CML37_ARATH
ID CML37_ARATH Reviewed; 185 AA.
AC Q9FIH9; Q8L8M5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Calcium-binding protein CML37 {ECO:0000303|Ref.5};
DE AltName: Full=Calmodulin-like protein 37 {ECO:0000303|Ref.5};
GN Name=CML37 {ECO:0000303|Ref.5};
GN OrderedLocusNames=At5g42380 {ECO:0000312|Araport:AT5G42380};
GN ORFNames=MDH9.7 {ECO:0000312|EMBL:BAB10479.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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].
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=15720654; DOI=10.1111/j.1469-8137.2004.01238.x;
RA Lee D., Polisensky D.H., Braam J.;
RT "Genome-wide identification of touch- and darkness-regulated Arabidopsis
RT genes: a focus on calmodulin-like and XTH genes.";
RL New Phytol. 165:429-444(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17579812; DOI=10.1007/s11103-007-9189-0;
RA Vanderbeld B., Snedden W.A.;
RT "Developmental and stimulus-induced expression patterns of Arabidopsis
RT calmodulin-like genes CML37, CML38 and CML39.";
RL Plant Mol. Biol. 64:683-697(2007).
RN [8]
RP INTERACTION WITH ABCG36.
RC STRAIN=cv. Columbia;
RX PubMed=26315018; DOI=10.1111/nph.13582;
RA Campe R., Langenbach C., Leissing F., Popescu G.V., Popescu S.C.,
RA Goellner K., Beckers G.J., Conrath U.;
RT "ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin that, like
RT PEN3, is required for Arabidopsis nonhost resistance.";
RL New Phytol. 209:294-306(2016).
CC -!- FUNCTION: Potential calcium sensor that binds calcium in vitro.
CC {ECO:0000269|PubMed:17579812}.
CC -!- SUBUNIT: Binds to ABCG36. {ECO:0000269|PubMed:26315018}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, stipule, young leaves and
CC at the hypocotyl-root junction. In mature root, expressed in the stele,
CC cortex, emerging lateral root, root tip and root cap. In mature plant,
CC expressed at the base of cauline and floral branches, and in rosette
CC and cauline leaves. Expressed from stage 9 to 14 of flower development
CC in anthers. At stage 15, expressed in carpel, sepals, petals and pollen
CC until dehiscence. Expressed in developing seeds and young siliques.
CC {ECO:0000269|PubMed:17579812}.
CC -!- INDUCTION: By touch, salt and hydrogen peroxide treatments, drought
CC stress, wounding, dark and infection by the bacterial pathogen
CC P.syringae. {ECO:0000269|PubMed:15720654, ECO:0000269|PubMed:17579812}.
CC -!- CAUTION: Although assigned as a calmodulin family member by Ref.5, it
CC only contains EF-hand domains. {ECO:0000305}.
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DR EMBL; AB016888; BAB10479.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94803.1; -; Genomic_DNA.
DR EMBL; AY093775; AAM10393.1; -; mRNA.
DR EMBL; AY143820; AAN28759.1; -; mRNA.
DR EMBL; AY088908; AAM67214.1; -; mRNA.
DR RefSeq; NP_199053.1; NM_123603.3.
DR AlphaFoldDB; Q9FIH9; -.
DR SMR; Q9FIH9; -.
DR BioGRID; 19494; 4.
DR STRING; 3702.AT5G42380.1; -.
DR PaxDb; Q9FIH9; -.
DR PRIDE; Q9FIH9; -.
DR ProteomicsDB; 240904; -.
DR EnsemblPlants; AT5G42380.1; AT5G42380.1; AT5G42380.
DR GeneID; 834244; -.
DR Gramene; AT5G42380.1; AT5G42380.1; AT5G42380.
DR KEGG; ath:AT5G42380; -.
DR Araport; AT5G42380; -.
DR TAIR; locus:2162326; AT5G42380.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_20_6_1; -.
DR InParanoid; Q9FIH9; -.
DR OMA; FYRVACH; -.
DR OrthoDB; 1340191at2759; -.
DR PhylomeDB; Q9FIH9; -.
DR PRO; PR:Q9FIH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIH9; baseline and differential.
DR Genevisible; Q9FIH9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
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; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..185
FT /note="Calcium-binding protein CML37"
FT /id="PRO_0000342961"
FT DOMAIN 45..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..154
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 155..185
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 33
FT /note="S -> A (in Ref. 4; AAM67214)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="N -> S (in Ref. 4; AAM67214)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="V -> L (in Ref. 4; AAM67214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20602 MW; 6F166F632BF26100 CRC64;
MTLAKNQKSS LSRLYKKVSS KRSESSRNLE DESRTSSNSS GSSSLNVNEL RTVFDYMDAN
SDGKISGEEL QSCVSLLGGA LSSREVEEVV KTSDVDGDGF IDFEEFLKLM EGEDGSDEER
RKELKEAFGM YVMEGEEFIT AASLRRTLSR LGESCTVDAC KVMIRGFDQN DDGVLSFDEF
VLMMR
