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Protein

Calmodulin

Gene

CAM

Organism
Paramecium tetraurelia
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 and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases.

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

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:CAM
ORF Names:GSPATT00015825001
OrganismiParamecium tetraurelia
Taxonomic identifieri5888 [NCBI]
Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium
Proteomesi
  • UP000000600 Componenti: Partially assembled WGS sequence

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36V → I in CAM13. 1 Publication1
Mutagenesisi41G → E in CAM12. 1 Publication1
Mutagenesisi51D → G in CAM15. 2 Publications1
Mutagenesisi51D → N in CAM12; lacks the Ca(2+)-dependent K(+) current. 2 Publications1
Mutagenesisi55E → K in CAM11. 1 Publication1
Mutagenesisi60G → S in CAM14. 1 Publication1
Mutagenesisi96D → G in CAM5. 1 Publication1
Mutagenesisi102S → F in CAM1 (also named PNTA1); lacks the Ca(2+)-dependent K(+) current. 1 Publication1
Mutagenesisi103A → V in CAM6. 1 Publication1
Mutagenesisi105E → K in CAM4. 1 Publication1
Mutagenesisi136H → R in CAM7. 1 Publication1
Mutagenesisi137I → T in CAM2 (also named PNTA2). 1 Publication1
Mutagenesisi146M → V in CAM3. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001982612 – 149CalmodulinAdd BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei14N6,N6-dimethyllysine1 Publication1
Modified residuei116N6,N6,N6-trimethyllysine1 Publication1

Post-translational modificationi

The pantophobiac mutant CAM2 is undermethylated on Lys-116.

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PRIDEiP07463.

Interactioni

Protein-protein interaction databases

DIPiDIP-59128N.
STRINGi412030.XP_001448363.1.

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 20Combined sources14
Beta strandi25 – 28Combined sources4
Helixi30 – 39Combined sources10
Helixi46 – 56Combined sources11
Beta strandi61 – 65Combined sources5
Helixi66 – 93Combined sources28
Beta strandi98 – 101Combined sources4
Helixi103 – 112Combined sources10
Turni114 – 116Combined sources3
Helixi119 – 129Combined sources11
Beta strandi131 – 137Combined sources7
Helixi139 – 147Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLMX-ray1.80A2-149[»]
1EXRX-ray1.00A2-149[»]
1N0YX-ray1.75A/B2-149[»]
1OSAX-ray1.68A2-149[»]
2KXWNMR-A77-149[»]
2M5ENMR-A77-149[»]
5E1KX-ray1.00A2-149[»]
5E1NX-ray1.00A2-149[»]
5E1PX-ray1.01A2-149[»]
ProteinModelPortaliP07463.
SMRiP07463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07463.

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

Sequence similaritiesi

Belongs to the calmodulin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
InParanoidiP07463.
KOiK02183.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQLTEEQI AEFKEAFALF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL SLMARKMKEQ DSEEELIEAF KVFDRDGNGL
110 120 130 140
ISAAELRHVM TNLGEKLTDD EVDEMIREAD IDGDGHINYE EFVRMMVSK
Length:149
Mass (Da):16,803
Last modified:January 23, 2007 - v3
Checksum:iCDE9230226C3BAB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34540 Genomic DNA. Translation: AAA29443.1.
S68025 Genomic DNA. Translation: AAB20487.1.
CT868385 Genomic DNA. Translation: CAK80966.1.
PIRiA35603. MCPP.
RefSeqiXP_001448363.1. XM_001448326.1.
UniGeneiPte.419.

Genome annotation databases

EnsemblProtistsiCAK80966; CAK80966; GSPATT00015825001.
GeneIDi5034148.
KEGGiptm:GSPATT00015825001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34540 Genomic DNA. Translation: AAA29443.1.
S68025 Genomic DNA. Translation: AAB20487.1.
CT868385 Genomic DNA. Translation: CAK80966.1.
PIRiA35603. MCPP.
RefSeqiXP_001448363.1. XM_001448326.1.
UniGeneiPte.419.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLMX-ray1.80A2-149[»]
1EXRX-ray1.00A2-149[»]
1N0YX-ray1.75A/B2-149[»]
1OSAX-ray1.68A2-149[»]
2KXWNMR-A77-149[»]
2M5ENMR-A77-149[»]
5E1KX-ray1.00A2-149[»]
5E1NX-ray1.00A2-149[»]
5E1PX-ray1.01A2-149[»]
ProteinModelPortaliP07463.
SMRiP07463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59128N.
STRINGi412030.XP_001448363.1.

Proteomic databases

PRIDEiP07463.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiCAK80966; CAK80966; GSPATT00015825001.
GeneIDi5034148.
KEGGiptm:GSPATT00015825001.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
InParanoidiP07463.
KOiK02183.

Miscellaneous databases

EvolutionaryTraceiP07463.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALM_PARTE
AccessioniPrimary (citable) accession number: P07463
Secondary accession number(s): A0DD49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.