CML20_ARATH
ID CML20_ARATH Reviewed; 169 AA.
AC O82659;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable calcium-binding protein CML20 {ECO:0000303|Ref.6};
DE AltName: Full=Calmodulin-like protein 20 {ECO:0000303|Ref.6};
DE AltName: Full=Centrin 1 {ECO:0000303|PubMed:18757558};
DE Short=AtCEN1 {ECO:0000303|PubMed:18757558};
GN Name=CML20 {ECO:0000303|Ref.6};
GN Synonyms=CEN1 {ECO:0000303|PubMed:18757558};
GN OrderedLocusNames=At3g50360 {ECO:0000312|Araport:AT3G50360};
GN ORFNames=F11C1.200 {ECO:0000312|EMBL:CAB62315.1};
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 [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9742960; DOI=10.1016/s0014-5793(98)01015-1;
RA Cordeiro M.C.R., Piqueras R., de Oliveira D.E., Castresana C.;
RT "Characterization of early induced genes in Arabidopsis thaliana responding
RT to bacterial inoculation: identification of centrin and of a novel protein
RT with two regions related to kinase domains.";
RL FEBS Lett. 434:387-393(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX DOI=10.1046/j.1469-8137.2003.00845.x;
RA McCormack E., Braam J.;
RT "Calmodulins and related potential calcium sensors of Arabidopsis.";
RL New Phytol. 159:585-598(2003).
RN [7]
RP INTERACTION WITH TON1A AND TON1B.
RC STRAIN=cv. Columbia;
RX PubMed=18757558; DOI=10.1105/tpc.107.056812;
RA Azimzadeh J., Nacry P., Christodoulidou A., Drevensek S., Camilleri C.,
RA Amiour N., Parcy F., Pastuglia M., Bouchez D.;
RT "Arabidopsis TONNEAU1 proteins are essential for preprophase band formation
RT and interact with centrin.";
RL Plant Cell 20:2146-2159(2008).
RN [8]
RP INTERACTION WITH SAC3A AND SAC3B.
RX PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT and anchoring nucleoporin.";
RL Plant J. 61:259-270(2010).
RN [9]
RP INTERACTION WITH UCH1 AND UCH2.
RX PubMed=22951400; DOI=10.4161/psb.21899;
RA Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT associate with the 26S proteasome and the TREX-2 complex.";
RL Plant Signal. Behav. 7:1415-1419(2012).
CC -!- FUNCTION: Potential calcium sensor. {ECO:0000250|UniProtKB:O23184}.
CC -!- SUBUNIT: Interacts with TON1A and TON1B (PubMed:18757558). Interacts
CC with SAC3A and SAC3B (PubMed:19843313). Interacts with UCH1 and UCH2
CC (PubMed:22951400). {ECO:0000269|PubMed:18757558,
CC ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:22951400}.
CC -!- INDUCTION: By wounding and infection by the bacterial pathogens
CC X.campestris and P.syringae. {ECO:0000269|PubMed:9742960}.
CC -!- CAUTION: Although assigned as a calmodulin family member by Ref.6, it
CC only contains EF-hand domains. {ECO:0000305}.
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DR EMBL; AJ009672; CAA08773.1; -; mRNA.
DR EMBL; AL132976; CAB62315.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78658.1; -; Genomic_DNA.
DR EMBL; AK175359; BAD43122.1; -; mRNA.
DR EMBL; AK175375; BAD43138.1; -; mRNA.
DR EMBL; AK176828; BAD44591.1; -; mRNA.
DR EMBL; BT025522; ABF58940.1; -; mRNA.
DR EMBL; AK176882; BAD44645.1; -; mRNA.
DR PIR; T45582; T45582.
DR RefSeq; NP_190605.1; NM_114896.5.
DR AlphaFoldDB; O82659; -.
DR SMR; O82659; -.
DR BioGRID; 9516; 4.
DR IntAct; O82659; 2.
DR STRING; 3702.AT3G50360.1; -.
DR PaxDb; O82659; -.
DR PRIDE; O82659; -.
DR ProteomicsDB; 240996; -.
DR EnsemblPlants; AT3G50360.1; AT3G50360.1; AT3G50360.
DR GeneID; 824198; -.
DR Gramene; AT3G50360.1; AT3G50360.1; AT3G50360.
DR KEGG; ath:AT3G50360; -.
DR Araport; AT3G50360; -.
DR TAIR; locus:2074780; AT3G50360.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; O82659; -.
DR OMA; YDEFEYM; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; O82659; -.
DR PRO; PR:O82659; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82659; baseline and differential.
DR Genevisible; O82659; AT.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..169
FT /note="Probable calcium-binding protein CML20"
FT /id="PRO_0000342949"
FT DOMAIN 23..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 59..94
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 132..167
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 169 AA; 19409 MW; 51D7BBDE05CD2C77 CRC64;
MSSIYRTVSR KEKPRRHHGL TTQKKQEIKE AFELFDTDGS GTIDAKELNV AMRALGFEMT
EEQINKMIAD VDKDGSGAID FDEFVHMMTA KIGERDTKEE LTKAFQIIDL DKNGKISPDD
IKRMAKDLGE NFTDAEIREM VEEADRDRDG EVNMDEFMRM MRRTAYGGN
