IQD6_ARATH
ID IQD6_ARATH Reviewed; 416 AA.
AC O64852;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Protein IQ-DOMAIN 6 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD6 {ECO:0000303|PubMed:16368012};
GN Name=IQD6 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At2g26180 {ECO:0000312|Araport:AT2G26180};
GN ORFNames=T1D16.18 {ECO:0000312|EMBL:AAC14531.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-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 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 [6]
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 [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 (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}. Nucleus, nuclear body
CC {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28115582}. Cell membrane
CC {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AC004484; AAC14531.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07805.1; -; Genomic_DNA.
DR EMBL; BT029734; ABM06004.1; -; mRNA.
DR PIR; D84657; D84657.
DR PIR; T02606; T02606.
DR RefSeq; NP_180187.1; NM_128176.3.
DR AlphaFoldDB; O64852; -.
DR IntAct; O64852; 480.
DR STRING; 3702.AT2G26180.1; -.
DR PaxDb; O64852; -.
DR PRIDE; O64852; -.
DR ProteomicsDB; 183272; -.
DR EnsemblPlants; AT2G26180.1; AT2G26180.1; AT2G26180.
DR GeneID; 817158; -.
DR Gramene; AT2G26180.1; AT2G26180.1; AT2G26180.
DR KEGG; ath:AT2G26180; -.
DR Araport; AT2G26180; -.
DR TAIR; locus:2057459; AT2G26180.
DR eggNOG; ENOG502QSVK; Eukaryota.
DR HOGENOM; CLU_037259_0_1_1; -.
DR InParanoid; O64852; -.
DR OMA; IEGATKC; -.
DR OrthoDB; 1101565at2759; -.
DR PhylomeDB; O64852; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64852; baseline and differential.
DR GO; GO:0016604; C:nuclear body; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0007105; P:cytokinesis, site selection; IDA:TAIR.
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; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..416
FT /note="Protein IQ-DOMAIN 6"
FT /id="PRO_0000453113"
FT DOMAIN 83..111
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 112..134
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 135..158
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 116..146
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 294..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..21
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 310..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46890 MW; 93A8B84C9671EB0C CRC64;
MGASGKWVKS IIGLKKLEKD EIEKGNGKNK KWKLWRTTSV DSWKGFRGKH RSDSDGVDSS
TVYSAAVATV LRAPPKDFKA VREEWAAIRI QTAFRGFLAR RALRALKGIV RLQALVRGRQ
VRKQAAVTLR CMQALVRVQA RVRARRVRMT VEGQAVQKLL DEHRTKSDLL KEVEEGWCDR
KGTVDDIKSK LQQRQEGAFK RERALAYALA QKQWRSTTSS NLKTNSSISY LKSQEFDKNS
WGWSWLERWM AARPWETRLM DTVDTAATPP PLPHKHLKSP ETADVVQVRR NNVTTRVSAK
PPPHMLSSSP GYEFNESSGS SSICTSTTPV SGKTGLVSDN SSSQAKKHKP SYMSLTESTK
AKRRTNRGLR QSMDEFQFMK NSGMFTGELK TSPSSDPFVS FSKPLGVPTR FEKPRG
