Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62155

- CALM_XENLA

UniProt

P62155 - CALM_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Calmodulin

Gene

calm1

more
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 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

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

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

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

Organism-specific databases

XenbaseiXB-GENE-976648. calm1.
XB-GENE-1014645. calm2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 149148CalmodulinPRO_0000198242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei116 – 1161N6,N6,N6-trimethyllysineBy 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

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Beta strandi22 – 243Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 3910Combined sources
Helixi46 – 5611Combined sources
Beta strandi58 – 603Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 7611Combined sources
Beta strandi77 – 815Combined sources
Helixi84 – 9310Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 11210Combined sources
Helixi119 – 12911Combined sources
Beta strandi134 – 1385Combined sources
Helixi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62155.

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

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

        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:January 23, 2007 - v2
Checksum:i6B4BC3FCDE10727B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 99 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