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IQD17_ARATH
ID   IQD17_ARATH             Reviewed;         534 AA.
AC   F4JHN2; O23094; Q0WPW7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Protein IQ-DOMAIN 17 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD17 {ECO:0000303|PubMed:16368012};
GN   Name=IQD17 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At4g00820 {ECO:0000312|Araport:AT4G00820};
GN   ORFNames=A_TM018A10.13 {ECO:0000312|EMBL:AAB62858.1},
GN   T18A10.11 {ECO:0000312|EMBL:AAB62858.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   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: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:28115582}. Cell membrane
CC       {ECO:0000269|PubMed:28115582}.
CC   -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB62858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80891.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF013294; AAB62858.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161472; CAB80891.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE81939.1; -; Genomic_DNA.
DR   EMBL; AK228943; BAF00832.1; -; mRNA.
DR   PIR; T01564; T01564.
DR   RefSeq; NP_567191.2; NM_116308.4.
DR   AlphaFoldDB; F4JHN2; -.
DR   SMR; F4JHN2; -.
DR   STRING; 3702.AT4G00820.1; -.
DR   iPTMnet; F4JHN2; -.
DR   PaxDb; F4JHN2; -.
DR   PRIDE; F4JHN2; -.
DR   ProteomicsDB; 197591; -.
DR   EnsemblPlants; AT4G00820.1; AT4G00820.1; AT4G00820.
DR   GeneID; 828002; -.
DR   Gramene; AT4G00820.1; AT4G00820.1; AT4G00820.
DR   KEGG; ath:AT4G00820; -.
DR   Araport; AT4G00820; -.
DR   TAIR; locus:2134628; AT4G00820.
DR   eggNOG; ENOG502R300; Eukaryota.
DR   HOGENOM; CLU_024547_1_0_1; -.
DR   InParanoid; F4JHN2; -.
DR   OMA; NNAHGNE; -.
DR   OrthoDB; 736229at2759; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JHN2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW   Reference proteome; Repeat.
FT   CHAIN           1..534
FT                   /note="Protein IQ-DOMAIN 17"
FT                   /id="PRO_0000453123"
FT   DOMAIN          131..159
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          160..182
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..173
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   REGION          259..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        335
FT                   /note="R -> H (in Ref. 3; BAF00832)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  59996 MW;  4EBA7810AE19F2D6 CRC64;
     MGKKSGSSSS WLTAVKRAFR SPTKKEHNNN AHGNEVDEDE DKKKEKRRWL FRKSTNHDSP
     VKTSGVGKDA PAQKSTETTT IINPTVLSSV TEQRYDASTP PATVSAASET HPPSTTKELP
     NLTRRTYTAR EDYAAVVIQT GFRGYLARRA LRALKGLVKL QALVRGHNVR KQAKMTLRCM
     QALVRVQSRV LDQRKRLSHD GSRKSAFSDT QSVLESRYLQ EISDRRSMSR EGSSIAEDWD
     DRPHTIEEVK AMLQQRRDNA LRRESNNSIS QAFSHQVRRT RGSYSTGDEY EEERPKWLDR
     WMASKPWDKR ASTDQRVPPV YKTVEIDTSQ PYLTRGNSRT GASPSRSQRP SSPSRTSHHY
     QQHNFSSATP SPAKSRPIQI RSASPRIQRD DRSAYNYTSN TPSLRSNYSF TARSGYSVCT
     TTTTATNAAL PNYMAITESA KARIRSQSAP RQRPSTPEKE RISSARKRLS FPVPPLPQQM
     DGQSLRSPSF KSIGGSQLGA LEQQSNYSSC CTESLGGGGE ISPASTSDYR RWLR
 
 
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