CALM2_SOLTU
ID CALM2_SOLTU Reviewed; 124 AA.
AC Q7DMP0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Calmodulin-2/4;
DE Short=CaM-2/4;
DE Flags: Fragment;
GN Name=PCM2;
GN and
GN Name=PCM4;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Russet Burbank-0;
RX PubMed=7727747; DOI=10.1007/bf00020223;
RA Takezawa D., Liu Z.H., An G., Poovaiah B.W.;
RT "Calmodulin gene family in potato: developmental and touch-induced
RT expression of the mRNA encoding a novel isoform.";
RL Plant Mol. Biol. 27:693-703(1995).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases.
CC -!- TISSUE SPECIFICITY: Expression of PCM4 very low in stolon tips, stems,
CC roots, leaves and tubers. PCM2 not detected in the organs tested.
CC {ECO:0000269|PubMed:7727747}.
CC -!- MISCELLANEOUS: This protein may have four calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
CC -!- CAUTION: The possibility that PCM2 is a pseudogene cannot be ruled out.
CC {ECO:0000305}.
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DR EMBL; U20291; AAA85152.1; -; Genomic_DNA.
DR EMBL; U20293; AAA85154.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7DMP0; -.
DR SMR; Q7DMP0; -.
DR EnsemblPlants; RHC01H1G0653.2.1; RHC01H1G0653.2.1; RHC01H1G0653.2.
DR Gramene; RHC01H1G0653.2.1; RHC01H1G0653.2.1; RHC01H1G0653.2.
DR InParanoid; Q7DMP0; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q7DMP0; baseline and differential.
DR GO; GO:0005509; F:calcium ion binding; 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; 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 2: Evidence at transcript level;
KW Calcium; Metal-binding; Methylation; Reference proteome; Repeat.
FT CHAIN <1..124
FT /note="Calmodulin-2/4"
FT /id="PRO_0000198303"
FT DOMAIN <1..18
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 19..54
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 56..91
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..124
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 91
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 124 AA; 13986 MW; 666BD8493784A79E CRC64;
GCITTKELGT VMRSLGQNPT EAELQDMINE VDADGNGTID FPEFLNLMAR KMKDTDSEEE
LKEAFRVFDK DQNGFISAAE LRHVMTNLGE KLTDEEVDEM IREADVDGDG QINYDEFVKV
MMAK
