FHA2_ARATH
ID FHA2_ARATH Reviewed; 320 AA.
AC Q9SFV2; Q8GXA6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=FHA domain-containing protein FHA2 {ECO:0000305};
DE AltName: Full=Protein FORKHEAD-ASSOCIATED DOMAIN 2 {ECO:0000303|Ref.4};
DE Short=AtFHA2 {ECO:0000303|Ref.4};
GN Name=FHA2 {ECO:0000303|Ref.4};
GN OrderedLocusNames=At3g07220 {ECO:0000312|Araport:AT3G07220};
GN ORFNames=T1B9.11 {ECO:0000312|EMBL:AAF20224.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1016/S0168-9452(03)00290-5;
RA Ahn J.-W., Kim M., Bang J.-W., Pai H.-S.;
RT "Molecular characteristics and differential expression of two nuclear
RT factors containing the FHA domain in Arabidopsis.";
RL Plant Sci. 165:1023-1032(2003).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23192389; DOI=10.1007/s00425-012-1815-7;
RA Ahn E.R., Cho H.K., Pai H.S.;
RT "The forkhead-associated domain 2 (FHA2) in Arabidopsis plays a role in
RT plant fertility by regulating stamen development.";
RL Planta 237:1015-1023(2013).
CC -!- FUNCTION: May play a role in the control of plant organ development and
CC specifically in the regulation of stamen development. Does not show
CC transactivation activity in yeast. {ECO:0000269|PubMed:23192389}.
CC -!- INTERACTION:
CC Q9SFV2; C0SUU6: At1g11510; NbExp=3; IntAct=EBI-15191747, EBI-15191973;
CC Q9SFV2; Q93XW7: At3g21810; NbExp=3; IntAct=EBI-15191747, EBI-15195363;
CC Q9SFV2; F4JI72: At4g03250; NbExp=3; IntAct=EBI-15191747, EBI-15192535;
CC Q9SFV2; O22763-3: BZIP10; NbExp=3; IntAct=EBI-15191747, EBI-15191815;
CC Q9SFV2; O80450: GT-3B; NbExp=3; IntAct=EBI-15191747, EBI-1571089;
CC Q9SFV2; Q9FDW1: MYB44; NbExp=3; IntAct=EBI-15191747, EBI-15192813;
CC Q9SFV2; O04017: NAC098; NbExp=3; IntAct=EBI-15191747, EBI-1998502;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23192389,
CC ECO:0000269|Ref.4}. Note=Detected at discrete loci in the nucleus.
CC {ECO:0000269|PubMed:23192389}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Slightly enlarged leaves, small siliques with few
CC seed set, severely reduced fertility mainly due to reduced stamen
CC filament elongation and defects in pollen development. Increased
CC polyploidy levels in cotyledon and leaf cells.
CC {ECO:0000269|PubMed:23192389}.
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DR EMBL; AC012395; AAF20224.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74516.1; -; Genomic_DNA.
DR EMBL; AK118338; BAC42952.1; -; mRNA.
DR RefSeq; NP_187378.1; NM_111602.4.
DR AlphaFoldDB; Q9SFV2; -.
DR SMR; Q9SFV2; -.
DR IntAct; Q9SFV2; 67.
DR STRING; 3702.AT3G07220.1; -.
DR iPTMnet; Q9SFV2; -.
DR PaxDb; Q9SFV2; -.
DR PRIDE; Q9SFV2; -.
DR ProteomicsDB; 230577; -.
DR EnsemblPlants; AT3G07220.1; AT3G07220.1; AT3G07220.
DR GeneID; 819910; -.
DR Gramene; AT3G07220.1; AT3G07220.1; AT3G07220.
DR KEGG; ath:AT3G07220; -.
DR Araport; AT3G07220; -.
DR TAIR; locus:2098480; AT3G07220.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_068161_0_0_1; -.
DR InParanoid; Q9SFV2; -.
DR OMA; GPRHHVN; -.
DR OrthoDB; 1093684at2759; -.
DR PhylomeDB; Q9SFV2; -.
DR PRO; PR:Q9SFV2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFV2; baseline and differential.
DR Genevisible; Q9SFV2; AT.
DR GO; GO:0016587; C:Isw1 complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IPI:TAIR.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0080086; P:stamen filament development; IMP:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR045178; Fhl1/FHA1.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR21712; PTHR21712; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Developmental protein; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..320
FT /note="FHA domain-containing protein FHA2"
FT /id="PRO_0000433004"
FT DOMAIN 32..89
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 138..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 55
FT /note="N -> S (in Ref. 3; BAC42952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35993 MW; DDAAA4F97D3FAE93 CRC64;
MATAVGGGSD VEVGFAKLQG EDFEYYMQSY SIILGRNSKK ATVDVDLSSL GGGMNISRNH
ARIFYDFTRR RFSLEVLGKN GCLVEGVLHL PGNPNVKLDS QDLLQIGDKE FYFLLPVRSI
LGGPLGPRHH VSGQTSVVPY HNYQSGPGSG SGKKGVRSRE LYEYDDEDDD DDDDEEDDMR
GSGKKTRRDG HEVVYASGEK KREGRSKVDR EADDQQFLQL EEKDVVSSVA TVLSDLCGPG
EWMPMEKLHS VILKEYGNVW HHSRVRRYLS QEDWAIPEAK GKPWYGLLML LRKYPEHFVI
NTRSKGRVTL EFVSLVTLLS
