CALM5_SOLTU
ID CALM5_SOLTU Reviewed; 149 AA.
AC Q7DMN9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Calmodulin-5/6/7/8;
DE Short=CaM-5/6/7/8;
GN Name=PCM5;
GN and
GN Name=PCM6;
GN and
GN Name=PCM7;
GN and
GN Name=PCM8;
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 / MRNA], INDUCTION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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: High expression of PCM5 and 8 in stolon tips and
CC stems, moderate in roots, and low in leaves. Steady-state expression of
CC PCM6 in all the tissues tested, except in the leaves where the
CC expression is lower. {ECO:0000269|PubMed:7727747}.
CC -!- DEVELOPMENTAL STAGE: Expression of PCM5 and 8 reduced during tuber
CC development. {ECO:0000269|PubMed:7727747}.
CC -!- INDUCTION: PCM5, PCM6 and PCM8 are not induced by touching.
CC {ECO:0000269|PubMed:7727747}.
CC -!- MISCELLANEOUS: The expression of PCM7 was not investigated.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; U20294; AAA85155.1; -; Genomic_DNA.
DR EMBL; U20295; AAA62351.1; -; mRNA.
DR EMBL; U20296; AAA85156.1; -; Genomic_DNA.
DR EMBL; U20297; AAA85157.1; -; Genomic_DNA.
DR RefSeq; NP_001275359.1; NM_001288430.1.
DR PDB; 1RFJ; X-ray; 2.00 A; A=1-149.
DR PDBsum; 1RFJ; -.
DR AlphaFoldDB; Q7DMN9; -.
DR SMR; Q7DMN9; -.
DR DIP; DIP-59736N; -.
DR IntAct; Q7DMN9; 1.
DR STRING; 4113.PGSC0003DMT400058435; -.
DR EnsemblPlants; PGSC0003DMT400058435; PGSC0003DMT400058435; PGSC0003DMG400022693.
DR EnsemblPlants; RHC01H1G0653.2.1; RHC01H1G0653.2.1; RHC01H1G0653.2.
DR GeneID; 102577873; -.
DR Gramene; PGSC0003DMT400058435; PGSC0003DMT400058435; PGSC0003DMG400022693.
DR Gramene; RHC01H1G0653.2.1; RHC01H1G0653.2.1; RHC01H1G0653.2.
DR KEGG; sot:102577873; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; Q7DMN9; -.
DR OMA; IARCITT; -.
DR OrthoDB; 1386217at2759; -.
DR EvolutionaryTrace; Q7DMN9; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q7DMN9; 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; 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 3D-structure; Acetylation; Calcium; Metal-binding; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..149
FT /note="Calmodulin-5/6/7/8"
FT /id="PRO_0000198305"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1RFJ"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1RFJ"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:1RFJ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1RFJ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1RFJ"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1RFJ"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:1RFJ"
SQ SEQUENCE 149 AA; 16848 MW; ABF12D8A91762013 CRC64;
MADQLTEDQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE
EVDEMIREAD VDGDGQINYD EFVKVMMAK
