SG29A_ARATH
ID SG29A_ARATH Reviewed; 270 AA.
AC Q8RXY6; Q9LTY5;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=SAGA-associated factor 29 homolog A {ECO:0000305};
DE Short=AtSGF29a {ECO:0000303|PubMed:21193996};
DE AltName: Full=29 kDa SAGA-associated factor homolog A {ECO:0000305};
GN Name=SGF29A {ECO:0000303|PubMed:21193996};
GN OrderedLocusNames=At3g27460 {ECO:0000312|Araport:AT3G27460};
GN ORFNames=K1G2.17 {ECO:0000312|EMBL:BAA95721.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21193996; DOI=10.1007/s00425-010-1337-0;
RA Kaldis A., Tsementzi D., Tanriverdi O., Vlachonasios K.E.;
RT "Arabidopsis thaliana transcriptional co-activators ADA2b and SGF29a are
RT implicated in salt stress responses.";
RL Planta 233:749-762(2011).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Chromatin reader component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA (By similarity). Involved in
CC salt stress tolerance. Enhances the effect of ADA2B in the positive
CC regulation of salt-induced gene expression (PubMed:21193996).
CC {ECO:0000250|UniProtKB:Q96ES7, ECO:0000269|PubMed:21193996}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC stems and flowers. {ECO:0000269|PubMed:21193996}.
CC -!- DOMAIN: The SGF29 tudor-like domain mediates binding to methylated
CC 'Lys-4' of histone H3 (H3K4me). {ECO:0000255|PROSITE-ProRule:PRU00851}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering. Increased tolerance to salt
CC stress. {ECO:0000269|PubMed:21193996}.
CC -!- SIMILARITY: Belongs to the SGF29 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00851}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95721.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB024028; BAA95721.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77322.1; -; Genomic_DNA.
DR EMBL; AY080609; AAL86293.1; -; mRNA.
DR EMBL; AY122985; AAM67518.1; -; mRNA.
DR RefSeq; NP_189382.2; NM_113661.4.
DR AlphaFoldDB; Q8RXY6; -.
DR SMR; Q8RXY6; -.
DR STRING; 3702.AT3G27460.1; -.
DR iPTMnet; Q8RXY6; -.
DR PaxDb; Q8RXY6; -.
DR EnsemblPlants; AT3G27460.1; AT3G27460.1; AT3G27460.
DR GeneID; 822367; -.
DR Gramene; AT3G27460.1; AT3G27460.1; AT3G27460.
DR KEGG; ath:AT3G27460; -.
DR Araport; AT3G27460; -.
DR TAIR; locus:2086711; AT3G27460.
DR eggNOG; KOG3038; Eukaryota.
DR HOGENOM; CLU_065257_0_0_1; -.
DR InParanoid; Q8RXY6; -.
DR OMA; TYIAKMG; -.
DR PhylomeDB; Q8RXY6; -.
DR PRO; PR:Q8RXY6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RXY6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR InterPro; IPR037802; SGF29.
DR InterPro; IPR010750; SGF29_tudor-like_dom.
DR PANTHER; PTHR21539; PTHR21539; 1.
DR Pfam; PF07039; DUF1325; 1.
DR PROSITE; PS51518; SGF29_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..270
FT /note="SAGA-associated factor 29 homolog A"
FT /id="PRO_0000443329"
FT DOMAIN 125..270
FT /note="SGF29 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 85..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..170
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 217..220
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 242..245
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 215
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT SITE 222
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 270 AA; 30499 MW; 76889E3F7A3D1F9A CRC64;
MSSSPDIAGI LDNTKELDRL RKEQEEVLVE INKMHKKLQA TPEIVEKPGD ISLSKLKNLY
IQAKELSESE VTVSNILLTQ LDSLLPSGPT GQQRRKLEGN EQKRKRMKVD TDVTRVSPSM
RNQIEAYASL KGEQVAARVT AEDAEKDEWF VVKVIHFDRE TKEVEVLDEE PGDDEEGGGQ
RTYKLSMSCI LPFPKRNDPS STQEFIPGKH VLAVYPGTTA LYKATVISTP RKRKSDEYLL
EFDDDEEDGA LPQRTVPFHK VVALPEGHRQ
