IQD11_ARATH
ID IQD11_ARATH Reviewed; 443 AA.
AC Q9LYR0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Protein IQ-DOMAIN 11 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD11 {ECO:0000303|PubMed:16368012};
GN Name=IQD11 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At5g13460 {ECO:0000312|Araport:AT5G13460};
GN ORFNames=T22N19.110 {ECO:0000312|EMBL:AED91897.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 (PubMed:28115582). Regulates cell shape and
CC elongation in aerial organs (i.e. epidermis pavement cells) probably by
CC regulating cortical microtubules (MT) arrays orientation
CC (PubMed:28115582). May associate with nucleic acids and regulate gene
CC expression at the transcriptional or post-transcriptional level (By
CC similarity). {ECO:0000250|UniProtKB:Q9SF32,
CC ECO:0000269|PubMed:28115582}.
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 -!- TISSUE SPECIFICITY: Expressed in hypocotyls, cotyledons, leaves and
CC petioles. {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AL163572; CAB87153.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91897.1; -; Genomic_DNA.
DR EMBL; AY054652; AAK96843.1; -; mRNA.
DR EMBL; AY128736; AAM91136.1; -; mRNA.
DR EMBL; AY086149; AAM63354.1; -; mRNA.
DR PIR; T48593; T48593.
DR RefSeq; NP_196850.1; NM_121349.4.
DR AlphaFoldDB; Q9LYR0; -.
DR SMR; Q9LYR0; -.
DR STRING; 3702.AT5G13460.1; -.
DR PaxDb; Q9LYR0; -.
DR PRIDE; Q9LYR0; -.
DR ProteomicsDB; 185027; -.
DR EnsemblPlants; AT5G13460.1; AT5G13460.1; AT5G13460.
DR GeneID; 831188; -.
DR Gramene; AT5G13460.1; AT5G13460.1; AT5G13460.
DR KEGG; ath:AT5G13460; -.
DR Araport; AT5G13460; -.
DR TAIR; locus:2181635; AT5G13460.
DR eggNOG; ENOG502QVDD; Eukaryota.
DR HOGENOM; CLU_024547_0_0_1; -.
DR InParanoid; Q9LYR0; -.
DR OMA; RIKEYAF; -.
DR OrthoDB; 1186768at2759; -.
DR PhylomeDB; Q9LYR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYR0; 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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR InterPro; IPR025064; DUF4005.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF13178; DUF4005; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..443
FT /note="Protein IQ-DOMAIN 11"
FT /id="PRO_0000453118"
FT DOMAIN 113..138
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 139..161
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 5..20
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..18
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 27..34
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 50..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50821 MW; EA3C8B85E2041D83 CRC64;
MAKKKGLFTV LKRIFISEVN SEKKEKRRKW TFWKLRIKKR LPSITAPPEH RTSHESHEEQ
KEEIVSDVGE ISQVSCSRQL DSIEESKGST SPETADLVVQ YQMFLNRQEE VLAATRIQTA
FRGHLARKAL RALKGIVKLQ AYIRGRAVRR QAMTTLKCLQ SVVNIQSQVC GKRTQIPGGV
HRDYEESNIF NDNILKVDTN GQKRWDDSLL TKEEKEAVVM SKKEASLRRE RIKEYAVTHR
KSAESYQKRS NTKWKYWLDE WVDTQLTKSK ELEDLDFSSK TKPKDETLNE KQLKTPRNSS
PRRLVNNHRR QVSIGEDEQS PAAVTITTPT YMVATESAKA KSRSLSSPRI RPRSFDTQSE
SYSPYKNKLC LTTSMMSEAP SKVRIANNGS NTRPSAYQQR SPGLRGFNIG PLKSCNNNNT
LLNDLSINSE RSLPSWNKQS SLR
