IQD7_ARATH
ID IQD7_ARATH Reviewed; 371 AA.
AC Q2NND9; Q9LNQ7; Q9LQK1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein IQ-DOMAIN 7 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD7 {ECO:0000303|PubMed:16368012};
GN Name=IQD7 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At1g17480 {ECO:0000312|Araport:AT1G17480};
GN ORFNames=F1L3.18 {ECO:0000312|EMBL:AAF79484.1},
GN F28G4.3 {ECO:0000312|EMBL:AAF97308.1};
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], INTERACTION WITH CALMODULIN, GENE FAMILY, AND
RP 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 [2]
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 [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;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF97308.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY702665; AAW22635.1; -; mRNA.
DR EMBL; AC007843; AAF97308.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC022492; AAF79484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29597.1; -; Genomic_DNA.
DR EMBL; BT032868; ACD85594.1; -; mRNA.
DR PIR; C86311; C86311.
DR RefSeq; NP_173191.2; NM_101610.3.
DR AlphaFoldDB; Q2NND9; -.
DR SMR; Q2NND9; -.
DR STRING; 3702.AT1G17480.1; -.
DR PaxDb; Q2NND9; -.
DR PRIDE; Q2NND9; -.
DR EnsemblPlants; AT1G17480.1; AT1G17480.1; AT1G17480.
DR GeneID; 838321; -.
DR Gramene; AT1G17480.1; AT1G17480.1; AT1G17480.
DR KEGG; ath:AT1G17480; -.
DR Araport; AT1G17480; -.
DR TAIR; locus:2018837; AT1G17480.
DR eggNOG; ENOG502SIC6; Eukaryota.
DR HOGENOM; CLU_037259_0_1_1; -.
DR InParanoid; Q2NND9; -.
DR OMA; LTYAQSH; -.
DR OrthoDB; 1101565at2759; -.
DR PhylomeDB; Q2NND9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2NND9; baseline and differential.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
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 InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..371
FT /note="Protein IQ-DOMAIN 7"
FT /id="PRO_0000453114"
FT DOMAIN 93..121
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 122..144
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..141
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 41153 MW; 24B55F719F377F86 CRC64;
MGGSGNWIRS LISNRKPVND QQEKLSDKSS KKKWKLWRIS SESLASSSFK SRGSYAASSL
GSELPSFSAD EAFTTAMAAL IRAPPRDFLM VKREWASTRI QAAFRAFLAR QAFRALKAVV
RIQAIFRGRQ VRKQAAVTLR CMQALVRVQS RVRAHRRAPS DSLELKDPVK QTEKGWCGSP
RSIKEVKTKL QMKQEGAIKR ERAMVYALTH QSRTCPSPSG RAITHHGLRK SSPGWNWYDD
VGTFSRKSSE SSVLSEYETV TVRKNNLSST RVLARPPLLL PPVSSGMSYD SLHDETSTSS
TSQSPVAFSS SVLDGGGYYR KPSYMSLTQS TQAKQRQSGL SCNGDARRSA GSDQCTDLYP
PGNVWAKSQR S
