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Protein

Calmodulin-3

Gene

Calm3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.By similarity

Miscellaneous

This protein has four functional calcium-binding sites.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi21 – 321Add BLAST12
Calcium bindingi57 – 682Add BLAST12
Calcium bindingi94 – 1053Add BLAST12
Calcium bindingi130 – 1414Add BLAST12

GO - Molecular functioni

  • adenylate cyclase binding Source: RGD
  • calcium channel inhibitor activity Source: RGD
  • calcium ion binding Source: RGD
  • enzyme regulator activity Source: RGD
  • ion channel binding Source: RGD
  • nitric-oxide synthase binding Source: RGD
  • nitric-oxide synthase regulator activity Source: RGD
  • protein kinase binding Source: RGD
  • protein N-terminus binding Source: RGD
  • protein phosphatase activator activity Source: RGD
  • titin binding Source: RGD

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin-3By similarity
Gene namesi
Name:Calm3Imported
Synonyms:Cam3, Camc, CaMIII1 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componentsi: Chromosome 1, Chromosome 6

Organism-specific databases

RGDi2259. Calm3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00004399402 – 149Calmodulin-3Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine2 Publications1
Modified residuei22N6-acetyllysine; alternateBy similarity1
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45Phosphothreonine; by CaMK41 Publication1
Modified residuei82PhosphoserineBy similarity1
Modified residuei95N6-acetyllysineBy similarity1
Modified residuei100PhosphotyrosineCombined sources1
Modified residuei102PhosphoserineCombined sources1
Modified residuei111PhosphothreonineBy similarity1
Modified residuei116N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei116N6-methyllysine; alternateBy similarity1
Modified residuei139PhosphotyrosineBy similarity1

Post-translational modificationi

Ubiquitination results in a strongly decreased activity.By similarity
Phosphorylation results in a decreased activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP0DP31.

Interactioni

Subunit structurei

Interacts with CEP97, CCP110, TTN/titin and SRY (By similarity). Interacts with MYO5A and RRAD (PubMed:18056528). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2 (By similarity). Interacts with SCN5A (By similarity). Interacts with RYR1 (By similarity). Interacts with FCHO1 (By similarity). Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure (By similarity). Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with SYT7 (By similarity). Interacts with MYO10 and MYO1C (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (PubMed:8576129). Interacts with RYR2; regulates RYR2 calcium-release channel activity (By similarity). Interacts with PCP4; regulates calmodulin calcium-binding (By similarity). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (By similarity).By similarity2 Publications

GO - Molecular functioni

  • adenylate cyclase binding Source: RGD
  • ion channel binding Source: RGD
  • nitric-oxide synthase binding Source: RGD
  • protein kinase binding Source: RGD
  • protein N-terminus binding Source: RGD
  • titin binding Source: RGD

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Helixi30 – 39Combined sources10
Helixi46 – 56Combined sources11
Helixi66 – 73Combined sources8
Helixi79 – 93Combined sources15
Beta strandi98 – 101Combined sources4
Helixi103 – 113Combined sources11
Helixi119 – 129Combined sources11
Beta strandi134 – 138Combined sources5
Helixi139 – 145Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UP5X-ray1.90A/B2-149[»]
3EK4X-ray2.65A45-149[»]
3EK7X-ray1.85A45-149[»]
3EK8X-ray2.80A45-149[»]
3EKHX-ray2.00A45-149[»]
3EKJX-ray2.80A45-149[»]
3EVUX-ray1.75A46-149[»]
3EVVX-ray2.60A46-149[»]
3SG2X-ray2.00A46-149[»]
3SG3X-ray2.10A46-149[»]
3SG4X-ray2.40A46-149[»]
3SG5X-ray1.90A46-149[»]
3SG6X-ray1.70A46-149[»]
3SG7X-ray1.90A46-149[»]
3WLCX-ray2.49A46-149[»]
3WLDX-ray2.70A46-149[»]
4I2YX-ray2.20A/B20-149[»]
SMRiP0DP31.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 43EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini44 – 79EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini81 – 116EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini117 – 149EF-hand 4PROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 149Necessary and sufficient for interaction with PCP4By similarityAdd BLAST73

Sequence similaritiesi

Belongs to the calmodulin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00760000118901.
KOiK02183.

Family and domain databases

CDDicd00051. EFh. 2 hits.
InterProiView protein in InterPro
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
PfamiView protein in Pfam
PF13499. EF-hand_7. 2 hits.
SMARTiView protein in SMART
SM00054. EFh. 4 hits.
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiView protein in PROSITE
PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0DP31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY
110 120 130 140
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK
Length:149
Mass (Da):16,838
Last modified:May 10, 2017 - v1
Checksum:i6B4BC3FCDE10727B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16659 mRNA. Translation: AAA40864.1.
X13817 mRNA. Translation: CAA32050.1.
X14265 Genomic DNA. Translation: CAA32478.1.
BC063187 mRNA. Translation: AAH63187.1.
RefSeqiNP_036650.1. NM_012518.3.
NP_059022.1. NM_017326.3.
NP_114175.1. NM_031969.2.
UniGeneiRn.129719.
Rn.216430.
Rn.2892.
Rn.4166.
Rn.5968.

Genome annotation databases

EnsembliENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770.
ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.
GeneIDi24242.
24244.
50663.
KEGGirno:24242.
rno:24244.
rno:50663.

Similar proteinsi

Entry informationi

Entry nameiCALM3_RAT
AccessioniPrimary (citable) accession number: P0DP31
Secondary accession number(s): P02593
, P62161, P70667, P99014, Q61379, Q61380
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: May 10, 2017
Last modified: November 22, 2017
This is version 7 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families