IQD29_ARATH
ID IQD29_ARATH Reviewed; 597 AA.
AC A0A1P8B0B7; O64504; Q56Y97;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Protein IQ-DOMAIN 29 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD29 {ECO:0000303|PubMed:16368012};
GN Name=IQD29 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At2g02790 {ECO:0000312|Araport:AT2G02790};
GN ORFNames=T20F6.7 {ECO:0000312|EMBL:AAC05343.1};
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] OF 1-117.
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 (MAR-2005) 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 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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=24134884; DOI=10.1104/pp.113.225607;
RA Hamada T., Nagasaki-Takeuchi N., Kato T., Fujiwara M., Sonobe S., Fukao Y.,
RA Hashimoto T.;
RT "Purification and characterization of novel microtubule-associated proteins
RT from Arabidopsis cell suspension cultures.";
RL Plant Physiol. 163:1804-1816(2013).
RN [7]
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 [8]
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:24134884, ECO:0000269|PubMed:28115582}. Cell
CC membrane {ECO:0000269|PubMed:28115582}. Note=Associates to cortical
CC microtubules (MTs). {ECO:0000269|PubMed:24134884}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05343.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002521; AAC05343.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; ANM62330.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62331.1; -; Genomic_DNA.
DR EMBL; AK221426; BAD94424.1; -; mRNA.
DR PIR; T00849; T00849.
DR RefSeq; NP_001324494.1; NM_001335145.1.
DR RefSeq; NP_001324495.1; NM_001335144.1.
DR AlphaFoldDB; A0A1P8B0B7; -.
DR ProteomicsDB; 177554; -.
DR EnsemblPlants; AT2G02790.2; AT2G02790.2; AT2G02790.
DR EnsemblPlants; AT2G02790.3; AT2G02790.3; AT2G02790.
DR GeneID; 814808; -.
DR Gramene; AT2G02790.2; AT2G02790.2; AT2G02790.
DR Gramene; AT2G02790.3; AT2G02790.3; AT2G02790.
DR KEGG; ath:AT2G02790; -.
DR Araport; AT2G02790; -.
DR OMA; LVRWTIS; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A0A1P8B0B7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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; 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..597
FT /note="Protein IQ-DOMAIN 29"
FT /id="PRO_0000453134"
FT DOMAIN 106..134
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 135..153
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 157..183
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..173
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 268..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..271
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 356..363
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 286..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65267 MW; 3DF037400D6AC4CA CRC64;
MGKTPSPGKW IKSLLGKKSS KSSLEKGGEK LRSAKKEELV VKVKDNNVSK LPTEPPVVSS
QEVAATQTVV VPDVVIAEKQ LSGDIEGDES SNVNLESGND SEEVKLEEAA TKVQAALRAQ
QAREESQNLK GITRVQAVIR GHLVRRQAVA TYSCIWGIVK VQALVRGKKA RSSETVAQLQ
KTNTETETSE TLQGSTYSWM ENPTKLSMID KLLVSSPTTL PLKIQYSPED PNSAKVWLGR
WTQLQVWAPG PLVVKNLVPK SQTKKRSFQA VEAEKGKLKR GVRKPTGVST TANSSTSRST
ADNEKPKRTV RKASTLGKEL SKIENDKSKQ SSRKSTSAIK EGSSVEVKDE KPRISHKKAS
LSNGIGKATR KSAEKKKEIA DAVQKELPIE EVSVSLVDAP EDEKMNLIPV TISKESDLDK
DEKSLVLDKP EQDELRTAER DDKAEEELKT AERDDSAEEK IQEPDAQISS ENGNVASENT
KPSDRRASLP AKIENHHQDD GLTQSGRKIP SYMAPTASAK ARIRGQGSPR IAQEKPEKNG
TTRRHSLPPA ANGKLSTMSP RAHRLLIASA KGSMNSDRSF SSSKDIGDKS TKAEWKR
