ID   IQD15_ARATH             Reviewed;         352 AA.
AC   Q9SG11;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein IQ-DOMAIN 15 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD15 {ECO:0000303|PubMed:16368012};
GN   Name=IQD15 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At3g49380 {ECO:0000312|EMBL:AEE78534.1};
GN   ORFNames=F2K15.240 {ECO:0000312|EMBL:CAB66417.1},
GN   T1G12.8 {ECO:0000312|EMBL:AAG52179.1};
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   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   [4]
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   [5]
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: Cell membrane {ECO:0000269|PubMed:28115582}.
CC       Nucleus envelope {ECO:0000269|PubMed:28115582}.
CC   -!- SIMILARITY: Belongs to the IQD family. {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; AC012329; AAG52179.1; -; Genomic_DNA.
DR   EMBL; AL132956; CAB66417.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78534.1; -; Genomic_DNA.
DR   PIR; T45843; T45843.
DR   RefSeq; NP_190507.1; NM_114798.2.
DR   AlphaFoldDB; Q9SG11; -.
DR   SMR; Q9SG11; -.
DR   STRING; 3702.AT3G49380.1; -.
DR   PaxDb; Q9SG11; -.
DR   PRIDE; Q9SG11; -.
DR   EnsemblPlants; AT3G49380.1; AT3G49380.1; AT3G49380.
DR   GeneID; 824100; -.
DR   Gramene; AT3G49380.1; AT3G49380.1; AT3G49380.
DR   KEGG; ath:AT3G49380; -.
DR   Araport; AT3G49380; -.
DR   TAIR; locus:2082946; AT3G49380.
DR   eggNOG; ENOG502QTQ9; Eukaryota.
DR   HOGENOM; CLU_776945_0_0_1; -.
DR   InParanoid; Q9SG11; -.
DR   OMA; HSIPNYM; -.
DR   OrthoDB; 1048958at2759; -.
DR   PhylomeDB; Q9SG11; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SG11; baseline and differential.
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   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13178; DUF4005; 1.
DR   Pfam; PF00612; IQ; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cell membrane; Membrane; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..352
FT                   /note="Protein IQ-DOMAIN 15"
FT                   /id="PRO_0000453121"
FT   DOMAIN          109..137
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          138..160
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          140..164
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   REGION          200..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  40765 MW;  0E79B3D257131986 CRC64;
     MGKTDGSSWF TAVKNVFRSP EKLIPRRINR RQDNDLVEEV EDELHQRPKR RKRRWLFKKV
     SSDPCAINVG INTTSTAINA IAAEETEKTV SPAAKETVFF CRTSVYLKRH VAAILIQTAF
     RGCLARTAVR ALKGVVKLQA LVRGHNVRRR TSITLQRVQA LVRIQALALD HRKKLTTKLG
     DEISYSHAFS KQMWRTMERE AHSESELEDK RPSRLNGYGY QETGRRMSTD QAIVEPVKIV
     EIDKYNNTYS HHQQLNDQTP RGNSFVTRQA HSIPNYMSTT ASTVARFRRP QSVPKQRSNR
     TCLDNNEPRL RLVRKRLSFH NDNPQSYGYI AGDGYFWYDI DKRTNAHEDF QY