FRIP2_ARATH
ID FRIP2_ARATH Reviewed; 310 AA.
AC O23550;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Protein FIP2 {ECO:0000305};
DE AltName: Full=FRIGIDA-interacting protein 2 {ECO:0000303|PubMed:19429606};
GN Name=FIP2 {ECO:0000303|PubMed:19429606};
GN OrderedLocusNames=At4g17060 {ECO:0000312|Araport:AT4G17060};
GN ORFNames=dl4560c {ECO:0000312|EMBL:CAB10486.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA De Los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP INTERACTION WITH FRI, AND DISRUPTION PHENOTYPE.
RX PubMed=19429606; DOI=10.1104/pp.109.137448;
RA Geraldo N., Baeurle I., Kidou S., Hu X., Dean C.;
RT "FRIGIDA delays flowering in Arabidopsis via a cotranscriptional mechanism
RT involving direct interaction with the nuclear cap-binding complex.";
RL Plant Physiol. 150:1611-1618(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INTERACTION WITH WAV3.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22122664; DOI=10.1111/j.1365-313x.2011.04870.x;
RA Sakai T., Mochizuki S., Haga K., Uehara Y., Suzuki A., Harada A., Wada T.,
RA Ishiguro S., Okada K.;
RT "The wavy growth 3 E3 ligase family controls the gravitropic response in
RT Arabidopsis roots.";
RL Plant J. 70:303-314(2012).
CC -!- SUBUNIT: Interacts with FRI (PubMed:19429606). Interacts with WAV3
CC (PubMed:22122664). {ECO:0000269|PubMed:19429606,
CC ECO:0000269|PubMed:22122664}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19429606}.
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DR EMBL; Z97342; CAB10486.1; -; Genomic_DNA.
DR EMBL; AL161545; CAB80977.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83844.1; -; Genomic_DNA.
DR EMBL; BT033104; ACF16166.1; -; mRNA.
DR PIR; A71439; A71439.
DR RefSeq; NP_193439.1; NM_117810.7.
DR AlphaFoldDB; O23550; -.
DR SMR; O23550; -.
DR STRING; 3702.AT4G17060.1; -.
DR iPTMnet; O23550; -.
DR PaxDb; O23550; -.
DR PRIDE; O23550; -.
DR ProteomicsDB; 228947; -.
DR EnsemblPlants; AT4G17060.1; AT4G17060.1; AT4G17060.
DR GeneID; 827414; -.
DR Gramene; AT4G17060.1; AT4G17060.1; AT4G17060.
DR KEGG; ath:AT4G17060; -.
DR Araport; AT4G17060; -.
DR TAIR; locus:3439226; AT4G17060.
DR eggNOG; KOG4282; Eukaryota.
DR HOGENOM; CLU_055205_0_0_1; -.
DR InParanoid; O23550; -.
DR OMA; KYNGNPK; -.
DR OrthoDB; 1361808at2759; -.
DR PhylomeDB; O23550; -.
DR PRO; PR:O23550; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23550; baseline and differential.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR InterPro; IPR044823; ASIL1/2-like.
DR PANTHER; PTHR31307; PTHR31307; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..310
FT /note="Protein FIP2"
FT /id="PRO_0000443509"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 310 AA; 34434 MW; B3328AC1D908589F CRC64;
MGFAPVTPAA VETYDPDVDH DDESNGLDGF RVRSKRSGKF SGGYSDSPRE VGDGYGVRSR
ARSNMKMYGG FKSEFDSDHD SGSGFGLKRK YNGNPKVSAD FDADSDDEIV LVPKATRLRT
HGKPSSGDFS HGSGGGFPLK SFGDRNFASH GFKPKNFSKP EPNFSQDLDY DDEFDDDRAE
REGFNPRIQS SRSSSRVNGY SRKDGSYPRN TGASNGYGSS SRFKHEQMNA AAEVESDPID
EVVSSVKMLT EMFVRVENSK MEMMREMEKS RMEMELKHCQ MMLESQQQII GAFAEALSEK
KSTNARRPVS
