IQD31_ARATH
ID IQD31_ARATH Reviewed; 587 AA.
AC Q8L4D8; Q9CA49; Q9SSF5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein IQ-DOMAIN 31 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD31 {ECO:0000303|PubMed:16368012};
GN Name=IQD31 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At1g74690 {ECO:0000312|Araport:AT1G74690};
GN ORFNames=F1M20.37 {ECO:0000312|EMBL:AAG52386.1},
GN F25A4.33 {ECO:0000312|EMBL:AAD55302.1};
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;
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.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP 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 [7]
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 [8]
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 [9]
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=AAD55302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008263; AAD55302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011765; AAG52386.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35622.1; -; Genomic_DNA.
DR EMBL; AY099679; AAM20530.1; -; mRNA.
DR EMBL; AY128860; AAM91260.1; -; mRNA.
DR PIR; B96776; B96776.
DR RefSeq; NP_177607.2; NM_106127.5.
DR AlphaFoldDB; Q8L4D8; -.
DR SMR; Q8L4D8; -.
DR BioGRID; 29027; 2.
DR IntAct; Q8L4D8; 2.
DR STRING; 3702.AT1G74690.1; -.
DR iPTMnet; Q8L4D8; -.
DR PaxDb; Q8L4D8; -.
DR PRIDE; Q8L4D8; -.
DR ProteomicsDB; 228834; -.
DR EnsemblPlants; AT1G74690.1; AT1G74690.1; AT1G74690.
DR GeneID; 843808; -.
DR Gramene; AT1G74690.1; AT1G74690.1; AT1G74690.
DR KEGG; ath:AT1G74690; -.
DR Araport; AT1G74690; -.
DR TAIR; locus:2019205; AT1G74690.
DR eggNOG; ENOG502QTUQ; Eukaryota.
DR HOGENOM; CLU_026881_0_0_1; -.
DR InParanoid; Q8L4D8; -.
DR OMA; NTIQVNW; -.
DR OrthoDB; 533192at2759; -.
DR PhylomeDB; Q8L4D8; -.
DR PRO; PR:Q8L4D8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L4D8; baseline and differential.
DR Genevisible; Q8L4D8; AT.
DR GO; GO:0005875; C:microtubule associated complex; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; 2.
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; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..587
FT /note="Protein IQ-DOMAIN 31"
FT /id="PRO_0000324124"
FT DOMAIN 112..140
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 141..163
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 164..188
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 57..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..159
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 344..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 176..183
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 355..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 587 AA; 65200 MW; 8CF17E73C810DBEB CRC64;
MGKSTKWLKN VLLGKKTSKS SGSKDKERVV SGKEVLVTSK VEESDVVSDL PSFEVAETNT
VDRSGGMLET QNVGPEEISD DEIELPEGKS TDSQNVAPVQ DHSLSDAERI QREIAATSVQ
AAFRGYLARR AFWALKGIIR LQALIRGHLV RRQAVATLFS VMGIVRLQAF ARGREIRKSD
IGVQVYRKCR LQLLQGNKLA NPTDAYLGIK KLTANAFAQK LLASSPKVLP VHAYDTSNPN
SNLIWLENWS ASCFWKPVPQ PKKTISRKPQ NRLLVEAESA KPKKSVRKVP ASNFESSSVQ
TSFEFEKPKR SFRKVSSQSI EPPAVEDPQI ELEKVKRSLR KVHNPVVESS IQPQRSPRKE
VEKPKLGVEK TRESSYPLVH ETAEEPVNVC DEKKKQEISE QPEEEVHALE MEVHTPGPLE
TNEALDSSLV NQIDSNEKAM VEEKPSMEKD TKEEKTPKPN NKENSAGKEN QKSRKKGSAT
SKTEREESNG HHETSPSIPS YMQATKSAKA KLRLQGSPKS AEQDGTEKAT VPRRHSLPSP
GNGRITSHSP RTTRLANSGD KTGNKKEKPL LSSREGNAKT TPAERKR
