IQD21_ARATH
ID IQD21_ARATH Reviewed; 471 AA.
AC Q9ASW3; Q9M3A6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein IQ-DOMAIN 21 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD21 {ECO:0000303|PubMed:16368012};
DE AltName: Full=Protein GROWTH CONTROLLED BY ABSCISIC ACID 2 {ECO:0000303|PubMed:11429606};
DE AltName: Full=Protein GUARD CELL ASSOCIATED 2 {ECO:0000303|PubMed:10963598};
GN Name=IQD21 {ECO:0000303|PubMed:16368012};
GN Synonyms=GCA2 {ECO:0000303|PubMed:10963598, ECO:0000303|PubMed:11429606};
GN OrderedLocusNames=At3g49260 {ECO:0000312|Araport:AT3G49260};
GN ORFNames=F2K15.120 {ECO:0000312|EMBL:CAB66405.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Moskal W.A. Jr., Smart L.B.;
RT "Characterization of genes associated with guard cell function and
RT differentiation in Arabidopsis thaliana.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10963598; DOI=10.1038/35021067;
RA Pei Z.M., Murata Y., Benning G., Thomine S., Kluesener B., Allen G.J.,
RA Grill E., Schroeder J.I.;
RT "Calcium channels activated by hydrogen peroxide mediate abscisic acid
RT signalling in guard cells.";
RL Nature 406:731-734(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11429606; DOI=10.1038/35082575;
RA Allen G.J., Chu S.P., Harrington C.L., Schumacher K., Hoffmann T.,
RA Tang Y.Y., Grill E., Schroeder J.I.;
RT "A defined range of guard cell calcium oscillation parameters encodes
RT stomatal movements.";
RL Nature 411:1053-1057(2001).
RN [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16651523; DOI=10.1073/pnas.0602225103;
RA Young J.J., Mehta S., Israelsson M., Godoski J., Grill E., Schroeder J.I.;
RT "CO(2) signaling in guard cells: calcium sensitivity response modulation, a
RT Ca(2+)-independent phase, and CO(2) insensitivity of the gca2 mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7506-7511(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18088305; DOI=10.1111/j.1365-313x.2007.03399.x;
RA Chung S., Parish R.W.;
RT "Combinatorial interactions of multiple cis-elements regulating the
RT induction of the Arabidopsis XERO2 dehydrin gene by abscisic acid and
RT cold.";
RL Plant J. 54:15-29(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19302418; DOI=10.1111/j.1365-313x.2009.03872.x;
RA Siegel R.S., Xue S., Murata Y., Yang Y., Nishimura N., Wang A.,
RA Schroeder J.I.;
RT "Calcium elevation-dependent and attenuated resting calcium-dependent
RT abscisic acid induction of stomatal closure and abscisic acid-induced
RT enhancement of calcium sensitivities of S-type anion and inward-rectifying
RT K channels in Arabidopsis guard cells.";
RL Plant J. 59:207-220(2009).
RN [12]
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 [13]
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). Involved in abscisic acid
CC (ABA)-mediated signaling pathways leading to the production of hydrogen
CC peroxide H(2)O(2) and the subsequent [Ca(2+)] cytoplasmic oscillations-
CC dependent regulation of stomatal closure (PubMed:10963598,
CC PubMed:11429606). Required for [CO(2)] modulation of the cytosolic
CC Ca(2+) transient rate and for high CO(2)-induced stomatal closing
CC (PubMed:16651523, PubMed:19302418). Essential for both cold and ABA
CC induction of XERO2 (PubMed:18088305). May associate with nucleic acids
CC and regulate gene expression at the transcriptional or post-
CC transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32,
CC ECO:0000269|PubMed:10963598, ECO:0000269|PubMed:11429606,
CC ECO:0000269|PubMed:16651523, ECO:0000269|PubMed:18088305,
CC ECO:0000269|PubMed:19302418}.
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:28115582}. Cell membrane
CC {ECO:0000269|PubMed:28115582}.
