IQD12_ARATH
ID IQD12_ARATH Reviewed; 404 AA.
AC A0A1P8BH03; Q9LZB4;
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 12 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD12 {ECO:0000303|PubMed:16368012};
GN Name=IQD12 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At5g03960 {ECO:0000312|Araport:AT5G03960};
GN ORFNames=F8F6.170 {ECO:0000312|EMBL:CAB85516.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Cell membrane {ECO:0000269|PubMed:28115582}. Note=Recruits calmodulin
CC (CaM2) at plasma membrane subdomains. {ECO:0000250|UniProtKB:F4JMV6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1P8BH03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1P8BH03-2; Sequence=VSP_061103;
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR EMBL; AL162873; CAB85516.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90676.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70876.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70877.1; -; Genomic_DNA.
DR PIR; T48423; T48423.
DR RefSeq; NP_001332454.1; NM_001342739.1. [A0A1P8BH03-1]
DR RefSeq; NP_001332455.1; NM_001342740.1. [A0A1P8BH03-1]
DR RefSeq; NP_196016.1; NM_120478.4. [A0A1P8BH03-2]
DR AlphaFoldDB; A0A1P8BH03; -.
DR IntAct; A0A1P8BH03; 1.
DR STRING; 3702.AT5G03960.1; -.
DR EnsemblPlants; AT5G03960.1; AT5G03960.1; AT5G03960. [A0A1P8BH03-2]
DR EnsemblPlants; AT5G03960.2; AT5G03960.2; AT5G03960. [A0A1P8BH03-1]
DR EnsemblPlants; AT5G03960.3; AT5G03960.3; AT5G03960. [A0A1P8BH03-1]
DR GeneID; 830275; -.
DR Gramene; AT5G03960.1; AT5G03960.1; AT5G03960. [A0A1P8BH03-2]
DR Gramene; AT5G03960.2; AT5G03960.2; AT5G03960. [A0A1P8BH03-1]
DR Gramene; AT5G03960.3; AT5G03960.3; AT5G03960. [A0A1P8BH03-1]
DR KEGG; ath:AT5G03960; -.
DR Araport; AT5G03960; -.
DR TAIR; locus:2150650; AT5G03960.
DR eggNOG; ENOG502QS6F; Eukaryota.
DR HOGENOM; CLU_024547_0_0_1; -.
DR OMA; LQMEQYT; -.
DR OrthoDB; 986134at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A0A1P8BH03; baseline and differential.
DR GO; GO:0005634; C:nucleus; 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 PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell membrane; Membrane; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..404
FT /note="Protein IQ-DOMAIN 12"
FT /id="PRO_0000453119"
FT DOMAIN 108..135
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 136..158
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 8..25
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT MOTIF 11..18
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 226..233
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT VAR_SEQ 25
FT /note="Missing (in isoform 2)"
FT /id="VSP_061103"
SQ SEQUENCE 404 AA; 46169 MW; 7AD8DE4A41FCA7D8 CRC64;
MAKRRSWFGW MKRLFICEAK ARAEKKPRRL RWVFKRLKLR PQLATCGQET RTLNEATQDQ
RKHAMNVAIA TAAAAEAAVA AAKAAAEVVR MAGNAFTSQH FVKKLAPNVA AIKIQSAFRA
SLARKALRAL KALVRLQAIV RGRAVRRKVS ALLKSSHSNK ASTSNIIQRQ TERKHWSNTK
SEIKEELQVS NHSLCNSKVK CNGWDSSALT KEDIKAIWLR KQEGVIKRDR MLKYSRSQRE
RRSPHMLVES LYAKDMGMRS CRLEHWGESK SAKSINSFLI PSEMLVPTKV KLRSLQRQDS
GDGQDSPFSF PRRSFSRLEQ SILEDESWFQ RSNGFQPYMS VTESAREKMR SLSTPRQRVG
IMDSLFDNYK KDGDKVSLWS TFVCENSKIN NAKKSSLTTY QHNC
