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IQD8_ARATH
ID   IQD8_ARATH              Reviewed;         414 AA.
AC   Q9CAI2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Protein IQ-DOMAIN 8 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD8 {ECO:0000303|PubMed:16368012};
GN   Name=IQD8 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At1g72670 {ECO:0000312|Araport:AT1G72670};
GN   ORFNames=F28P22.14 {ECO:0000312|EMBL:AAG51853.1};
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;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2004) 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   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). 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   -!- INTERACTION:
CC       Q9CAI2; O23160: MYB73; NbExp=3; IntAct=EBI-25517196, EBI-25506855;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}. Nucleus envelope
CC       {ECO:0000269|PubMed:28115582}. Note=Recruits calmodulin (CaM2) to
CC       microtubules. {ECO:0000269|PubMed:28115582}.
CC   -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR   EMBL; AC010926; AAG51853.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35359.1; -; Genomic_DNA.
DR   EMBL; BT010652; AAR07516.1; -; mRNA.
DR   EMBL; AK175909; BAD43672.1; -; mRNA.
DR   PIR; D96751; D96751.
DR   RefSeq; NP_177411.1; NM_105926.5.
DR   AlphaFoldDB; Q9CAI2; -.
DR   SMR; Q9CAI2; -.
DR   IntAct; Q9CAI2; 1.
DR   STRING; 3702.AT1G72670.1; -.
DR   PaxDb; Q9CAI2; -.
DR   PRIDE; Q9CAI2; -.
DR   ProteomicsDB; 175098; -.
DR   EnsemblPlants; AT1G72670.1; AT1G72670.1; AT1G72670.
DR   GeneID; 843599; -.
DR   Gramene; AT1G72670.1; AT1G72670.1; AT1G72670.
DR   KEGG; ath:AT1G72670; -.
DR   Araport; AT1G72670; -.
DR   TAIR; locus:2030225; AT1G72670.
DR   eggNOG; ENOG502SIC6; Eukaryota.
DR   HOGENOM; CLU_037259_0_1_1; -.
DR   InParanoid; Q9CAI2; -.
DR   OMA; QSMSYNG; -.
DR   OrthoDB; 1101565at2759; -.
DR   PhylomeDB; Q9CAI2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAI2; baseline and differential.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR   GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:2000073; P:regulation of cytokinesis, site selection; IDA:TAIR.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF00612; IQ; 2.
DR   SMART; SM00015; IQ; 2.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..414
FT                   /note="Protein IQ-DOMAIN 8"
FT                   /id="PRO_0000453115"
FT   DOMAIN          92..120
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          121..143
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          144..169
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          40..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..132
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   REGION          155..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           14..21
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           336..343
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        157..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45894 MW;  BCD313F4AD8525F8 CRC64;
     MGGSGNWIKS LITNKKNITD DQEKNIKKKW KLWRTSSEGL ISSSKGFKSR GGSYGTPSLG
     SDPPSFSADD SFTAAVAAVI RAPPKDFFLV KREWAATRIQ AAFRAFLARQ ALRALKAVVR
     IQAIFRGRQV RKQADVTLRC MQALVRVQAR VRAHCNRGPS DGQELEKPSD QQKDDPAKQA
     EKGWCDSPGS INEVRTKLQM RQEGAIKRER AMVYALTHQP RTCPSPAKAS KQGSVKKNNG
     SCKSSPGWNW LDRWVADRPW EGRLMEGPTN SSENARKSES SVSEHDTVQV RKNNLTTRVL
     ARPPPMSSSA TSSESSSTSQ SPVPFSGSFL EEGGYYRKPS YMSLTQSIKA KQRRSGSSSS
     CSKTPFEKKQ SMSYNGDVNV RRSAGSDPLN NQWTDLYPPA QVTGRHMWAK SQRG
 
 
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