IKU1_ARATH
ID IKU1_ARATH Reviewed; 402 AA.
AC O82170;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein HAIKU1 {ECO:0000305};
DE AltName: Full=MPK3/6-targeted VQ-motif-containing protein 9 {ECO:0000303|PubMed:24750137};
DE AltName: Full=VQ motif-containing protein 14 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ14 {ECO:0000303|PubMed:22535423};
GN Name=IKU1 {ECO:0000303|PubMed:12692325};
GN Synonyms=MVQ9 {ECO:0000303|PubMed:24750137},
GN VQ14 {ECO:0000303|PubMed:22535423};
GN OrderedLocusNames=At2g35230 {ECO:0000312|Araport:AT2G35230};
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;
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 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12692325; DOI=10.1104/pp.102.018762;
RA Garcia D., Saingery V., Chambrier P., Mayer U., Juergens G., Berger F.;
RT "Arabidopsis haiku mutants reveal new controls of seed size by endosperm.";
RL Plant Physiol. 131:1661-1670(2003).
RN [6]
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 [7]
RP FUNCTION, INTERACTION WITH WRKY10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 58-ILE--GLN-61.
RX PubMed=20545893; DOI=10.1111/j.1365-313x.2010.04271.x;
RA Wang A., Garcia D., Zhang H., Feng K., Chaudhury A., Berger F.,
RA Peacock W.J., Dennis E.S., Luo M.;
RT "The VQ motif protein IKU1 regulates endosperm growth and seed size in
RT Arabidopsis.";
RL Plant J. 63:670-679(2010).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(2012).
RN [9]
RP INTERACTION WITH MPK6.
RX PubMed=24750137; DOI=10.1111/nph.12817;
RA Pecher P., Eschen-Lippold L., Herklotz S., Kuhle K., Naumann K., Bethke G.,
RA Uhrig J., Weyhe M., Scheel D., Lee J.;
RT "The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6
RT target a subclass of 'VQ-motif'-containing proteins to regulate immune
RT responses.";
RL New Phytol. 203:592-606(2014).
CC -!- FUNCTION: Modulates seed size by negatively regulating the
CC cellularization of syncytial endosperm (PubMed:12692325,
CC PubMed:20545893). May function by binding and modulating the activity
CC of WRKY10 transcription factor (PubMed:20545893).
CC {ECO:0000269|PubMed:12692325, ECO:0000269|PubMed:20545893}.
CC -!- SUBUNIT: Interacts with WRKY10 (PubMed:20545893). Interacts with MPK6
CC (PubMed:24750137). {ECO:0000269|PubMed:20545893,
CC ECO:0000269|PubMed:24750137}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20545893}.
CC Note=Expressed both in the unfused polar nuclei and in the fused polar
CC nucleus in the central cell before fertilization, in the syncytial
CC endosperm after fertilization and in the endosperm nuclei.
CC {ECO:0000269|PubMed:20545893}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=O82170-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Reduced seed size and early endosperm
CC cellularization. {ECO:0000269|PubMed:12692325}.
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DR EMBL; AC004667; AAC61815.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09083.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62246.1; -; Genomic_DNA.
DR EMBL; AK117327; BAC41998.1; -; mRNA.
DR EMBL; BT009652; AAP75802.1; -; mRNA.
DR PIR; A84766; A84766.
DR RefSeq; NP_001324419.1; NM_001336551.1. [O82170-1]
DR RefSeq; NP_181066.1; NM_129075.4. [O82170-1]
DR AlphaFoldDB; O82170; -.
DR STRING; 3702.AT2G35230.1; -.
DR iPTMnet; O82170; -.
DR PaxDb; O82170; -.
DR PRIDE; O82170; -.
DR ProteomicsDB; 228837; -. [O82170-1]
DR EnsemblPlants; AT2G35230.1; AT2G35230.1; AT2G35230. [O82170-1]
DR EnsemblPlants; AT2G35230.3; AT2G35230.3; AT2G35230. [O82170-1]
DR GeneID; 818090; -.
DR Gramene; AT2G35230.1; AT2G35230.1; AT2G35230. [O82170-1]
DR Gramene; AT2G35230.3; AT2G35230.3; AT2G35230. [O82170-1]
DR KEGG; ath:AT2G35230; -.
DR Araport; AT2G35230; -.
DR TAIR; locus:2063419; AT2G35230.
DR eggNOG; ENOG502QSYF; Eukaryota.
DR HOGENOM; CLU_063567_1_0_1; -.
DR InParanoid; O82170; -.
DR OMA; DQSWSNT; -.
DR PhylomeDB; O82170; -.
DR PRO; PR:O82170; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82170; baseline and differential.
DR Genevisible; O82170; AT.
DR GO; GO:0043078; C:polar nucleus; IDA:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0080113; P:regulation of seed growth; IMP:TAIR.
DR InterPro; IPR008889; VQ.
DR InterPro; IPR039825; VQ5/14.
DR InterPro; IPR039612; VQ_5/9/14.
DR PANTHER; PTHR33783; PTHR33783; 2.
DR PANTHER; PTHR33783:SF1; PTHR33783:SF1; 2.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..402
FT /note="Protein HAIKU1"
FT /id="PRO_0000432304"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 55..64
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 20..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 58..61
FT /note="IVQQ->EDLE: Loss of function."
FT /evidence="ECO:0000269|PubMed:20545893"
SQ SEQUENCE 402 AA; 44686 MW; 67889CB93F4F7F7B CRC64;
MDRPRQNDHL GVNRIGKNIR KSPLHQSTFA ASTSNGAAPR LQTQPQVYNI SKNDFRSIVQ
QLTGSPSRES LPRPPQNNSL RPQNTRLQRI RPSPLTQLNR PAVPLPSMAP PQSHPQFARQ
PPHQPPFPQT TQQPMMGHRD QFWSNTAESP VSEYMRYLQS SLGDSGPNAN QMQPGHEQRP
YIPGHEQRPY VPGNEQQPYM PGNEQRPYIP GHEQRSYMPA QSQSQSQPQP QPQPQQHMMP
GPQPRMNMQG PLQPNQYLPP PGLVPSPVPH NLPSPRFNAP VPVTPTQPSP MFSQMYGGFP
SPRYNGFGPL QSPTSQFLQP SPTGYPNMFS PRSPYPLLSP GVQYPQPLTP NFSFSQIAQQ
GSLGPGAGPS QGPPQPPPSP GLMFPLSPSG FFPMPSPRWN DY