CC -!- DISRUPTION PHENOTYPE: Insensitivity to abscisic acid (ABA) associated
CC with disrupted activation of Ca(2+) channels by hydrogen peroxide
CC H(2)O(2), increased frequencies but reduced transient duration of
CC [Ca(2+)] cytoplasmic oscillations, and leading to altered ABA- and
CC H(2)O(2)-induced stomatal closing (PubMed:10963598, PubMed:11429606).
CC Abnormal [CO(2)] modulation of the cytosolic Ca(2+) transient rate and
CC strong impairment in high CO(2)-induced stomatal closing
CC (PubMed:16651523, PubMed:19302418). Reduced induction of XERO2 in
CC response to cold and ABA (PubMed:18088305).
CC {ECO:0000269|PubMed:10963598, ECO:0000269|PubMed:11429606,
CC ECO:0000269|PubMed:16651523, ECO:0000269|PubMed:18088305,
CC ECO:0000269|PubMed:19302418}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY484700; AAR32943.1; -; mRNA.
DR EMBL; AL132956; CAB66405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78516.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78517.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65033.1; -; Genomic_DNA.
DR EMBL; AF361635; AAK32803.1; -; mRNA.
DR EMBL; BT000602; AAN18171.1; -; mRNA.
DR EMBL; AY087861; AAM65413.1; -; mRNA.
DR PIR; T45831; T45831.
DR RefSeq; NP_001319716.1; NM_001339406.1.
DR RefSeq; NP_566917.1; NM_114785.4.
DR RefSeq; NP_974405.1; NM_202676.1.
DR AlphaFoldDB; Q9ASW3; -.
DR SMR; Q9ASW3; -.
DR IntAct; Q9ASW3; 2.
DR PRIDE; Q9ASW3; -.
DR ProteomicsDB; 181544; -.
DR EnsemblPlants; AT3G49260.1; AT3G49260.1; AT3G49260.
DR EnsemblPlants; AT3G49260.2; AT3G49260.2; AT3G49260.
DR EnsemblPlants; AT3G49260.4; AT3G49260.4; AT3G49260.
DR GeneID; 824087; -.
DR Gramene; AT3G49260.1; AT3G49260.1; AT3G49260.
DR Gramene; AT3G49260.2; AT3G49260.2; AT3G49260.
DR Gramene; AT3G49260.4; AT3G49260.4; AT3G49260.
DR KEGG; ath:AT3G49260; -.
DR Araport; AT3G49260; -.
DR OMA; KREAGWH; -.
DR PhylomeDB; Q9ASW3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ASW3; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR InterPro; IPR025064; DUF4005.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF13178; DUF4005; 1.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00015; IQ; 2.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Nucleus; Reference proteome; Repeat;
KW Stress response.
FT CHAIN 1..471
FT /note="Protein IQ-DOMAIN 21"
FT /id="PRO_0000453126"
FT DOMAIN 119..147
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 148..170
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..145
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 196..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..9
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 52094 MW; 556415C17392BBCF CRC64;
MGKKGSGGWF STVKKKVFKS SPKDSKRENN IGSNNADIWQ QQHDTQEVVS FEHFPAESSP
EISHDVESTA STPATNVGDR KHAMAVAIAT AAAAEAAVAA AQAAAKVVRL AGYNRQTEED
SAAVLIQSHY RGYLARRALR ALKGLVRLQA LVRGNHVRKQ AQMTMKCMQA LVRVQGRVRA
RRLQVAHDRF KKQFEEEEKR SGMEKPNKGF ANLKTEREKP KKLHEVNRTS LYQTQGKEKE
RSEGMMKRER ALAYAYTYQR QMQHTNSEEG IGLSSNGPDR NQWAWNWLDH WMSSQPYTGR
QTGPGPGPGQ YNPPPYPPFP TAAATTTSDD VSEKTVEMDV TTPTSLKGNI IGLIDREYID
LGSYRQGHKQ RKSPTHIPSY MAPTASAKAK VRDQGPTVKL QGTSFMPYWN SSTKNGSVNG
SGCDSSSSGG AITTGYPGPR SPNPKSDIRR KPVSPSQSPT GFGKRGWRHD H
