Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62155 (CALM_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calmodulin

Short name=CaM
Gene names
Name:calm1
AND
Name:calm2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Methylation
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

receptor binding

Inferred from physical interaction PubMed 18618700. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cyaP401362EBI-397568,EBI-457011From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 149148Calmodulin
PRO_0000198242

Regions

Domain8 – 4336EF-hand 1
Domain44 – 7936EF-hand 2
Domain81 – 11636EF-hand 3
Domain117 – 14933EF-hand 4
Calcium binding21 – 32121
Calcium binding57 – 68122
Calcium binding94 – 105123
Calcium binding130 – 141124

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1161N6,N6,N6-trimethyllysine By similarity

Secondary structure

........................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62155 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B4BC3FCDE10727B

FASTA14916,838
        10         20         30         40         50         60 
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 

        70         80         90        100        110        120 
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE 

       130        140 
EVDEMIREAD IDGDGQVNYE EFVQMMTAK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of calmodulin genes from Xenopus laevis."
Chien Y.-H., Dawid I.B.
Mol. Cell. Biol. 4:507-513(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1 AND CALM2).
Tissue: Embryo and Kidney.
[3]"Solution structure of calcium-free calmodulin."
Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A.
Nat. Struct. Biol. 2:768-776(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"Calcium-induced conformational transition revealed by the solution structure of apo calmodulin."
Zhang M., Tanaka T., Ikura M.
Nat. Struct. Biol. 2:758-767(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition."
Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T., Ikura M.
J. Mol. Biol. 276:165-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"NMR solution structure of a complex of calmodulin with a binding peptide of the Ca(2+) pump."
Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M., Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H., Vorherr T.E., Carafoli E.
Biochemistry 38:12320-12332(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[7]"A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase."
Osawa M., Tokumitsu H., Swindells M.B., Kurihara H., Orita M., Shibanuma T., Furuya T., Ikura M.
Nat. Struct. Biol. 6:819-824(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[8]"Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings."
Chou J.J., Li S., Bax A.
J. Biomol. NMR 18:217-227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-77 AND 83-149.
[9]"Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin."
Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M.
J. Mol. Biol. 328:193-204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[10]"Solution structure of magnesium-bound form of calmodulin C-domain E104D/E140D Mutant."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 79-149.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01944 mRNA. Translation: AAA49668.1.
K01945 mRNA. Translation: AAA49669.1.
BC054973 mRNA. Translation: AAH54973.1.
BC072232 mRNA. Translation: AAH72232.1.
BC094079 mRNA. Translation: AAH94079.1.
PIRI51402.
RefSeqNP_001080864.1. NM_001087395.1.
NP_001084025.1. NM_001090556.1.
NP_001089059.1. NM_001095590.1.
UniGeneXl.54061.
Xl.543.
Xl.54419.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFCNMR-A2-149[»]
1CFDNMR-A2-149[»]
1CFFNMR-A2-149[»]
1CKKNMR-A2-149[»]
1DMONMR-A2-149[»]
1F70NMR-A2-77[»]
1F71NMR-A83-149[»]
1IQ5X-ray1.80A1-149[»]
1MUXNMR-A2-149[»]
1NWDNMR-A2-149[»]
1SY9NMR-A2-148[»]
1X02NMR-A2-148[»]
1Y0VX-ray3.60H/I/J/K/L/M6-148[»]
2COLX-ray2.20B80-146[»]
2K3SNMR-B83-149[»]
2KDUNMR-A2-149[»]
2LLONMR-A2-81[»]
2LLQNMR-A83-149[»]
2RRTNMR-A79-149[»]
ProteinModelPortalP62155.
SMRP62155. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62155. 3 interactions.
MINTMINT-7032991.

Chemistry

BindingDBP62155.

Proteomic databases

PRIDEP62155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380558.
399259.
606721.
KEGGxla:380558.
xla:399259.
xla:606721.

Organism-specific databases

CTD801.
805.
XenbaseXB-GENE-976648. calm1.
XB-GENE-1014645. calm2.

Phylogenomic databases

HOVERGENHBG012180.
KOK02183.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin_like.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
[Graphical view]
PRINTSPR00450. RECOVERIN.
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62155.

Entry information

Entry nameCALM_XENLA
AccessionPrimary (citable) accession number: P62155
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q61379, Q61380, Q6INP3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references