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P62155

- CALM_XENLA

UniProt

P62155 - CALM_XENLA

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Protein
Calmodulin
Gene
calm1
calm2
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 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 – 32121
Add
BLAST
Calcium bindingi57 – 68122
Add
BLAST
Calcium bindingi94 – 105123
Add
BLAST
Calcium bindingi130 – 141124
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: IntAct
  3. receptor binding Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:calm1
AND
Name:calm2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus
XenbaseiXB-GENE-976648. calm1.
XB-GENE-1014645. calm2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 149148Calmodulin
PRO_0000198242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei116 – 1161N6,N6,N6-trimethyllysine By similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PRIDEiP62155.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cyaP401362EBI-397568,EBI-457011From a different organism.

Protein-protein interaction databases

IntActiP62155. 3 interactions.
MINTiMINT-7032991.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014
Beta strandi22 – 243
Beta strandi25 – 284
Helixi30 – 3910
Helixi46 – 5611
Beta strandi58 – 603
Beta strandi61 – 655
Helixi66 – 7611
Beta strandi77 – 815
Helixi84 – 9310
Turni95 – 973
Beta strandi98 – 1014
Helixi103 – 11210
Helixi119 – 12911
Beta strandi134 – 1385
Helixi139 – 1468

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-A2-149[»]
1X02NMR-A2-149[»]
1Y0VX-ray3.60H/I/J/K/L/M6-149[»]
2COLX-ray2.20B80-146[»]
2K3SNMR-B83-149[»]
2KDUNMR-A2-149[»]
2LLONMR-A2-81[»]
2LLQNMR-A83-149[»]
2RRTNMR-A79-149[»]
ProteinModelPortaliP62155.
SMRiP62155. Positions 1-149.

Miscellaneous databases

EvolutionaryTraceiP62155.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the calmodulin family.
Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG012180.
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]
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.

P62155-1 [UniParc]FASTAAdd to Basket

« Hide

MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ    50
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY 100
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK 149
Length:149
Mass (Da):16,838
Last modified:January 23, 2007 - v2
Checksum:i6B4BC3FCDE10727B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiI51402.
RefSeqiNP_001080864.1. NM_001087395.1.
NP_001084025.1. NM_001090556.1.
NP_001089059.1. NM_001095590.1.
UniGeneiXl.54061.
Xl.543.
Xl.54419.

Genome annotation databases

GeneIDi380558.
399259.
606721.
KEGGixla:380558.
xla:399259.
xla:606721.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi I51402.
RefSeqi NP_001080864.1. NM_001087395.1.
NP_001084025.1. NM_001090556.1.
NP_001089059.1. NM_001095590.1.
UniGenei Xl.54061.
Xl.543.
Xl.54419.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CFC NMR - A 2-149 [» ]
1CFD NMR - A 2-149 [» ]
1CFF NMR - A 2-149 [» ]
1CKK NMR - A 2-149 [» ]
1DMO NMR - A 2-149 [» ]
1F70 NMR - A 2-77 [» ]
1F71 NMR - A 83-149 [» ]
1IQ5 X-ray 1.80 A 1-149 [» ]
1MUX NMR - A 2-149 [» ]
1NWD NMR - A 2-149 [» ]
1SY9 NMR - A 2-149 [» ]
1X02 NMR - A 2-149 [» ]
1Y0V X-ray 3.60 H/I/J/K/L/M 6-149 [» ]
2COL X-ray 2.20 B 80-146 [» ]
2K3S NMR - B 83-149 [» ]
2KDU NMR - A 2-149 [» ]
2LLO NMR - A 2-81 [» ]
2LLQ NMR - A 83-149 [» ]
2RRT NMR - A 79-149 [» ]
ProteinModelPortali P62155.
SMRi P62155. Positions 1-149.
ModBasei Search...

Protein-protein interaction databases

IntActi P62155. 3 interactions.
MINTi MINT-7032991.

Chemistry

BindingDBi P62155.

Proteomic databases

PRIDEi P62155.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 380558.
399259.
606721.
KEGGi xla:380558.
xla:399259.
xla:606721.

Organism-specific databases

CTDi 801.
805.
Xenbasei XB-GENE-976648. calm1.
XB-GENE-1014645. calm2.

Phylogenomic databases

HOVERGENi HBG012180.
KOi K02183.

Miscellaneous databases

EvolutionaryTracei P62155.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 2 hits.
[Graphical view ]
SMARTi SM00054. EFh. 4 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiCALM_XENLA
AccessioniPrimary (citable) accession number: P62155
Secondary accession number(s): P02593
, P70667, P99014, Q61379, Q61380, Q6INP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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