CML38_ARATH
ID CML38_ARATH Reviewed; 177 AA.
AC Q9SRE6; A8MQS8; Q8LBV6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Calcium-binding protein CML38 {ECO:0000303|Ref.5};
DE AltName: Full=Calmodulin-like protein 38 {ECO:0000303|Ref.5};
GN Name=CML38 {ECO:0000303|Ref.5};
GN OrderedLocusNames=At1g76650 {ECO:0000312|Araport:AT1G76650};
GN ORFNames=F28O16.2 {ECO:0000312|EMBL:AAF04447.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 1).
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] (ISOFORM 1).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SRE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SRE6-2; Sequence=VSP_034554;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and guard cells of young
CC leaves. In mature root, expressed in the epidermis, trichoblasts, young
CC lateral root and root tip. Expressed from stage 9 to 15 of flower
CC development in anther wall. {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; AC010718; AAF04447.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35869.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35870.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35871.1; -; Genomic_DNA.
DR EMBL; BT002421; AAO00781.1; -; mRNA.
DR EMBL; BT006556; AAP21364.1; -; mRNA.
DR EMBL; AY086972; AAM64535.1; -; mRNA.
DR PIR; G96794; G96794.
DR RefSeq; NP_001077834.1; NM_001084365.1. [Q9SRE6-2]
DR RefSeq; NP_001185413.1; NM_001198484.1. [Q9SRE6-1]
DR RefSeq; NP_177791.1; NM_106315.3. [Q9SRE6-1]
DR AlphaFoldDB; Q9SRE6; -.
DR SMR; Q9SRE6; -.
DR BioGRID; 29217; 2.
DR STRING; 3702.AT1G76650.1; -.
DR iPTMnet; Q9SRE6; -.
DR PaxDb; Q9SRE6; -.
DR PRIDE; Q9SRE6; -.
DR ProteomicsDB; 241050; -. [Q9SRE6-1]
DR EnsemblPlants; AT1G76650.1; AT1G76650.1; AT1G76650. [Q9SRE6-1]
DR EnsemblPlants; AT1G76650.2; AT1G76650.2; AT1G76650. [Q9SRE6-2]
DR EnsemblPlants; AT1G76650.3; AT1G76650.3; AT1G76650. [Q9SRE6-1]
DR GeneID; 843998; -.
DR Gramene; AT1G76650.1; AT1G76650.1; AT1G76650. [Q9SRE6-1]
DR Gramene; AT1G76650.2; AT1G76650.2; AT1G76650. [Q9SRE6-2]
DR Gramene; AT1G76650.3; AT1G76650.3; AT1G76650. [Q9SRE6-1]
DR KEGG; ath:AT1G76650; -.
DR Araport; AT1G76650; -.
DR TAIR; locus:2030141; AT1G76650.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; Q9SRE6; -.
DR OMA; EATMTTM; -.
DR PhylomeDB; Q9SRE6; -.
DR PRO; PR:Q9SRE6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRE6; baseline and differential.
DR Genevisible; Q9SRE6; AT.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009611; P:response to wounding; 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; 4.
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 Alternative splicing; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..177
FT /note="Calcium-binding protein CML38"
FT /id="PRO_0000342962"
FT DOMAIN 39..74
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 75..110
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 111..146
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..177
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 76..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034554"
FT CONFLICT 23
FT /note="E -> K (in Ref. 4; AAM64535)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> T (in Ref. 4; AAM64535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 20113 MW; 9B53AD3C8194ED23 CRC64;
MKNNTQPQSS FKKLCRKLSP KREDSAGEIQ QHNSSNGEDK NRELEAVFSY MDANRDGRIS
PEELQKSFMT LGEQLSDEEA VAAVRLSDTD GDGMLDFEEF SQLIKVDDEE EKKMELKGAF
RLYIAEGEDC ITPRSLKMML KKLGESRTTD DCRVMISAFD LNADGVLSFD EFALMMR
