ID   IQD4_ARATH              Reviewed;         527 AA.
AC   F4IUJ7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein IQ-DOMAIN 4 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD4 {ECO:0000303|PubMed:16368012};
GN   Name=IQD4 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At2g26410 {ECO:0000312|Araport:AT2G26410};
GN   ORFNames=T9J22.8 {ECO:0000312|EMBL:AEC07834.1};
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=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   INTERACTION WITH CALMODULIN, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=16368012; DOI=10.1186/1471-2148-5-72;
RA   Abel S., Savchenko T., Levy M.;
RT   "Genome-wide comparative analysis of the IQD gene families in Arabidopsis
RT   thaliana and Oryza sativa.";
RL   BMC Evol. Biol. 5:72-72(2005).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=15960618; DOI=10.1111/j.1365-313x.2005.02435.x;
RA   Levy M., Wang Q., Kaspi R., Parrella M.P., Abel S.;
RT   "Arabidopsis IQD1, a novel calmodulin-binding nuclear protein, stimulates
RT   glucosinolate accumulation and plant defense.";
RL   Plant J. 43:79-96(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=28115582; DOI=10.1104/pp.16.01743;
RA   Buerstenbinder K., Moeller B., Ploetner R., Stamm G., Hause G., Mitra D.,
RA   Abel S.;
RT   "The IQD family of calmodulin-binding proteins links calcium signaling to
RT   microtubules, membrane subdomains, and the nucleus.";
RL   Plant Physiol. 173:1692-1708(2017).
RN   [6]
RP   REVIEW.
RX   PubMed=28534650; DOI=10.1080/15592324.2017.1331198;
RA   Buerstenbinder K., Mitra D., Quegwer J.;
RT   "Functions of IQD proteins as hubs in cellular calcium and auxin signaling:
RT   A toolbox for shape formation and tissue-specification in plants?";
RL   Plant Signal. Behav. 12:E1331198-E1331198(2017).
CC   -!- FUNCTION: May be involved in cooperative interactions with calmodulins
CC       or calmodulin-like proteins (By similarity). Recruits calmodulin
CC       proteins to microtubules, thus being a potential scaffold in cellular
CC       signaling and trafficking (By similarity). May associate with nucleic
CC       acids and regulate gene expression at the transcriptional or post-
CC       transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
CC   -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of Ca(2+)
CC       and CaM-like proteins. {ECO:0000250|UniProtKB:Q9SF32}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:28115582}.
CC   -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR   EMBL; AC002505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002685; AEC07834.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM63182.1; -; Genomic_DNA.
DR   RefSeq; NP_001325287.1; NM_001336066.1.
DR   RefSeq; NP_180209.4; NM_128198.5.
DR   AlphaFoldDB; F4IUJ7; -.
DR   STRING; 3702.AT2G26410.1; -.
DR   PaxDb; F4IUJ7; -.
DR   PRIDE; F4IUJ7; -.
DR   ProteomicsDB; 175605; -.
DR   EnsemblPlants; AT2G26410.1; AT2G26410.1; AT2G26410.
DR   EnsemblPlants; AT2G26410.2; AT2G26410.2; AT2G26410.
DR   GeneID; 817181; -.
DR   Gramene; AT2G26410.1; AT2G26410.1; AT2G26410.
DR   Gramene; AT2G26410.2; AT2G26410.2; AT2G26410.
DR   KEGG; ath:AT2G26410; -.
DR   Araport; AT2G26410; -.
DR   TAIR; locus:2066226; AT2G26410.
DR   eggNOG; ENOG502QUAG; Eukaryota.
DR   HOGENOM; CLU_024547_3_1_1; -.
DR   OMA; PWDAESI; -.
DR   OrthoDB; 799418at2759; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IUJ7; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Coiled coil; Nucleus; Reference proteome.
FT   CHAIN           1..527
FT                   /note="Protein IQ-DOMAIN 4"
FT                   /id="PRO_0000453111"
FT   DOMAIN          147..175
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          13..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..273
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   REGION          323..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           478..485
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        19..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  58278 MW;  A9128C8327FF1621 CRC64;
     MGKNWLTCVS VACLSPGKDK KNQKPEKPKR KWSFGKQKSR ESFDFPLEET PPVDPSPSSV
     HRPYPPPPPL PDFAPQPLLP PPSPPPPPPA YTINTRIYGE SKESKNRQAL ALASAVAAEA
     AVVAAHAAAE VIRLTTPSTP QIEESKEETA AIKIQNAYRC YTARRTLRAL RGMARLKSLL
     QGKYVKRQMN AMLSSMQTLT RLQTQIQERR NRLSAENKTR HRLIQQKGHQ KENHQNLVTA
     GNFDSSNKSK EQIVARSVNR KEASVRRERA LAYAYSHQQT WRNSSKLPHQ TLMDTNTTDW
     GWSWLERWMA SRPWDAESID DQVSVKSSLK RENSIKSSPA RSKTQKSASQ SSIQWPVNND
     TKSRKIEVTN RRHSIGGGSS ENAKDDESVG SSSSRRNSLD NTQTVKSKVS VETTSNVSNA
     QTVKPKANVG AKRNLDNTKT LKSKSSVGTT GNLANTEAVK SKVNVGTTSM PKKEVVADKK
     KPPQMVLPKK RLSSSTSLGK TKKLSDSDKA TTGVANGEKK RRNGGSS