IQD14_ARATH
ID IQD14_ARATH Reviewed; 668 AA.
AC Q8LPG9; O22835;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein IQ-DOMAIN 14 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD14 {ECO:0000303|PubMed:16368012};
GN Name=IQD14 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At2g43680 {ECO:0000312|Araport:AT2G43680};
GN ORFNames=F18O19.21 {ECO:0000312|EMBL:AAB64038.1};
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28803875; DOI=10.1016/j.cub.2017.06.059;
RA Sugiyama Y., Wakazaki M., Toyooka K., Fukuda H., Oda Y.;
RT "A novel plasma membrane-anchored protein regulates xylem cell-wall
RT deposition through microtubule-dependent lateral inhibition of Rho GTPase
RT domains.";
RL Curr. Biol. 27:2522.e4-2528.e4(2017).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [9]
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 (PubMed:28115582). Regulates cell and organ
CC shapes (prevents twisting) in aerial parts probably by regulating
CC transverse microtubules (MT) arrays alignment (PubMed:28115582).
CC Regulates the formation of oval xylem secondary cell-wall deposition
CC pits through microtubule-dependent lateral inhibition of Rho GTPase
CC domains, thus confining the area of active ROP domains within the
CC lattice of the cortical microtubules (PubMed:28803875). May associate
CC with nucleic acids and regulate gene expression at the transcriptional
CC or post-transcriptional level (By similarity).
CC {ECO:0000250|UniProtKB:Q9SF32, ECO:0000269|PubMed:28115582,
CC ECO:0000269|PubMed:28803875}.
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: Cell membrane {ECO:0000269|PubMed:28115582}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LPG9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, cotyledons, leaves and
CC petioles. {ECO:0000269|PubMed:28115582}.
CC -!- DISRUPTION PHENOTYPE: The double mutant iqd13 iqd14 exhibits abnormally
CC large and round secondary cell-wall pits in roots metaxylem vessels.
CC {ECO:0000269|PubMed:28803875}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64038.1; 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; AC002333; AAB64038.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10305.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10307.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62407.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62408.1; -; Genomic_DNA.
DR EMBL; AY099822; AAM20673.1; -; mRNA.
DR EMBL; BT008408; AAP37767.1; -; mRNA.
DR EMBL; AK226517; BAE98657.1; -; mRNA.
DR PIR; B84869; B84869.
DR RefSeq; NP_001154574.1; NM_001161102.2. [Q8LPG9-1]
DR RefSeq; NP_001318416.1; NM_001337049.1. [Q8LPG9-1]
DR RefSeq; NP_001324566.1; NM_001337050.1. [Q8LPG9-1]
DR RefSeq; NP_973681.2; NM_201952.2. [Q8LPG9-1]
DR AlphaFoldDB; Q8LPG9; -.
DR SMR; Q8LPG9; -.
DR BioGRID; 4306; 2.
DR STRING; 3702.AT2G43680.1; -.
DR iPTMnet; Q8LPG9; -.
DR PaxDb; Q8LPG9; -.
DR PRIDE; Q8LPG9; -.
DR ProteomicsDB; 228832; -. [Q8LPG9-1]
DR EnsemblPlants; AT2G43680.2; AT2G43680.2; AT2G43680. [Q8LPG9-1]
DR EnsemblPlants; AT2G43680.3; AT2G43680.3; AT2G43680. [Q8LPG9-1]
DR EnsemblPlants; AT2G43680.4; AT2G43680.4; AT2G43680. [Q8LPG9-1]
DR EnsemblPlants; AT2G43680.5; AT2G43680.5; AT2G43680. [Q8LPG9-1]
DR GeneID; 818970; -.
DR Gramene; AT2G43680.2; AT2G43680.2; AT2G43680. [Q8LPG9-1]
DR Gramene; AT2G43680.3; AT2G43680.3; AT2G43680. [Q8LPG9-1]
DR Gramene; AT2G43680.4; AT2G43680.4; AT2G43680. [Q8LPG9-1]
DR Gramene; AT2G43680.5; AT2G43680.5; AT2G43680. [Q8LPG9-1]
DR KEGG; ath:AT2G43680; -.
DR Araport; AT2G43680; -.
DR eggNOG; ENOG502R9C0; Eukaryota.
DR HOGENOM; CLU_025762_0_0_1; -.
DR InParanoid; Q8LPG9; -.
DR PhylomeDB; Q8LPG9; -.
DR PRO; PR:Q8LPG9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LPG9; baseline and differential.
DR Genevisible; Q8LPG9; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:2000652; P:regulation of secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0010089; P:xylem development; 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; 1.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Repeat.
FT CHAIN 1..668
FT /note="Protein IQ-DOMAIN 14"
FT /id="PRO_0000311121"
FT DOMAIN 321..350
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 343..372
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..11
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 16..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74282 MW; 98456CD41AD79B2E CRC64;
MVKKGSWFSA IKRVFTPHSK EKLANEPERK SGKEKKKKGF GKLRHGETNS FLPIFREPSS
IEKILGEAER DHNLVFRPPT PDRPNPYSAS PPPRPASPRV ASPRPTSPRV ASPRVPSPRA
EVPRTLSPKP PSPRAEVPRS LSPKPPSPRA DLPRSLSPKP FDRSKPSSAS ANAPPTLRPA
STRVPSQRIT PHSVPSPRPS SPRGASPQAI SSKPPSPRAE PPTLDTPRPP SPRAASLRAD
PPRLDAARPT TPRPPSPLAD APRLDAPRPT TPKPPSPRSD PPRLDAPRPT TPKPPSPRSV
SPRAVQRREI VYRPEPTLPV QHASATKIQG AFRGYMARKS FRALKGLVRL QGVVRGYSVK
RQTINAMKYM QQVVRVQSQI QSRRIKMLEN QAQVEKDEAK WAASEAGNDN WDDSVLTKEE
RDSRSQRKTD AIIKRERSMA YAYSRKLWKN SPKSTQDNRS FPQWWNWVDR QNPLASPAPS
YSQPQRDFRL TPSRLCPSPL SQSSKQHHIR LDNHFDTSTP RSSRSTFHTP SRPIHTGTSR
YSRGRLRGQD SPFKDDDSLT SCPPFPSYMA PTVSAKAKVR PNSNPKERVM GTPVSEKRRM
SYPPTQDTFR WNKGSLVMSN SSSHRGPGSP GGVVLEKHKT LKSVGNLSIG STASMATTVG
RKEFNRFV
