IQD13_ARATH
ID IQD13_ARATH Reviewed; 517 AA.
AC Q9M199;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Protein IQ-DOMAIN 13 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD13 {ECO:0000303|PubMed:16368012};
GN Name=IQD13 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At3g59690 {ECO:0000312|Araport:AT3G59690};
GN ORFNames=T16L24.240 {ECO:0000312|EMBL:CAB75466.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
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 [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CALMODULIN.
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). Regulates the formation of
CC oval xylem secondary cell-wall deposition pits through microtubule-
CC dependent lateral inhibition of Rho GTPase domains, thus confining the
CC area of active ROP domains within the lattice of the cortical
CC microtubules (PubMed:28803875). May associate with nucleic acids and
CC regulate gene expression at the transcriptional or post-transcriptional
CC level (By similarity). {ECO:0000250|UniProtKB:Q9SF32,
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 ECO:0000269|PubMed:28803875}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28115582, ECO:0000269|PubMed:28803875}.
CC Note=Recruits calmodulin (CaM2) to microtubules (PubMed:28115582).
CC Associates with cortical microtubules and the plasma membrane to
CC laterally restrict the localization of ROP GTPase domains
CC (PubMed:28803875). {ECO:0000269|PubMed:28115582,
CC ECO:0000269|PubMed:28803875}.
CC -!- TISSUE SPECIFICITY: Expressed in vessels of roots, cotyledons and
CC leaves, as well as in trichomes. {ECO:0000269|PubMed:28803875}.
CC -!- DEVELOPMENTAL STAGE: In roots, mostly localized to microtubule-like
CC filaments beneath the secondary cell walls of metaxylem cells.
CC {ECO:0000269|PubMed:28803875}.
CC -!- DISRUPTION PHENOTYPE: Formation of abnormally large and round secondary
CC cell-wall pits in roots metaxylem vessels (PubMed:28803875). The double
CC mutant iqd13 iqd14 exhibits larger secondary cell-wall pits
CC (PubMed:28803875). {ECO:0000269|PubMed:28803875}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AL138659; CAB75466.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79956.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64846.1; -; Genomic_DNA.
DR EMBL; AY128329; AAM91532.1; -; mRNA.
DR EMBL; BT001176; AAN65063.1; -; mRNA.
DR PIR; T49310; T49310.
DR RefSeq; NP_001326850.1; NM_001339994.1.
DR RefSeq; NP_191528.1; NM_115831.3.
DR AlphaFoldDB; Q9M199; -.
DR SMR; Q9M199; -.
DR STRING; 3702.AT3G59690.1; -.
DR PaxDb; Q9M199; -.
DR PRIDE; Q9M199; -.
DR ProteomicsDB; 185832; -.
DR EnsemblPlants; AT3G59690.1; AT3G59690.1; AT3G59690.
DR EnsemblPlants; AT3G59690.2; AT3G59690.2; AT3G59690.
DR GeneID; 825138; -.
DR Gramene; AT3G59690.1; AT3G59690.1; AT3G59690.
DR Gramene; AT3G59690.2; AT3G59690.2; AT3G59690.
DR KEGG; ath:AT3G59690; -.
DR Araport; AT3G59690; -.
DR TAIR; locus:2097478; AT3G59690.
DR eggNOG; ENOG502R9C0; Eukaryota.
DR HOGENOM; CLU_025762_0_0_1; -.
DR InParanoid; Q9M199; -.
DR OMA; SHQLWKN; -.
DR OrthoDB; 885729at2759; -.
DR PhylomeDB; Q9M199; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M199; baseline and differential.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0051592; P:response to calcium ion; IEP:TAIR.
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 Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..517
FT /note="Protein IQ-DOMAIN 13"
FT /id="PRO_0000453120"
FT DOMAIN 168..196
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 197..218
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..11
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 81..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 58505 MW; 6044EC65798DC56B CRC64;
MGKKGSWFSA IKRVFTPHSK EKQLSNNNQE PEIKSENKEK KKKGFGKKLR NGETNSFLPI
FRQPSSIEKI LSEAEREHNL VFRPPTPTDR ANSSSTSVAS PLVRPASPKV PSQRYVSSPK
PISPRVAYPQ VHYPKPPSPK PPSPRAVSPR IVQRREFVHR PEPSLLVKNA YAIKIQAAFR
GYMARRSFRA LKGLVRLQGV VRGHSVKRQT MNAMKYMQLL VRVQTQVQSR RIQMLENRAR
NDKDDTKLVS SRMSDDWDDS VLTKEEKDVR LHRKIDAMIK RERSMAYAYS HQLWKNSPKS
AQDIRTSGFP LWWNWVDRQK NQNQPFRLTP TRPSLSPQPQ SSNQNHFRLN NSFDTSTPNS
SKSTFVTPSR PIHTPQPYSS SVSRYSRGGG RATQDSPFKD DDSLTSCPPF SAPSYMAPTV
SAKAKLRANS NPKERMDRTP VSTNEKRRSS FPLGSFKWNK GSLFMSNNSN NKGPGSSSSG
AVVLEKHKTL KSVGNLSIDS TVSMPATIGR RAFNRFA
