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IQM1_ARATH
ID   IQM1_ARATH              Reviewed;         488 AA.
AC   O82645; Q3E9R9; Q8W4H9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=IQ domain-containing protein IQM1 {ECO:0000305};
DE   AltName: Full=IQ motif-containing protein 1 {ECO:0000303|Ref.6};
GN   Name=IQM1 {ECO:0000303|Ref.6};
GN   Synonyms=EDA39 {ECO:0000312|EMBL:AEE86164.1};
GN   OrderedLocusNames=At4g33050 {ECO:0000312|Araport:AT4G33050};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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] (ISOFORM 2).
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   TISSUE SPECIFICITY.
RX   PubMed=17032064; DOI=10.1371/journal.pbio.0040327;
RA   Mori I.C., Murata Y., Yang Y., Munemasa S., Wang Y.-F., Andreoli S.,
RA   Tiriac H., Alonso J.M., Harper J.F., Ecker J.R., Kwak J.M., Schroeder J.I.;
RT   "CDPKs CPK6 and CPK3 function in ABA regulation of guard cell S-type
RT   anion- and Ca(2+)-permeable channels and stomatal closure.";
RL   PLoS Biol. 4:E327-E327(2006).
RN   [5]
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   [6]
RP   GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX   DOI=10.1007/s11738-009-0398-9;
RA   Zhou Y., Chen Y., Yamamoto K.T., Duan J., Tian C.;
RT   "Sequence and expression analysis of the Arabidopsis IQM family.";
RL   Acta Physiol. Plant. 32:191-198(2010).
RN   [7]
RP   FUNCTION, INTERACTION WITH CAM5, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=22572939; DOI=10.1007/s11103-012-9915-0;
RA   Zhou Y.P., Duan J., Fujibe T., Yamamoto K.T., Tian C.E.;
RT   "AtIQM1, a novel calmodulin-binding protein, is involved in stomatal
RT   movement in Arabidopsis.";
RL   Plant Mol. Biol. 79:333-346(2012).
CC   -!- FUNCTION: Involved in the modulation of stomatal movement. Promotes
CC       stomatal opening. May play a role in the regulation of chitin
CC       signaling. May be involved in biotic and abiotic stress responses.
CC       {ECO:0000269|PubMed:22572939}.
CC   -!- SUBUNIT: Interacts (via IQ domain) with CAM5.
CC       {ECO:0000269|PubMed:22572939}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22572939}. Nucleus
CC       {ECO:0000269|PubMed:22572939}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O82645-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O82645-2; Sequence=VSP_057855, VSP_057856;
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaf mesophyll cells
CC       (PubMed:17032064). Expressed in roots, rosette and cauline leaves,
CC       stems, flowers and siliques (Ref.6). {ECO:0000269|PubMed:17032064,
CC       ECO:0000269|Ref.6}.
CC   -!- INDUCTION: By light, cadmium and lead. Down-regulated by salt stress
CC       and treatment with mannitol. {ECO:0000269|Ref.6}.
CC   -!- DISRUPTION PHENOTYPE: Reduced primary root length. Reduced stomatal
CC       aperture. {ECO:0000269|PubMed:22572939}.
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DR   EMBL; AL031804; CAA21214.1; -; Genomic_DNA.
DR   EMBL; AL161582; CAB80022.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86164.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86165.1; -; Genomic_DNA.
DR   EMBL; AY062551; AAL32629.1; -; mRNA.
DR   EMBL; BT008453; AAP37812.1; -; mRNA.
DR   PIR; T05313; T05313.
DR   RefSeq; NP_195031.2; NM_119459.4. [O82645-2]
DR   RefSeq; NP_974673.2; NM_202944.3. [O82645-1]
DR   AlphaFoldDB; O82645; -.
DR   STRING; 3702.AT4G33050.2; -.
DR   iPTMnet; O82645; -.
DR   EnsemblPlants; AT4G33050.1; AT4G33050.1; AT4G33050. [O82645-2]
DR   EnsemblPlants; AT4G33050.3; AT4G33050.3; AT4G33050. [O82645-1]
DR   GeneID; 829442; -.
DR   Gramene; AT4G33050.1; AT4G33050.1; AT4G33050. [O82645-2]
DR   Gramene; AT4G33050.3; AT4G33050.3; AT4G33050. [O82645-1]
DR   KEGG; ath:AT4G33050; -.
DR   Araport; AT4G33050; -.
DR   eggNOG; ENOG502QRIN; Eukaryota.
DR   HOGENOM; CLU_026344_0_1_1; -.
DR   PhylomeDB; O82645; -.
DR   PRO; PR:O82645; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O82645; baseline and differential.
DR   Genevisible; O82645; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
DR   GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR   InterPro; IPR044159; IQM.
DR   PANTHER; PTHR31250; PTHR31250; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..488
FT                   /note="IQ domain-containing protein IQM1"
FT                   /id="PRO_0000433917"
FT   DOMAIN          106..135
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          20..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         197
FT                   /note="A -> AVSPHNLNIFVTSYQRQVPYLTSKAIIEYTLMIHLLKLQ (in
FT                   isoform 2)"
FT                   /id="VSP_057855"
FT   VAR_SEQ         334..488
FT                   /note="AIWPYSGHYLPTEDNFKEFISFLEEHNVDLTNVKRCSVNEEYSSFKSTADEE
FT                   EERKEVSEEVEIPSEKEERARPVFDPVKRLSCKWTSGYGPRIGCVRDYPMELQAQALEQ
FT                   VSLSPRVSPANSYGPIPSPRPSPKVRVSPRLAYMGIPSPRAVKC -> VLE (in
FT                   isoform 2)"
FT                   /id="VSP_057856"
SQ   SEQUENCE   488 AA;  55497 MW;  261DCF8206F236C4 CRC64;
     MGLEVGSLCF KLKDGGLTSR TNSFKRDDTN RHQNSPKSTM ERSLSFNSWE VPKETKTDSD
     FEVLETKKST PNTLNGRNCE RIQIKKPTVT PPEPFVFFSP RPVTELDAAA TTLQKVYKSY
     RTRRNLADCA VVVEELWWRT LEGAALDLSS VSFFGEEKHE TAVSKWARAR KRAAKVGKGL
     SKDEKAQKLA LQHWLEAIDP RHRYGHNLHF YYDVWSASKS TQPFFYWLDI GDGKDVNLEK
     HPRSVLQKQC IRYLGPMERE AYEVIVEDGR LMYKQGMTLI NSTEEAKSIF VLSTTRNLYV
     GIKKKGLFQH SSFLSGGATT AAGRLVARDG ILEAIWPYSG HYLPTEDNFK EFISFLEEHN
     VDLTNVKRCS VNEEYSSFKS TADEEEERKE VSEEVEIPSE KEERARPVFD PVKRLSCKWT
     SGYGPRIGCV RDYPMELQAQ ALEQVSLSPR VSPANSYGPI PSPRPSPKVR VSPRLAYMGI
     PSPRAVKC
 
 
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