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IQD16_ARATH
ID   IQD16_ARATH             Reviewed;         423 AA.
AC   Q7XA83; Q9T0C1; Q9ZSC0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Protein IQ-DOMAIN 16 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD16 {ECO:0000303|PubMed:16368012};
GN   Name=IQD16 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At4g10640 {ECO:0000312|Araport:AT4G10640};
GN   ORFNames=F3H7.10 {ECO:0000312|EMBL:AAD03435.1},
GN   T4F9.100 {ECO:0000312|EMBL:CAB40030.1};
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=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].
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   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 (JUL-2006) 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   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   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 (PubMed:28115582). Regulates cell shape and
CC       elongation in aerial organs (i.e. cotyledons, leaves, and hypocotyls)
CC       probably by regulating cortical microtubules (MT) arrays orientation
CC       (PubMed:28115582). May associate with nucleic acids and regulate gene
CC       expression at the transcriptional or post-transcriptional level (By
CC       similarity). {ECO:0000250|UniProtKB:Q9SF32,
CC       ECO:0000269|PubMed:28115582}.
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: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:28115582}. Cell membrane
CC       {ECO:0000269|PubMed:28115582}. Note=Recruits calmodulin (CaM2) to
CC       microtubules. {ECO:0000269|PubMed:28115582}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:28115582}.
CC   -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD03435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB40030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF118222; AAD03435.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL049523; CAB40030.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161518; CAB81165.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82912.1; -; Genomic_DNA.
DR   EMBL; BT010145; AAQ22614.1; -; mRNA.
DR   EMBL; AK228338; BAF00278.1; -; mRNA.
DR   PIR; T04199; T04199.
DR   RefSeq; NP_192802.2; NM_117132.4.
DR   AlphaFoldDB; Q7XA83; -.
DR   SMR; Q7XA83; -.
DR   STRING; 3702.AT4G10640.1; -.
DR   PaxDb; Q7XA83; -.
DR   PRIDE; Q7XA83; -.
DR   ProteomicsDB; 191576; -.
DR   EnsemblPlants; AT4G10640.1; AT4G10640.1; AT4G10640.
DR   GeneID; 826656; -.
DR   Gramene; AT4G10640.1; AT4G10640.1; AT4G10640.
DR   KEGG; ath:AT4G10640; -.
DR   Araport; AT4G10640; -.
DR   TAIR; locus:2139187; AT4G10640.
DR   eggNOG; ENOG502R300; Eukaryota.
DR   HOGENOM; CLU_048049_0_0_1; -.
DR   InParanoid; Q7XA83; -.
DR   OMA; KSAYNGC; -.
DR   OrthoDB; 736229at2759; -.
DR   PhylomeDB; Q7XA83; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q7XA83; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IPI:TAIR.
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; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Membrane; Reference proteome; Repeat.
FT   CHAIN           1..423
FT                   /note="Protein IQ-DOMAIN 16"
FT                   /id="PRO_0000453122"
FT   DOMAIN          99..127
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          128..150
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          235..252
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   COILED          231..251
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  48718 MW;  84193D2717B75C05 CRC64;
     MAKKNGTSWF TAVKKILWSP SKDSDKKTHH HKETDIKRKE KKGWIFRKTK LETTNSVLQH
     TVRTVEAEEK EKPPVIVSSV EEGVTEIVKL TATPGFIRRH WAAIIIQTAF RGYLSRRALR
     ALKGIVKLQA LVRGNNVRNQ AKLTLRCIKA LVRVQDQVLN HHQQQRSRVL LSPPSRNYNI
     EARRNSMFAE SNGFWDTKTY LQDIRSRRSL SRDMNRCNNE FYSEETELIL QKKLEIAIKR
     EKAQALALSN QIRSRSSRNQ SAGDDRELLE RTQWLDRWMA TKQWDDTITN STNVRDPIKT
     LEAVTTHHHQ RSYPATPPSC RASRSVMVRS ASPRIPCSPS SMQPNYMSAT ESAKAKARTQ
     STPRRRPMTA KKRLCYAEEE SLRSPSFKSC LWGDHESDYS CCYGDGFAGK ISPCSTTELR
     WLK
 
 
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