IQD2_ARATH
ID IQD2_ARATH Reviewed; 461 AA.
AC Q93ZH7; Q9LYY1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Protein IQ-DOMAIN 2 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD2 {ECO:0000303|PubMed:16368012};
GN Name=IQD2 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At5g03040 {ECO:0000312|EMBL:AED90548.1};
GN ORFNames=F15A17.70 {ECO:0000312|EMBL:CAB86071.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 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 [8]
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 Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86071.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163002; CAB86071.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90548.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90549.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90550.1; -; Genomic_DNA.
DR EMBL; AY057527; AAL09767.1; -; mRNA.
DR EMBL; AY143972; AAN28911.1; -; mRNA.
DR PIR; T48325; T48325.
DR RefSeq; NP_001154693.1; NM_001161221.1.
DR RefSeq; NP_001190211.1; NM_001203282.1.
DR RefSeq; NP_568110.2; NM_120382.4.
DR AlphaFoldDB; Q93ZH7; -.
DR SMR; Q93ZH7; -.
DR IntAct; Q93ZH7; 3.
DR STRING; 3702.AT5G03040.1; -.
DR PaxDb; Q93ZH7; -.
DR PRIDE; Q93ZH7; -.
DR ProMEX; Q93ZH7; -.
DR ProteomicsDB; 175239; -.
DR EnsemblPlants; AT5G03040.1; AT5G03040.1; AT5G03040.
DR EnsemblPlants; AT5G03040.2; AT5G03040.2; AT5G03040.
DR EnsemblPlants; AT5G03040.3; AT5G03040.3; AT5G03040.
DR GeneID; 831696; -.
DR Gramene; AT5G03040.1; AT5G03040.1; AT5G03040.
DR Gramene; AT5G03040.2; AT5G03040.2; AT5G03040.
DR Gramene; AT5G03040.3; AT5G03040.3; AT5G03040.
DR KEGG; ath:AT5G03040; -.
DR Araport; AT5G03040; -.
DR TAIR; locus:2143503; AT5G03040.
DR eggNOG; ENOG502QUAG; Eukaryota.
DR HOGENOM; CLU_024547_3_1_1; -.
DR InParanoid; Q93ZH7; -.
DR OMA; NEENQHT; -.
DR OrthoDB; 799418at2759; -.
DR PhylomeDB; Q93ZH7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZH7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA: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; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..461
FT /note="Protein IQ-DOMAIN 2"
FT /id="PRO_0000453109"
FT DOMAIN 114..142
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..158
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 278..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 425..432
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 26..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50463 MW; 975794140856C201 CRC64;
MGKKAKWFSS VKKAFSPDSK KSKQKLAEGQ NGVISNPPVV DNVRQSSSSP PPALAPREVR
VAEVIVERNR DLSPPSTADA VNVTATDVPV VPSSSAPGVV RRATPTRFAG KSNEEAAAIL
IQTIFRGYLA RRALRAMRGL VRLKLLMEGS VVKRQAANTL KCMQTLSRVQ SQIRARRIRM
SEENQARQKQ LLQKHAKELA GLKNGDNWND SIQSKEKVEA NLLSKYEATM RRERALAYSY
SHQQNWKNNS KSGNPMFMDP SNPTWGWSWL ERWMAGRPLE SSEKEQSNSN NDNAASVKGS
INRNEAAKSL TRNGSTQPNT PSSARGTPRN KNSFFSPPTP SRLNQSSRKS NDDDSKSTIS
VLSERNRRHS IAGSSVRDDE SLAGSPALPS YMVPTKSARA RLKPQSPLGG TTQENEGFTD
KASAKKRLSY PTSPALPKPR RFSAPPKVES GGVTVTNGAG S
