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Entry version 19 (08 May 2019)
Sequence version 1 (10 May 2017)
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Protein

Calmodulin-3

Gene

Calm3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi21 – 321Add BLAST12
Calcium bindingi57 – 682Add BLAST12
Calcium bindingi94 – 1053Add BLAST12
Calcium bindingi130 – 1414Add BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-111932 CaMK IV-mediated phosphorylation of CREB
R-RNO-111933 Calmodulin induced events
R-RNO-111957 Cam-PDE 1 activation
R-RNO-114608 Platelet degranulation
R-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-RNO-163615 PKA activation
R-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol
R-RNO-2025928 Calcineurin activates NFAT
R-RNO-203615 eNOS activation
R-RNO-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-RNO-2672351 Stimuli-sensing channels
R-RNO-2871809 FCERI mediated Ca+2 mobilization
R-RNO-4086398 Ca2+ pathway
R-RNO-418359 Reduction of cytosolic Ca++ levels
R-RNO-425561 Sodium/Calcium exchangers
R-RNO-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-RNO-442729 CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
R-RNO-445355 Smooth Muscle Contraction
R-RNO-451308 Activation of Ca-permeable Kainate Receptor
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5576892 Phase 0 - rapid depolarisation
R-RNO-5578775 Ion homeostasis
R-RNO-5607763 CLEC7A (Dectin-1) induces NFAT activation
R-RNO-5626467 RHO GTPases activate IQGAPs
R-RNO-5627123 RHO GTPases activate PAKs
R-RNO-5673000 RAF activation
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-70221 Glycogen breakdown (glycogenolysis)
R-RNO-9009391 Non-genomic estrogen signaling
R-RNO-936837 Ion transport by P-type ATPases
R-RNO-9619229 Activation of RAC1 downstream of NMDARs
R-RNO-9620244 Long-term potentiation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Calmodulin-3By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Calm3Imported
Synonyms:Cam3, Camc, CaMIII1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 1, Chromosome 6

Organism-specific databases

Rat genome database

More...
RGDi
2259 Calm3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004399402 – 149Calmodulin-3Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine2 Publications1
Modified residuei22N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0DP31

PRoteomics IDEntifications database

More...
PRIDEi
P0DP31

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0DP31

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P0DP31 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0DP31

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni77 – 149Necessary and sufficient for interaction with PCP4By similarityAdd BLAST73

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the calmodulin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182980

KEGG Orthology (KO)

More...
KOi
K02183

Database of Orthologous Groups

More...
OrthoDBi
1386217at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00051 EFh, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039030 Calmodulin
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom

The PANTHER Classification System

More...
PANTHERi
PTHR23050:SF379 PTHR23050:SF379, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13499 EF-hand_7, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00054 EFh, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 4 hits
PS50222 EF_HAND_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6B4BC3FCDE10727B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M16659 mRNA Translation: AAA40864.1
X13817 mRNA Translation: CAA32050.1
X14265 Genomic DNA Translation: CAA32478.1
BC063187 mRNA Translation: AAH63187.1

NCBI Reference Sequences

More...
RefSeqi
NP_036650.1, NM_012518.3
NP_059022.1, NM_017326.3
NP_114175.1, NM_031969.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770
ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24242
24244
50663

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24242
rno:24244
rno:50663

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

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...

PTM databases

iPTMnetiP0DP31

Proteomic databases

jPOSTiP0DP31
PRIDEiP0DP31

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
801
805
808
RGDi2259 Calm3

Phylogenomic databases

GeneTreeiENSGT00950000182980
KOiK02183
OrthoDBi1386217at2759

Enzyme and pathway databases

ReactomeiR-RNO-111932 CaMK IV-mediated phosphorylation of CREB
R-RNO-111933 Calmodulin induced events
R-RNO-111957 Cam-PDE 1 activation
R-RNO-114608 Platelet degranulation
R-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-RNO-163615 PKA activation
R-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol
R-RNO-2025928 Calcineurin activates NFAT
R-RNO-203615 eNOS activation
R-RNO-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-RNO-2672351 Stimuli-sensing channels
R-RNO-2871809 FCERI mediated Ca+2 mobilization
R-RNO-4086398 Ca2+ pathway
R-RNO-418359 Reduction of cytosolic Ca++ levels
R-RNO-425561 Sodium/Calcium exchangers
R-RNO-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-RNO-442729 CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
R-RNO-445355 Smooth Muscle Contraction
R-RNO-451308 Activation of Ca-permeable Kainate Receptor
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5576892 Phase 0 - rapid depolarisation
R-RNO-5578775 Ion homeostasis
R-RNO-5607763 CLEC7A (Dectin-1) induces NFAT activation
R-RNO-5626467 RHO GTPases activate IQGAPs
R-RNO-5627123 RHO GTPases activate PAKs
R-RNO-5673000 RAF activation
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-70221 Glycogen breakdown (glycogenolysis)
R-RNO-9009391 Non-genomic estrogen signaling
R-RNO-936837 Ion transport by P-type ATPases
R-RNO-9619229 Activation of RAC1 downstream of NMDARs
R-RNO-9620244 Long-term potentiation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0DP31

Gene expression databases

ExpressionAtlasiP0DP31 baseline and differential

Family and domain databases

CDDicd00051 EFh, 2 hits
InterProiView protein in InterPro
IPR039030 Calmodulin
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PANTHERiPTHR23050:SF379 PTHR23050:SF379, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCALM3_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DP31
Secondary accession number(s): P02593
, P62161, P70667, P99014, Q61379, Q61380
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: May 10, 2017
Last modified: May 8, 2019
This is version 19 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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