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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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi21 – 32121Add
BLAST
Calcium bindingi57 – 68122Add
BLAST
Calcium bindingi94 – 105123Add
BLAST
Calcium bindingi130 – 141124Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361V → I in CAM13. 1 Publication
Mutagenesisi41 – 411G → E in CAM12. 1 Publication
Mutagenesisi51 – 511D → G in CAM15. 2 Publications
Mutagenesisi51 – 511D → N in CAM12; lacks the Ca(2+)-dependent K(+) current. 2 Publications
Mutagenesisi55 – 551E → K in CAM11. 1 Publication
Mutagenesisi60 – 601G → S in CAM14. 1 Publication
Mutagenesisi96 – 961D → G in CAM5. 1 Publication
Mutagenesisi102 – 1021S → F in CAM1 (also named PNTA1); lacks the Ca(2+)-dependent K(+) current. 1 Publication
Mutagenesisi103 – 1031A → V in CAM6. 1 Publication
Mutagenesisi105 – 1051E → K in CAM4. 1 Publication
Mutagenesisi136 – 1361H → R in CAM7. 1 Publication
Mutagenesisi137 – 1371I → T in CAM2 (also named PNTA2). 1 Publication
Mutagenesisi146 – 1461M → V in CAM3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 149148CalmodulinPRO_0000198261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei14 – 141N6,N6-dimethyllysine1 Publication
Modified residuei116 – 1161N6,N6,N6-trimethyllysine1 Publication

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

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 3910Combined sources
Helixi46 – 5611Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 9328Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 11210Combined sources
Turni114 – 1163Combined sources
Helixi119 – 12911Combined sources
Beta strandi131 – 1377Combined sources
Helixi139 – 1479Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07463.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationAdd
BLAST

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

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
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. Positions 2-149.
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

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...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in paramecium calmodulin indicate functional differences between the C-terminal and N-terminal lobes in vivo."
    Kink J.A., Maley M.E., Preston R.R., Ling K.Y., Wallen-Friedman M.A., Saimi Y., Kung C.
    Cell 62:165-174(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Stock d4-2.
  3. "Amino acid sequence of a novel calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain."
    Schaefer W.H., Lukas T.J., Blair I.A., Schultz J.E., Watterson D.M.
    J. Biol. Chem. 262:1025-1029(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-14 AND LYS-116.
  4. "A mutant Paramecium with a defective calcium-dependent potassium conductance has an altered calmodulin: a nonlethal selective alteration in calmodulin regulation."
    Schaefer W.H., Hinrichsen R.D., Burgess-Cassler A., Kung C., Blair I.A., Watterson D.M.
    Proc. Natl. Acad. Sci. U.S.A. 84:3931-3935(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-102.
  5. "In vivo mutations of calmodulin: a mutant Paramecium with altered ion current regulation has an isoleucine-to-threonine change at residue 136 and an altered methylation state at lysine residue 115."
    Lukas T.J., Wallen-Friedman M., Kung C., Watterson D.M.
    Proc. Natl. Acad. Sci. U.S.A. 86:7331-7335(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-137.
  6. "Primary mutations in calmodulin prevent activation of the Ca(2+)-dependent Na+ channel in Paramecium."
    Ling K.-Y., Preston R.R., Burns R., Kink J.A., Saimi Y., Kung C.
    Proteins 12:365-371(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-51.
  7. "New non-lethal calmodulin mutations in Paramecium. A structural and functional bipartition hypothesis."
    Ling K.-Y., Maley M.E., Preston R.R., Saimi Y., Kung C.
    Eur. J. Biochem. 222:433-439(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-36; GLY-41; ASP-51; GLU-55; GLY-60; ASP-96; ALA-103; GLU-105; HIS-136 AND MET-146.
  8. "Structure of Paramecium tetraurelia calmodulin at 1.8-A resolution."
    Rao S.T., Wu S., Satyshur K.A., Ling K.-Y., Kung C., Sundaralingam M.
    Protein Sci. 2:436-447(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  9. "Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68-A resolution."
    Ban C., Ramakrishnan B., Ling K.-Y., Kung C., Sundaralingam M.
    Acta Crystallogr. D 50:50-63(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).

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: March 16, 2016
This is version 127 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.