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AHL29_ARATH
ID   AHL29_ARATH             Reviewed;         302 AA.
AC   Q9C9K7;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=AT-hook motif nuclear-localized protein 29 {ECO:0000312|EMBL:AEE35850.1};
DE   AltName: Full=Protein SUPPRESSOR OF PHYB-4#3 {ECO:0000303|PubMed:18088311};
GN   Name=AHL29 {ECO:0000303|PubMed:15604740};
GN   Synonyms=SOB3 {ECO:0000303|PubMed:18088311};
GN   OrderedLocusNames=At1g76500 {ECO:0000312|Araport:AT1G76500};
GN   ORFNames=F14G6.10 {ECO:0000312|EMBL:AAG51949.1};
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=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   [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;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF ARG-77.
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   [6]
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   [7]
RP   GENE FAMILY, MUTAGENESIS OF ARG-77, SUBUNIT, INTERACTION WITH AHL5; AHL12;
RP   AHL25; AHL27; TCP4; TCP13 AND EF114, SUBCELLULAR LOCATION, 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) (By
CC       similarity). Acts redundantly with AHL18, AHL22 and AHL27 in the
CC       regulation of flowering and regulation of the hypocotyl elongation
CC       (PubMed:19517252). Acts redundantly with AHL27/ESC to modulate
CC       hypocotyl growth inhibition in response to light (PubMed:18088311).
CC       {ECO:0000250|UniProtKB:Q8VYJ2, ECO:0000269|PubMed:18088311,
CC       ECO:0000269|PubMed:19517252}.
CC   -!- SUBUNIT: Homodimer. Interacts with AHL5, AHL12, AHL25, AHL27, TCP4,
CC       TCP13 and EF114. {ECO:0000269|PubMed:24218605}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18088311,
CC       ECO:0000269|PubMed:24218605}.
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 AHL29 results in altered cell
CC       expansion dynamics and delayed senescence.
CC       {ECO:0000269|PubMed:18088311}.
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DR   EMBL; AC015450; AAG51949.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35850.1; -; Genomic_DNA.
DR   EMBL; BX817317; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BR000365; FAA00300.1; -; mRNA.
DR   PIR; H96792; H96792.
DR   RefSeq; NP_177776.1; NM_106300.4.
DR   AlphaFoldDB; Q9C9K7; -.
DR   SMR; Q9C9K7; -.
DR   STRING; 3702.AT1G76500.1; -.
DR   PaxDb; Q9C9K7; -.
DR   PRIDE; Q9C9K7; -.
DR   ProteomicsDB; 244847; -.
DR   EnsemblPlants; AT1G76500.1; AT1G76500.1; AT1G76500.
DR   GeneID; 843983; -.
DR   Gramene; AT1G76500.1; AT1G76500.1; AT1G76500.
DR   KEGG; ath:AT1G76500; -.
DR   Araport; AT1G76500; -.
DR   TAIR; locus:2011701; AT1G76500.
DR   eggNOG; ENOG502QV94; Eukaryota.
DR   HOGENOM; CLU_039808_2_2_1; -.
DR   InParanoid; Q9C9K7; -.
DR   OMA; GQLRGNM; -.
DR   OrthoDB; 1342088at2759; -.
DR   PhylomeDB; Q9C9K7; -.
DR   PRO; PR:Q9C9K7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9K7; baseline and differential.
DR   Genevisible; Q9C9K7; 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: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: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   DNA-binding; Flowering; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..302
FT                   /note="AT-hook motif nuclear-localized protein 29"
FT                   /id="PRO_0000432046"
FT   DOMAIN          96..241
FT                   /note="PPC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT   DNA_BIND        72..84
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..169
FT                   /note="Required for the binding to non-AHL interactors"
FT                   /evidence="ECO:0000269|PubMed:24218605"
FT   REGION          229..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         77
FT                   /note="R->H: In sob3-6; Abolishes binding to AT-rich DNA;
FT                   Exhibits a long hypocotyl phenotype in the light."
FT                   /evidence="ECO:0000269|PubMed:18088311,
FT                   ECO:0000269|PubMed:24218605"
FT   CONFLICT        108..112
FT                   /note="SGADI -> TGADK (in Ref. 3; BX817317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="I -> F (in Ref. 3; BX817317)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   302 AA;  30615 MW;  6EC755021E3DD375 CRC64;
     MDGGYDQSGG ASRYFHNLFR PELHHQLQPQ PQLHPLPQPQ PQPQPQQQNS DDESDSNKDP
     GSDPVTSGST GKRPRGRPPG SKNKPKPPVI VTRDSPNVLR SHVLEVSSGA DIVESVTTYA
     RRRGRGVSIL SGNGTVANVS LRQPATTAAH GANGGTGGVV ALHGRFEILS LTGTVLPPPA
     PPGSGGLSIF LSGVQGQVIG GNVVAPLVAS GPVILMAASF SNATFERLPL EDEGGEGGEG
     GEVGEGGGGE GGPPPATSSS PPSGAGQGQL RGNMSGYDQF AGDPHLLGWG AAAAAAPPRP
     AF
 
 
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