
DR   Araport; AT1G20900; -.
DR   TAIR; locus:2037350; AT1G20900.
DR   eggNOG; ENOG502QV94; Eukaryota.
DR   HOGENOM; CLU_039808_2_2_1; -.
DR   InParanoid; Q9S7C9; -.
DR   OMA; QMQHAPS; -.
DR   OrthoDB; 1350381at2759; -.
DR   PhylomeDB; Q9S7C9; -.
DR   PRO; PR:Q9S7C9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S7C9; baseline and differential.
DR   Genevisible; Q9S7C9; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR   GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR   GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:TAIR.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IMP:TAIR.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
DR   GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR   CDD; cd11378; DUF296; 1.
DR   InterPro; IPR014476; AHL15-29.
DR   InterPro; IPR005175; PPC_dom.
DR   PANTHER; PTHR31100; PTHR31100; 1.
DR   Pfam; PF03479; PCC; 1.
DR   PIRSF; PIRSF016021; ESCAROLA; 1.
DR   PROSITE; PS51742; PPC; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; DNA-binding; Flowering; Immunity; Innate immunity; Nucleus;
KW   Plant defense; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..311
FT                   /note="AT-hook motif nuclear-localized protein 27"
FT                   /id="PRO_0000087056"
FT   DOMAIN          110..258
FT                   /note="PPC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT   DNA_BIND        86..98
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          40..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..183
FT                   /note="Required for the binding to non-AHL interactors"
FT                   /evidence="ECO:0000269|PubMed:24218605"
FT   REGION          246..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         91
FT                   /note="R->H: In esc-11; Exhibits a long hypocotyl phenotype
FT                   in the light."
FT                   /evidence="ECO:0000269|PubMed:24218605"
SQ   SEQUENCE   311 AA;  31842 MW;  A80B445C9776EB7D CRC64;
     MEGGYEQGGG ASRYFHNLFR PEIHHQQLQP QGGINLIDQH HHQHQQHQQQ QQPSDDSRES
     DHSNKDHHQQ GRPDSDPNTS SSAPGKRPRG RPPGSKNKAK PPIIVTRDSP NALRSHVLEV
     SPGADIVESV STYARRRGRG VSVLGGNGTV SNVTLRQPVT PGNGGGVSGG GGVVTLHGRF
     EILSLTGTVL PPPAPPGAGG LSIFLAGGQG QVVGGSVVAP LIASAPVILM AASFSNAVFE
     RLPIEEEEEE GGGGGGGGGG GPPQMQQAPS ASPPSGVTGQ GQLGGNVGGY GFSGDPHLLG
     WGAGTPSRPP F
 
 
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