IQD5_ARATH
ID IQD5_ARATH Reviewed; 422 AA.
AC F4J061; A0A178VHN2; Q9LIE3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein IQ-DOMAIN 5 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD5 {ECO:0000303|PubMed:16368012};
GN Name=IQD5 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At3g22190 {ECO:0000312|Araport:AT3G22190};
GN ORFNames=MKA23.10 {ECO:0000312|EMBL:BAB03067.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [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).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=29976837; DOI=10.1104/pp.18.00558;
RA Liang H., Zhang Y., Martinez P., Rasmussen C.G., Xu T., Yang Z.;
RT "The microtubule-associated protein IQ67 DOMAIN5 modulates microtubule
RT dynamics and pavement cell shape.";
RL Plant Physiol. 177:1555-1568(2018).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=30407556; DOI=10.1093/jxb/ery395;
RA Mitra D., Klemm S., Kumari P., Quegwer J., Moeller B., Poeschl Y.,
RA Pflug P., Stamm G., Abel S., Buerstenbinder K.;
RT "Microtubule-associated protein IQ67 DOMAIN5 regulates morphogenesis of
RT leaf pavement cells in Arabidopsis thaliana.";
RL J. Exp. Bot. 70:529-543(2019).
CC -!- FUNCTION: May be involved in cooperative interactions with calmodulins
CC or calmodulin-like proteins (By similarity). Recruits calmodulin (CaM)
CC calcium sensor proteins to cortical microtubule arrays, thus being a
CC potential scaffold in cellular signaling and trafficking
CC (PubMed:29976837, PubMed:30407556). Binds to microtubules (MTs) and
CC promotes MT assembly and dynamics to modulate pavement cell (PC)
CC morphogenesis via cellulose deposition-dependent anisotropic cell
CC expansion triggered by cellulose synthase complexes (CSCs)
CC (PubMed:29976837, PubMed:30407556). 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:29976837, ECO:0000269|PubMed:30407556}.
CC -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of Ca(2+)
CC and CaM-like proteins. {ECO:0000269|PubMed:29976837,
CC ECO:0000269|PubMed:30407556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582,
CC ECO:0000269|PubMed:29976837, ECO:0000269|PubMed:30407556}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:29976837}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:29976837}.
CC Note=Localized to microtubules (MTs) arrays in dynamic pattern,
CC including cortical MT in leaf pavement and hypocotyl epidermal cells
CC (in a discontinuous and punctate manner corresponding to indentation
CC regions), as well as preprophase bands, mitotic spindles, and
CC phragmoplasts of mitotic cells in root tips.
CC {ECO:0000269|PubMed:29976837, ECO:0000269|PubMed:30407556}.
CC -!- TISSUE SPECIFICITY: Expressed mostly in vegetative tissues including
CC older parts of the root, cotyledons, leaves and shoot apical meristems
CC (SAM) (PubMed:30407556). Present at low levels in pollen, siliques and
CC seeds (PubMed:30407556). {ECO:0000269|PubMed:30407556}.
CC -!- DEVELOPMENTAL STAGE: In leaves and hypocotyls, mostly observed in
CC vascular tissues (PubMed:30407556). In root tips, restricted to the
CC lateral root cap of primary and lateral root meristems
CC (PubMed:30407556). {ECO:0000269|PubMed:30407556}.
CC -!- DISRUPTION PHENOTYPE: Abnormal pavement cell morphogenesis in
CC cotyledons characterized by reduced interdigitation associated with
CC altered microtubules organization and dynamics and reduced rates of
CC cellulose deposition in anticlinal cell walls thus correleted with a
CC reduced anisotropic cell expansion (PubMed:29976837, PubMed:30407556).
CC Hypersensitivity to the microtubule-disrupting drug oryzalin
CC (PubMed:29976837). {ECO:0000269|PubMed:29976837,
CC ECO:0000269|PubMed:30407556}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03067.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001306; BAB03067.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76599.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76600.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63858.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63859.1; -; Genomic_DNA.
DR RefSeq; NP_001189946.1; NM_001203017.2.
DR RefSeq; NP_001319617.1; NM_001338571.1.
DR RefSeq; NP_001325926.1; NM_001338572.1.
DR RefSeq; NP_188858.4; NM_113116.4.
DR AlphaFoldDB; F4J061; -.
DR SMR; F4J061; -.
DR STRING; 3702.AT3G22190.2; -.
DR PaxDb; F4J061; -.
DR PRIDE; F4J061; -.
DR ProteomicsDB; 191482; -.
DR EnsemblPlants; AT3G22190.1; AT3G22190.1; AT3G22190.
DR EnsemblPlants; AT3G22190.2; AT3G22190.2; AT3G22190.
DR EnsemblPlants; AT3G22190.3; AT3G22190.3; AT3G22190.
DR EnsemblPlants; AT3G22190.4; AT3G22190.4; AT3G22190.
DR GeneID; 821783; -.
DR Gramene; AT3G22190.1; AT3G22190.1; AT3G22190.
DR Gramene; AT3G22190.2; AT3G22190.2; AT3G22190.
DR Gramene; AT3G22190.3; AT3G22190.3; AT3G22190.
DR Gramene; AT3G22190.4; AT3G22190.4; AT3G22190.
DR KEGG; ath:AT3G22190; -.
DR Araport; AT3G22190; -.
DR TAIR; locus:2090409; AT3G22190.
DR eggNOG; ENOG502QT9B; Eukaryota.
DR HOGENOM; CLU_037259_1_1_1; -.
DR InParanoid; F4J061; -.
DR OMA; NATCATI; -.
DR OrthoDB; 1003690at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J061; baseline and differential.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR GO; GO:0090436; P:leaf pavement cell development; IMP:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IMP:UniProtKB.
DR GO; GO:0072699; P:protein localization to cortical microtubule cytoskeleton; IMP:UniProtKB.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF00612; IQ; 1.
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..422
FT /note="Protein IQ-DOMAIN 5"
FT /id="PRO_0000453112"
FT DOMAIN 87..115
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 116..138
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 139..164
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 137..151
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 269..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..30
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 275..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46899 MW; 4CF2142BDDD8C295 CRC64;
MGASGRWIKA LVGFTKSDKS RSSKKDENVK VATKSRFGRK NSVDFDFEKF QDGFEDSNTR
SMVDTGVSTS TSLQSYGGVA YDEQSRENRA ATRIQTAYRG FLARRALRAL KGLVRLQALV
RGHAVRKQAA VTLRCMQALV RVQARVRARR VRLALELESE TSQQTLQQQL ADEARVREIE
EGWCDSIGSV EQIQAKLLKR QEAAAKRERA MAYALTHQWQ AGTRLLSAHS GFQPDKNNWG
WNWLERWMAV RPWENRFLDS NLRDDAKLGE NGMEQSENVP KTQIKSVSKM PNTSNLVSGV
SSQMTGPCQS DGDSSSPGIS SSIPVVSKAK SKPAKDDLAV EVNSRPGAGP RSHSNPKERS
REPNRSSKER LSLPNSGKSL GSQSTKANRA GKLTPASQKV VEEKSAQNQR RRNSDPIKQR
LA
