IQD1_ARATH
ID IQD1_ARATH Reviewed; 454 AA.
AC Q9SF32;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Protein IQ-DOMAIN 1 {ECO:0000303|PubMed:15960618};
DE Short=AtIQD1 {ECO:0000303|PubMed:16368012};
GN Name=IQD1 {ECO:0000303|PubMed:15960618};
GN OrderedLocusNames=At3g09710 {ECO:0000312|Araport:AT3G09710};
GN ORFNames=F11F8.30 {ECO:0000312|EMBL:AAF23301.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, INTERACTION WITH CALMODULIN, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
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 [2]
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 [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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH KLCR1; CAM1; CAM2; CML8 AND CML9, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23204523; DOI=10.1074/jbc.m112.396200;
RA Buerstenbinder K., Savchenko T., Mueller J., Adamson A.W., Stamm G.,
RA Kwong R., Zipp B.J., Dinesh D.C., Abel S.;
RT "Arabidopsis calmodulin-binding protein IQ67-domain 1 localizes to
RT microtubules and interacts with kinesin light chain-related protein-1.";
RL J. Biol. Chem. 288:1871-1882(2013).
RN [7]
RP REVIEW.
RX PubMed=23531692; DOI=10.4161/psb.24369;
RA Abel S., Buerstenbinder K., Mueller J.;
RT "The emerging function of IQD proteins as scaffolds in cellular signaling
RT and trafficking.";
RL Plant Signal. Behav. 8:E24369-E24369(2013).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CALMODULIN.
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 [9]
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. Modulates expression of glucosinolate
CC pathway genes. May associate with nucleic acids and regulate gene
CC expression at the transcriptional or post-transcriptional level
CC (PubMed:15960618, PubMed:23204523). Recruits KLCR1 and calmodulin
CC proteins to microtubules, thus being a potential scaffold in cellular
CC signaling and trafficking (PubMed:23204523).
CC {ECO:0000269|PubMed:15960618, ECO:0000269|PubMed:23204523}.
CC -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of
CC Ca(2+)(e.g. CaM1 and CaM2) and CaM-like (e.g. CML8 and CML9) proteins
CC (PubMed:15960618, PubMed:23204523). Interacts with KLCR1
CC (PubMed:23204523). {ECO:0000269|PubMed:15960618,
CC ECO:0000269|PubMed:23204523}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:15960618, ECO:0000269|PubMed:23204523,
CC ECO:0000269|PubMed:28115582}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23204523, ECO:0000269|PubMed:28115582}.
CC Note=Recruits KLCR1 and calmodulin (CaM2) to microtubules, nucleus and
CC nucleolus. {ECO:0000269|PubMed:23204523, ECO:0000269|PubMed:28115582}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SF32-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, stems, siliques,
CC inflorescence stems and whole shoots. Restricted to the vascular
CC bundles. {ECO:0000269|PubMed:15960618}.
CC -!- INDUCTION: By mechanical stimuli and aphid infestation, but not by
CC jasmonate, salicylic acid, 1-aminocyclopropane-1-carboxylate (ACC) ou
CC auxin (IAA). {ECO:0000269|PubMed:15960618}.
CC -!- MISCELLANEOUS: IQD1 overexpression leads to increased resistance
CC against herbivory by generalist chewing and phloem-feeding insects.
CC {ECO:0000269|PubMed:15960618}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AY827468; AAX33644.1; -; mRNA.
DR EMBL; AC016661; AAF23301.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74801.1; -; Genomic_DNA.
DR EMBL; BT020272; AAV84493.1; -; mRNA.
DR EMBL; BT020448; AAW30026.1; -; mRNA.
DR RefSeq; NP_187582.1; NM_111805.3. [Q9SF32-1]
DR AlphaFoldDB; Q9SF32; -.
DR SMR; Q9SF32; -.
DR BioGRID; 5462; 2.
DR IntAct; Q9SF32; 1.
DR STRING; 3702.AT3G09710.2; -.
DR iPTMnet; Q9SF32; -.
DR PaxDb; Q9SF32; -.
DR PRIDE; Q9SF32; -.
DR ProteomicsDB; 228833; -. [Q9SF32-1]
DR EnsemblPlants; AT3G09710.1; AT3G09710.1; AT3G09710. [Q9SF32-1]
DR GeneID; 820128; -.
DR Gramene; AT3G09710.1; AT3G09710.1; AT3G09710. [Q9SF32-1]
DR KEGG; ath:AT3G09710; -.
DR Araport; AT3G09710; -.
DR eggNOG; ENOG502QUAG; Eukaryota.
DR HOGENOM; CLU_024547_3_1_1; -.
DR InParanoid; Q9SF32; -.
DR PhylomeDB; Q9SF32; -.
DR PRO; PR:Q9SF32; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF32; baseline and differential.
DR Genevisible; Q9SF32; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..454
FT /note="Protein IQ-DOMAIN 1"
FT /id="PRO_0000311120"
FT DOMAIN 107..136
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 103..113
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 272..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..428
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 274..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50540 MW; 93376980F5367F34 CRC64;
MVKKAKWLKN VKKAFSPDSK KLKHESVECQ DSVISYPVLI ATSRSSSPQF EVRVDEVNYE
QKKNLYPPSS DSVTATVAHV LVDSPPSSPE SVHQAIVVNR FAGKSKEEAA AILIQSTFRG
HLARRESQVM RGQERLKLLM EGSVVQRQAA ITLKCMQTLS RVQSQIRSRR IRMSEENQAR
HKQLLQKHAK ELGGLKNGGN WNYSNQSKEQ VEAGMLHKYE ATMRRERALA YAFTHQQNLK
SFSKTANPMF MDPSNPTWGW SWLERWMAGR PWESSEKEQN TTNNDNSSVK NSTNRNSQGG
ETAKSSNRNK LNSSTKPNTP SASSTATRNP RKKRPIPSSI KSKSSDDEAK SSERNRRPSI
ARPSVSDDET LSSSTARRSS NLIPTTKSAR GKPKSQTSSR VAVTTSTTEE SSILPEKAPA
KKRLSTSASP APKPRRSSAP PKVEKGVLKA ERTP
