IQD32_ARATH
ID IQD32_ARATH Reviewed; 794 AA.
AC Q9FXI5; Q570I0; Q8LFD0; Q8LPF6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein IQ-DOMAIN 32 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD32 {ECO:0000303|PubMed:16368012};
GN Name=IQD32 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At1g19870 {ECO:0000312|Araport:AT1G19870};
GN ORFNames=F6F9.8 {ECO:0000312|EMBL:AAG12559.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 476-794.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-794.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP INTERACTION WITH CALMODULIN, GENE FAMILY, AND NOMENCLATURE.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80; SER-459 AND
RP SER-502, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-193; SER-459 AND
RP SER-544, AND 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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=24134884; DOI=10.1104/pp.113.225607;
RA Hamada T., Nagasaki-Takeuchi N., Kato T., Fujiwara M., Sonobe S., Fukao Y.,
RA Hashimoto T.;
RT "Purification and characterization of novel microtubule-associated proteins
RT from Arabidopsis cell suspension cultures.";
RL Plant Physiol. 163:1804-1816(2013).
RN [14]
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 [15]
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 ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}.
CC Note=Associates to cortical microtubules (MTs) (PubMed:24134884).
CC Recruits calmodulin (CaM2) to microtubules (PubMed:28115582).
CC {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG12559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM61480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007797; AAG12559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29908.1; -; Genomic_DNA.
DR EMBL; AY102110; AAM26680.1; -; mRNA.
DR EMBL; BT001081; AAN46862.1; -; mRNA.
DR EMBL; AY084918; AAM61480.1; ALT_INIT; mRNA.
DR EMBL; AK220728; BAD93867.1; -; mRNA.
DR PIR; A86332; A86332.
DR RefSeq; NP_564097.1; NM_101842.5.
DR AlphaFoldDB; Q9FXI5; -.
DR BioGRID; 23814; 2.
DR STRING; 3702.AT1G19870.1; -.
DR iPTMnet; Q9FXI5; -.
DR SwissPalm; Q9FXI5; -.
DR PaxDb; Q9FXI5; -.
DR PRIDE; Q9FXI5; -.
DR ProteomicsDB; 228740; -.
DR EnsemblPlants; AT1G19870.1; AT1G19870.1; AT1G19870.
DR GeneID; 838575; -.
DR Gramene; AT1G19870.1; AT1G19870.1; AT1G19870.
DR KEGG; ath:AT1G19870; -.
DR Araport; AT1G19870; -.
DR TAIR; locus:2035428; AT1G19870.
DR eggNOG; KOG1075; Eukaryota.
DR HOGENOM; CLU_019543_0_0_1; -.
DR InParanoid; Q9FXI5; -.
DR OMA; KGNERKW; -.
DR OrthoDB; 234221at2759; -.
DR PRO; PR:Q9FXI5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXI5; baseline and differential.
DR Genevisible; Q9FXI5; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005875; C:microtubule associated complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..794
FT /note="Protein IQ-DOMAIN 32"
FT /id="PRO_0000317069"
FT DOMAIN 214..242
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 243..265
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 15..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..241
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 277..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 657..664
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 357
FT /note="E -> G (in Ref. 3; AAM26680/AAN46862)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="G -> W (in Ref. 4; AAM61480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 86882 MW; B690D5778163F119 CRC64;
MGRSPASSCL RLISCSGGDD TSADPNSTAL ENKSSGDKRG WSFRKKSGKQ RGLITSVVSE
TTPASRTRET LESALLKSPS PDNNNVSEKQ QQSFSVDEKK SQLPVVTYVA EPVDEKKTQS
VIEEKTELLS VEEQIDHRTE VSPVIVESKG TETEEDDLIG TELQGPSAAD AAKIEEDVTS
EVEMASKVEP EESESDDVII VRKESDEKVD EKLDESVIVV IQAAVRGFLA RRELLRSKKV
IKLQAAVRGH LVRSQAMGSL RCVQAIVKMQ AMVRARHSTK DGSRVSATSD KSEPNAAAQK
LLENKFAKHL MESTPKTKPI NIKCDPTKPS SAWNWLERWM SVPKPEKTSK ANLTTEEQNL
EETQNVKISP QADFVNSDST VENKTETDMP SYEASKVEGQ NVELSETEKM SQYDSPEASA
EVYYDSIQSQ PLAAKPDSLL EEPEYVDGQI KHSLKRKVSN PSFIAAQSKF EELTSSTGSN
KAMTLSSKDD VLGEEGKTDI DSPDTTNTIK DHSLEDVTPA ELSGSECGTE LSVTSSLDTL
EKKSDAEGAE PRVEAKLLED DTFKTDQAEL IEIDVKDATS MGTVEDPKEK VENAKDEVEI
SATHHEPVIS TPDSKKRRAE DESGPQAYAL SEGALTPMTI TESQATPASQ ASSSVKARKG
KSEKSGSSQK RKVSKKITSS PKQEIGTGEA TEQEEGKEQK SGRRTSFGYD QEARESSGGK
NSLPRFMQPT QSAKAKVQEH NSPRSSPDLQ ERDVVSAKKR HSLPGVTNGK QVSPRIQRSA
SQAQQGTKDR KWQR
