IQD3_ARATH
ID IQD3_ARATH Reviewed; 430 AA.
AC Q9FT53; A0A178VCT8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Protein IQ-DOMAIN 3 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD3 {ECO:0000303|PubMed:16368012};
GN Name=IQD3 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At3g52290 {ECO:0000312|Araport:AT3G52290};
GN ORFNames=T25B15.60 {ECO:0000312|EMBL:CAC07920.1};
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=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=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 [4]
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 [5]
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 [6]
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 [7]
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}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AL132972; CAC07920.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78927.1; -; Genomic_DNA.
DR EMBL; BT002936; AAO22750.1; -; mRNA.
DR EMBL; BT005639; AAO64059.1; -; mRNA.
DR PIR; T46099; T46099.
DR RefSeq; NP_190797.1; NM_115089.3.
DR AlphaFoldDB; Q9FT53; -.
DR SMR; Q9FT53; -.
DR STRING; 3702.AT3G52290.1; -.
DR PaxDb; Q9FT53; -.
DR PRIDE; Q9FT53; -.
DR ProteomicsDB; 252029; -.
DR EnsemblPlants; AT3G52290.1; AT3G52290.1; AT3G52290.
DR GeneID; 824394; -.
DR Gramene; AT3G52290.1; AT3G52290.1; AT3G52290.
DR KEGG; ath:AT3G52290; -.
DR Araport; AT3G52290; -.
DR TAIR; locus:2100504; AT3G52290.
DR eggNOG; ENOG502QUAG; Eukaryota.
DR HOGENOM; CLU_024547_3_1_1; -.
DR InParanoid; Q9FT53; -.
DR OMA; QSERFNR; -.
DR OrthoDB; 799418at2759; -.
DR PhylomeDB; Q9FT53; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FT53; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 Calmodulin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..430
FT /note="Protein IQ-DOMAIN 3"
FT /id="PRO_0000453110"
FT DOMAIN 107..135
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..231
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 271..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..224
FT /evidence="ECO:0000255"
FT MOTIF 9..16
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 396..403
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 306..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48118 MW; EF9445C3E39D8F48 CRC64;
MGKSWFSAVK KALSPEPKQK KEQKPHKSKK WFGKSKKLDV TNSGAAYSPR TVKDAKLKEI
EEQQSRHAYS VAIATAAAAE AAVAAAQAAA EVVRLSALSR FPGKSMEEIA AIKIQTAFRG
YMARRALRAL RGLVRLKSLV QGKCVRRQAT STLQSMQTLA RVQYQIRERR LRLSEDKQAL
TRQLQQKHNK DFDKTGENWN DSTLSREKVE ANMLNKQVAT MRREKALAYA FSHQNTWKNS
TKMGSQTFMD PNNPHWGWSW LERWMAARPN ENHSLTPDNA EKDSSARSVA SRAMSEMIPR
GKNLSPRGKT PNSRRGSSPR VRQVPSEDSN SIVSFQSEQP CNRRHSTCGS IPSTRDDESF
TSSFSQSVPG YMAPTQAAKA RARFSNLSPL SSEKTAKKRL SFSGSPKTVR RFSGPPKLES
NVTKKDTNLA
