P62155 (CALM_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calmodulin
Short name=CaM

Gene names

Name:	calm1
AND
Name:	calm2

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Repeat
Ligand	Calcium Metal-binding
PTM	Acetylation Methylation
Technical term	3D-structure
Gene Ontology (GO)
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cya	P40136	2	EBI-397568,EBI-457011	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 149

148

Calmodulin

PRO_0000198242

Regions

Domain

8 – 43

36

EF-hand 1

Domain

44 – 79

36

EF-hand 2

Domain

81 – 116

36

EF-hand 3

Domain

117 – 149

33

EF-hand 4

Calcium binding

21 – 32

12

1

Calcium binding

57 – 68

12

2

Calcium binding

94 – 105

12

3

Calcium binding

130 – 141

12

4

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

116

1

N6,N6,N6-trimethyllysine By similarity

Secondary structure

1

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149

Helix Strand Turn

Details...

Helix

7 – 20

14

Beta strand

22 – 24

3

Beta strand

25 – 28

4

Helix

30 – 39

10

Helix

46 – 56

11

Beta strand

58 – 60

3

Beta strand

61 – 65

5

Helix

66 – 76

11

Beta strand

77 – 81

5

Helix

84 – 93

10

Turn

95 – 97

3

Beta strand

98 – 101

4

Helix

103 – 112

10

Helix

119 – 129

11

Beta strand

134 – 138

5

Helix

139 – 146

8

Sequences

	Sequence		Length	Mass (Da)
	P62155 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B4BC3FCDE10727B	FASTA	149	16,838
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

I51402.

RefSeq

NP_001080864.1. NM_001087395.1.
NP_001084025.1. NM_001090556.1.
NP_001089059.1. NM_001095590.1.

UniGene

Xl.54061.
Xl.543.
Xl.54419.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-148	[»]
1X02	NMR	-	A	2-148	[»]
1Y0V	X-ray	3.60	H/I/J/K/L/M	6-148	[»]
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	[»]

ProteinModelPortal

P62155.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62155. 1 interaction.

Proteomic databases

PRIDE

P62155.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

380558.
399259.
606721.

KEGG

xla:380558.
xla:399259.
xla:606721.

Organism-specific databases

CTD

801.
805.

Xenbase

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

Phylogenomic databases

HOVERGEN

HBG012180.

KO

K02183.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin.
[Graphical view]

Pfam

PF13499. EF_hand_5. 2 hits.
[Graphical view]

PRINTS

PR00450. RECOVERIN.

SMART

SM00054. EFh. 4 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62155.

EvolutionaryTrace

P62155.

Entry information

Entry name

CALM_XENLA

Accession

Primary (citable) accession number: P62155
Secondary accession number(s): P02593 , P70667, P99014, Q61379, Q61380, Q6INP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program