IQD28_ARATH
ID IQD28_ARATH Reviewed; 664 AA.
AC Q8GZ87; Q8LAE0; Q9M9S5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein IQ-DOMAIN 28 {ECO:0000303|PubMed:16368012};
DE Short=AtIQD28 {ECO:0000303|PubMed:16368012};
GN Name=IQD28 {ECO:0000303|PubMed:16368012};
GN OrderedLocusNames=At1g14380 {ECO:0000312|Araport:AT1G14380};
GN ORFNames=F14L17.15 {ECO:0000312|EMBL:AAF43938.1};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}.
CC Note=Associates to cortical microtubules (MTs).
CC {ECO:0000269|PubMed:24134884}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012188; AAF43938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29154.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29156.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61047.1; -; Genomic_DNA.
DR EMBL; AK117145; BAC41823.1; -; mRNA.
DR EMBL; BT005935; AAO64870.1; -; mRNA.
DR EMBL; AY087873; AAM65425.1; -; mRNA.
DR PIR; C86278; C86278.
DR RefSeq; NP_001031046.1; NM_001035969.2.
DR RefSeq; NP_001323290.1; NM_001332115.1.
DR RefSeq; NP_563950.1; NM_101305.4.
DR AlphaFoldDB; Q8GZ87; -.
DR STRING; 3702.AT1G14380.1; -.
DR PaxDb; Q8GZ87; -.
DR PRIDE; Q8GZ87; -.
DR ProteomicsDB; 189763; -.
DR EnsemblPlants; AT1G14380.1; AT1G14380.1; AT1G14380.
DR EnsemblPlants; AT1G14380.3; AT1G14380.3; AT1G14380.
DR EnsemblPlants; AT1G14380.4; AT1G14380.4; AT1G14380.
DR GeneID; 838000; -.
DR Gramene; AT1G14380.1; AT1G14380.1; AT1G14380.
DR Gramene; AT1G14380.3; AT1G14380.3; AT1G14380.
DR Gramene; AT1G14380.4; AT1G14380.4; AT1G14380.
DR KEGG; ath:AT1G14380; -.
DR Araport; AT1G14380; -.
DR TAIR; locus:2012507; AT1G14380.
DR eggNOG; ENOG502QTUQ; Eukaryota.
DR InParanoid; Q8GZ87; -.
DR OrthoDB; 533192at2759; -.
DR PhylomeDB; Q8GZ87; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GZ87; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005875; C:microtubule associated complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..664
FT /note="Protein IQ-DOMAIN 28"
FT /id="PRO_0000453133"
FT DOMAIN 93..121
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 122..140
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 144..170
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..116
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:16368012"
FT REGION 244..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 251..258
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 351..358
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 22..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 264
FT /note="K -> T (in Ref. 5; AAM65425)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> E (in Ref. 5; AAM65425)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> P (in Ref. 5; AAM65425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 72849 MW; 35B56828126A1A01 CRC64;
MGKTPGKWIK TLLLGKKSPK SNSDNRSQKL KSAKKEELVE SVTEDLSNLT VDPPVVSSQP
VPASTAQNVV SPINGDESKD NLESRNDLGE VELEQAAIKV QATFRAHQAR RAFRTLKGII
RLQAVIRGHL VRRQAIATYS CIWGIVKFQA LVRGQKARSS DIAIQFQKKH MEASDSEVLQ
SSTCSWMDNP TKFVFVDKLL ASSPTALPLK IQYGPEEPNS AKVWLERWTQ LQVWSSGSRV
PRIEIPKSQS KKRNYQAVVE AEKKRPKRSI KKPSGTTSGT GPSRFTAERN KPKRNVRKAS
TLSKDPLRNE SDKANHNSRK SRSGSKEGSP LEIKDEKPSP SLKRSSLSNG SKKATLRSAE
KKKKDIPDSS VQIQPEGKVS ENVLEGGDNI EFAEKEKDTT DSVQIESEGK VSGNVLEGGE
GENIVFTEKE KDTADPVQIE PERKVLEEGD NIESSGKEKD TGDSVQIESE GKVLEGGDNI
EFGEKEKDKA DAVPIEFDIV KDEKSPVLDR TEEDELKTAE TSDKAEALKC ADVKVSSENG
NVGSDNTKQS EKRALLPANI DKQDDGLTLS GRKIPSYMAP TASAKARVKG EASPRFAQAK
TEINGALRRH SLPSPANGKL STTTMSPRAQ KLLLASAKGS MNGDKSFTSS KDITHKSTRT
DWKR
