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AHL22_ARATH
ID   AHL22_ARATH             Reviewed;         317 AA.
AC   O22130;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=AT-hook motif nuclear-localized protein 22 {ECO:0000312|EMBL:FAA00293.1};
GN   Name=AHL22 {ECO:0000303|PubMed:15604740};
GN   OrderedLocusNames=At2g45430 {ECO:0000312|Araport:AT2G45430};
GN   ORFNames=F4L23.6 {ECO:0000312|EMBL:AAB82621.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
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   [7]
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   HDA1/HDA19; HDA6 AND HDA9, AND SUBUNIT.
RX   PubMed=22442143; DOI=10.1074/jbc.m111.318477;
RA   Yun J., Kim Y.S., Jung J.H., Seo P.J., Park C.M.;
RT   "The AT-hook motif-containing protein AHL22 regulates flowering initiation
RT   by modifying FLOWERING LOCUS T chromatin in Arabidopsis.";
RL   J. Biol. Chem. 287:15307-15316(2012).
RN   [8]
RP   GENE FAMILY, AND DOMAIN 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       Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter
CC       (PubMed:22442143). Acts redundantly with AHL18, AHL27 and AHL29 in the
CC       regulation of flowering and regulation of the hypocotyl elongation.
CC       Plays a role in both photo- and skotomorphogenesis (PubMed:19517252).
CC       Acts as a chromatin remodeling factor that modifies the architecture of
CC       FLOWERING LOCUS T (FT) chromatin by modulating both H3 acetylation and
CC       methylation leading to the regulation of FT expression during flowering
CC       induction (PubMed:22442143). {ECO:0000269|PubMed:19517252,
CC       ECO:0000269|PubMed:22442143}.
CC   -!- SUBUNIT: Homodimer. Interacts with HDA1/HDA19, HDA6 AND HDA9.
CC       {ECO:0000269|PubMed:22442143}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19517252,
CC       ECO:0000269|PubMed:22442143}.
CC   -!- TISSUE SPECIFICITY: Expressed at the hypocotyl-root transition zone and
CC       the root hair zone. Also detected in the inflorescence.
CC       {ECO:0000269|PubMed:19517252}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in earlier growth stages in
CC       hypocotyls, roots and the vascular bundles of the leaves. Detected
CC       later in the vascular bundles of the basal leaves aera.
CC       {ECO:0000269|PubMed:22442143}.
CC   -!- DOMAIN: The PPC domain mediates interactions between AHL proteins.
CC       {ECO:0000269|PubMed:24218605}.
CC   -!- DISRUPTION PHENOTYPE: Slightly longer hypocotyls.
CC       {ECO:0000269|PubMed:19517252}.
CC   -!- MISCELLANEOUS: Overexpression of AHL22 results in delayed flowering and
CC       inhibition of hypocotyl growth. {ECO:0000269|PubMed:19517252}.
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DR   EMBL; AC002387; AAB82621.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10552.1; -; Genomic_DNA.
DR   EMBL; BT014980; AAT70431.1; -; mRNA.
DR   EMBL; BT020250; AAV74244.1; -; mRNA.
DR   EMBL; AB493592; BAH30430.1; -; mRNA.
DR   EMBL; BR000358; FAA00293.1; -; mRNA.
DR   PIR; D84890; D84890.
DR   RefSeq; NP_182067.1; NM_130105.4.
DR   AlphaFoldDB; O22130; -.
DR   SMR; O22130; -.
DR   STRING; 3702.AT2G45430.1; -.
DR   iPTMnet; O22130; -.
DR   PaxDb; O22130; -.
DR   PRIDE; O22130; -.
DR   ProteomicsDB; 244923; -.
DR   EnsemblPlants; AT2G45430.1; AT2G45430.1; AT2G45430.
DR   GeneID; 819151; -.
DR   Gramene; AT2G45430.1; AT2G45430.1; AT2G45430.
DR   KEGG; ath:AT2G45430; -.
DR   Araport; AT2G45430; -.
DR   TAIR; locus:2050946; AT2G45430.
DR   eggNOG; ENOG502QRBV; Eukaryota.
DR   HOGENOM; CLU_039808_2_1_1; -.
DR   InParanoid; O22130; -.
DR   OMA; RDHNGKS; -.
DR   OrthoDB; 1369071at2759; -.
DR   PhylomeDB; O22130; -.
DR   PRO; PR:O22130; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22130; baseline and differential.
DR   Genevisible; O22130; 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:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR   GO; GO:0009647; P:skotomorphogenesis; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
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   DNA-binding; Flowering; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..317
FT                   /note="AT-hook motif nuclear-localized protein 22"
FT                   /id="PRO_0000432040"
FT   DOMAIN          113..253
FT                   /note="PPC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT   DNA_BIND        89..101
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000305"
FT   REGION          22..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  33519 MW;  3A3677B991AE25F0 CRC64;
     MDQVSRSLPP PFLSRDLHLH PHHQFQHQQQ QQQQNHGHDI DQHRIGGLKR DRDADIDPNE
     HSSAGKDQST PGSGGESGGG GGGDNHITRR PRGRPAGSKN KPKPPIIITR DSANALKSHV
     MEVANGCDVM ESVTVFARRR QRGICVLSGN GAVTNVTIRQ PASVPGGGSS VVNLHGRFEI
     LSLSGSFLPP PAPPAASGLT IYLAGGQGQV VGGSVVGPLM ASGPVVIMAA SFGNAAYERL
     PLEEDDQEEQ TAGAVANNID GNATMGGGTQ TQTQTQQQQQ QQLMQDPTSF IQGLPPNLMN
     SVQLPAEAYW GTPRPSF
 
 
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