CML19_ARATH
ID CML19_ARATH Reviewed; 167 AA.
AC O23184; Q8LCE6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Calcium-binding protein CML19 {ECO:0000303|Ref.7};
DE AltName: Full=Calmodulin-like protein 19 {ECO:0000303|Ref.7};
DE AltName: Full=Centrin 2 {ECO:0000303|PubMed:15155891};
DE Short=AtCEN2 {ECO:0000303|PubMed:15155891};
GN Name=CML19 {ECO:0000303|Ref.7};
GN Synonyms=CEN2 {ECO:0000303|PubMed:15155891};
GN OrderedLocusNames=At4g37010 {ECO:0000312|Araport:AT4G37010};
GN ORFNames=AP22.11, C7A10.350 {ECO:0000312|EMBL:CAB16762.1};
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 FUNCTION.
RX PubMed=14688294; DOI=10.1105/tpc.016600;
RA Reddy V.S., Day I.S., Thomas T., Reddy A.S.N.;
RT "KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a
RT microtubule motor protein and regulates trichome morphogenesis.";
RL Plant Cell 16:185-200(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP FUNCTION, INDUCTION BY UV-C, AND TISSUE SPECIFICITY.
RX PubMed=15155891; DOI=10.1105/tpc.021378;
RA Molinier J., Ramos C., Fritsch O., Hohn B.;
RT "CENTRIN2 modulates homologous recombination and nucleotide excision repair
RT in Arabidopsis.";
RL Plant Cell 16:1633-1643(2004).
RN [9]
RP FUNCTION, INTERACTION WITH RAD4, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=16786311; DOI=10.1007/s11103-006-0016-9;
RA Liang L., Flury S., Kalck V., Hohn B., Molinier J.;
RT "CENTRIN2 interacts with the Arabidopsis homolog of the human XPC protein
RT (AtRAD4) and contributes to efficient synthesis-dependent repair of bulky
RT DNA lesions.";
RL Plant Mol. Biol. 61:345-356(2006).
RN [10]
RP INTERACTION WITH 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).
CC -!- FUNCTION: Potential calcium sensor that binds calcium in vitro
CC (PubMed:14688294). Modulates homologous recombination and nucleotide
CC excision repair (NER) (PubMed:15155891). Involved in the early response
CC to UV irradiation (PubMed:16786311). {ECO:0000269|PubMed:14688294,
CC ECO:0000269|PubMed:15155891, ECO:0000269|PubMed:16786311}.
CC -!- SUBUNIT: Interacts with RAD4 (PubMed:16786311). Calcium is required for
CC this interaction (PubMed:16786311). Interacts with SAC3B
CC (PubMed:19843313). {ECO:0000269|PubMed:16786311,
CC ECO:0000269|PubMed:19843313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16786311}. Nucleus
CC {ECO:0000269|PubMed:16786311}. Note=Localizes to the nucleus after
CC exposure to UV-C and cicplatin. {ECO:0000269|PubMed:16786311}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23184-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, and at lower level in
CC stems. Barely detectable in flower buds and flowers.
CC {ECO:0000269|PubMed:15155891}.
CC -!- INDUCTION: Up-regulated by UV-C induced DNA damage, but not by DNA
CC double-strand breaks caused by bleomycin.
CC {ECO:0000269|PubMed:15155891}.
CC -!- DOMAIN: The C-terminal EF-hand is necessary for the binding to RAD4 and
CC for efficient nucleotide excision repair (NER).
CC {ECO:0000269|PubMed:16786311}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
CC -!- CAUTION: Although assigned as a calmodulin family member by Ref.7, it
CC only contains EF-hand domains. {ECO:0000305}.
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DR EMBL; AY363869; AAR16087.1; -; mRNA.
DR EMBL; Z99707; CAB16762.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80367.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86734.1; -; Genomic_DNA.
DR EMBL; BT024826; ABD60709.1; -; mRNA.
DR EMBL; AY086644; AAM63702.1; -; mRNA.
DR PIR; B85437; B85437.
DR RefSeq; NP_195418.1; NM_119864.5. [O23184-1]
DR AlphaFoldDB; O23184; -.
DR SMR; O23184; -.
DR BioGRID; 15136; 5.
DR IntAct; O23184; 2.
DR STRING; 3702.AT4G37010.2; -.
DR iPTMnet; O23184; -.
DR PaxDb; O23184; -.
DR PRIDE; O23184; -.
DR EnsemblPlants; AT4G37010.1; AT4G37010.1; AT4G37010. [O23184-1]
DR GeneID; 829855; -.
DR Gramene; AT4G37010.1; AT4G37010.1; AT4G37010. [O23184-1]
DR KEGG; ath:AT4G37010; -.
DR Araport; AT4G37010; -.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; O23184; -.
DR OMA; TIDIAMW; -.
DR PhylomeDB; O23184; -.
DR PRO; PR:O23184; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23184; baseline and differential.
DR Genevisible; O23184; AT.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
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 Alternative splicing; Calcium; Cytoplasm; DNA damage; DNA repair;
KW Metal-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..167
FT /note="Calcium-binding protein CML19"
FT /id="PRO_0000342948"
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 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"
FT CONFLICT 113
FT /note="N -> S (in Ref. 6; AAM63702)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="Y -> F (in Ref. 6; AAM63702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19156 MW; 8BF97BB1AD7B9E6C CRC64;
MSEAAQLRRG LKPKGKTYGL TNQKRREIRE IFDLFDIDGS GSIDASELNV AMRSLGFEMN
NQQINELMAE VDKNQSGAID FDEFVHMMTT KFGERDSIDE LSKAFKIIDH DNNGKISPRD
IKMIAKELGE NFTDNDIEEM IEEADRDKDG EVNLEEFMKM MKRTSYG
