IQD30_ARATH
ID IQD30_ARATH Reviewed; 572 AA.
AC Q501D2; B9DH53; Q2NND8; Q9M9V3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein IQ-DOMAIN 30 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD30 {ECO:0000303|PubMed:16368012};
GN Name=IQD30 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At1g18840 {ECO:0000312|Araport:AT1G18840};
GN ORFNames=F6A14.7 {ECO:0000312|EMBL:AAF27097.1};
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; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-563, INTERACTION WITH CALMODULIN, GENE
RP 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 [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 envelope {ECO:0000269|PubMed:28115582}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27097.1; 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; AC011809; AAF27097.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29769.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29770.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60334.1; -; Genomic_DNA.
DR EMBL; AK317400; BAH20070.1; -; mRNA.
DR EMBL; BT022035; AAY25447.1; -; mRNA.
DR EMBL; AY702666; AAW22636.1; -; mRNA.
DR PIR; C86322; C86322.
DR RefSeq; NP_001031067.1; NM_001035990.2.
DR RefSeq; NP_001322630.1; NM_001332375.1.
DR RefSeq; NP_173318.2; NM_101741.4.
DR AlphaFoldDB; Q501D2; -.
DR STRING; 3702.AT1G18840.1; -.
DR PaxDb; Q501D2; -.
DR PRIDE; Q501D2; -.
DR ProteomicsDB; 174847; -.
DR EnsemblPlants; AT1G18840.1; AT1G18840.1; AT1G18840.
DR EnsemblPlants; AT1G18840.2; AT1G18840.2; AT1G18840.
DR EnsemblPlants; AT1G18840.3; AT1G18840.3; AT1G18840.
DR GeneID; 838465; -.
DR Gramene; AT1G18840.1; AT1G18840.1; AT1G18840.
DR Gramene; AT1G18840.2; AT1G18840.2; AT1G18840.
DR Gramene; AT1G18840.3; AT1G18840.3; AT1G18840.
DR KEGG; ath:AT1G18840; -.
DR Araport; AT1G18840; -.
DR TAIR; locus:2034929; AT1G18840.
DR eggNOG; ENOG502QTUQ; Eukaryota.
DR HOGENOM; CLU_026881_0_0_1; -.
DR InParanoid; Q501D2; -.
DR OMA; VPHIEVE; -.
DR OrthoDB; 533192at2759; -.
DR PhylomeDB; Q501D2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q501D2; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; 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 InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13178; DUF4005; 1.
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..572
FT /note="Protein IQ-DOMAIN 30"
FT /id="PRO_0000453135"
FT DOMAIN 108..136
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 137..154
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 75..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 282..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 183
FT /note="R -> G (in Ref. 3; BAH20070)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="K -> R (in Ref. 3; BAH20070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 62732 MW; 188936165BBB8BBC CRC64;
MGKPARWLKS VLLGKKPSKS SGSKDKERIV NGKEVVVISK IEESDVVSDL SSIGNAAVYT
SGIVETQNLK HEDVSDDEIQ VSEVQPTDSQ DVASVPDDSL SESEKIQQEI AAVTVQAAYR
GYLARRAFKI LKGIIRLQAL IRGHMVRRQA VSTLCCVMGI VRLQALARGR EIRHSDIGVE
VQRKCHLHHQ PLENKANSVV DTHSYLGINK LTGNAFAQKL LASSPNVLPL SLDNDSSNSI
WLENWSASCF WKPVPQPKKA SLRKSQKKFA SNPQIVEAEF ARPKKSVRKV PSSNLDNSSV
AQTSSELEKP KRSFRKVSTS QSVEPLPSMD NPQVDLEKVK RGLRKVHNPV VENSIQPQLV
PQIAVEKPNG SLEESVNAFD EEKEDEVAET VVQQPEELIQ THTPLGTNES LDSTLVNQIE
ESEENVMAEE KEDVKEERTP KQNHKENSAG KENQKSGKKA SSVTATQTAE FQESGNGNQT
SSPGIPSYMQ ATKSAKAKLR LQGSSSPRQL GTTEKASRRY SLPSSGNSAK ITSHSPKTRV
SNSSGKSGNK TEKTLLSSRE GNGKATPVEW KR
