P06787 (CALM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calmodulin
Short name=CaM

Gene names

Name:	CMD1
Ordered Locus Names:	YBR109C
ORF Names:	YBR0904

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
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. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Ref.11
Subunit structure	Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110. Interacts with SPC110. Ref.10
Subcellular location	Cytoplasm › cytoskeleton › spindle pole body Ref.10.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	This protein has three functional calcium-binding sites.
Sequence similarities	Belongs to the calmodulin family. Contains 4 EF-hand domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Ligand	Calcium
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Inferred from mutant phenotype. Source: SGD cell budding Inferred from mutant phenotype. Source: SGD karyogamy involved in conjugation with cellular fusion Inferred from mutant phenotype. Source: SGD microautophagy Inferred from mutant phenotype. Source: SGD phosphatidylinositol biosynthetic process Inferred from mutant phenotype. Source: SGD receptor-mediated endocytosis Inferred from mutant phenotype. Source: SGD spindle pole body organization Inferred from mutant phenotype. Source: SGD transcription factor import into nucleus Inferred from mutant phenotype. Source: SGD vacuole fusion, non-autophagic Inferred from direct assay. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD cellular bud tip Inferred from direct assay. Source: SGD central plaque of spindle pole body Inferred from direct assay. Source: SGD incipient cellular bud site Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from direct assay Ref.1. Source: SGD calcium-dependent protein binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNA1	P23287	4	EBI-3976,EBI-12771

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 147

147

Calmodulin

PRO_0000198328

Regions

Domain

8 – 43

36

EF-hand 1

Domain

44 – 79

36

EF-hand 2

Domain

81 – 116

36

EF-hand 3

Domain

117 – 147

31

EF-hand 4

Calcium binding

21 – 32

12

1 Ref.8

Calcium binding

57 – 68

12

2 Ref.8

Calcium binding

94 – 105

12

3 Ref.8

Amino acid modifications

Modified residue

29

1

Phosphoserine Ref.13

Modified residue

82

1

Phosphoserine Ref.13

Modified residue

102

1

Phosphoserine Ref.13

Modified residue

112

1

Phosphoserine Ref.12 Ref.13

Experimental info

Mutagenesis

21

1

D → A: Highly reduced affinity for Ca(2+).

Mutagenesis

32

1

E → V: Highly reduced affinity for Ca(2+).

Mutagenesis

57

1

D → A: Highly reduced affinity for Ca(2+).

Mutagenesis

68

1

E → V: Highly reduced affinity for Ca(2+).

Mutagenesis

94

1

D → A: Highly reduced affinity for Ca(2+).

Mutagenesis

105

1

E → V: Highly reduced affinity for Ca(2+).

Secondary structure

1

.

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.

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.

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.

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.

.

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.

.

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147

Helix Strand Turn

Details...

Helix

7 – 19

13

Beta strand

25 – 29

5

Helix

30 – 40

11

Helix

46 – 54

9

Beta strand

63 – 65

3

Helix

66 – 73

8

Helix

82 – 93

12

Beta strand

95 – 98

4

Beta strand

100 – 102

3

Helix

103 – 113

11

Helix

119 – 129

11

Beta strand

132 – 137

6

Helix

138 – 145

8

Sequences

	Sequence		Length	Mass (Da)
	P06787 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 819ED1AD5D9400D3	FASTA	147	16,135
	10 20 30 40 50 60 MSSNLTEEQI AEFKEAFALF DKDNNGSISS SELATVMRSL GLSPSEAEVN DLMNEIDVDG 70 80 90 100 110 120 NHQIEFSEFL ALMSRQLKSN DSEQELLEAF KVFDKNGDGL ISAAELKHVL TSIGEKLTDA 130 140 EVDDMLREVS DGSGEINIQQ FAALLSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the yeast calmodulin gene: calmodulin is an essential protein." Davis T.N., Urdea M.S., Masiarz F.R., Thorner J. Cell 47:423-431(1986) [PubMed: 3533275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Gain of function mutations for yeast calmodulin and calcium dependent regulation of protein kinase activity." Lukas T.J., Collinge M., Haiech J., Watterson D.M. Biochim. Biophys. Acta 1223:341-347(1994) [PubMed: 7918668] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of a 70 kb region on the right arm of yeast chromosome II." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 10:1363-1381(1994) [PubMed: 7900426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"Isolation of the yeast calmodulin gene using synthetic oligonucleotide probes." Davis T.N., Thorner J. Methods Enzymol. 139:248-259(1987) [PubMed: 3295478] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-30 AND 128-145.
[8]	"Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry." Brockerhoff S.E., Edmonds C.G., Davis T.N. Protein Sci. 1:504-516(1992) [PubMed: 1304352] [Abstract] Cited for: CALCIUM-BINDING DATA.
[9]	"Can calmodulin function without binding calcium?" Geiser J.R., van Tuinen D., Brockerhoff S.E., Neff M.M., Davis T.N. Cell 65:949-959(1991) [PubMed: 2044154] [Abstract] Cited for: MUTAGENESIS.
[10]	"The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae." Geiser J.R., Sundberg H.A., Chang B.H., Muller E.G., Davis T.N. Mol. Cell. Biol. 13:7913-7924(1993) [PubMed: 8247006] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SPC110.
[11]	"Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication." Elliott S., Knop M., Schlenstedt G., Schiebel E. Proc. Natl. Acad. Sci. U.S.A. 96:6205-6210(1999) [PubMed: 10339566] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SPC110 COMPLEX.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-82; SER-102 AND SER-112, MASS SPECTROMETRY.
[14]	"Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR." Ohki S.-Y., Miura K., Saito M., Nakashima K., Maekawa H., Yazawa M., Tsuda S., Hikichi K. J. Biochem. 119:1045-1055(1996) [PubMed: 8827436] [Abstract] Cited for: STRUCTURE BY NMR OF 1-78.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14760 Genomic DNA. Translation: AAA34504.1.
AF081667 Genomic DNA. Translation: AAC68888.1.
X78993 Genomic DNA. Translation: CAA55612.1.
Z35978 Genomic DNA. Translation: CAA85064.1.
AY558184 Genomic DNA. Translation: AAS56510.1.
BK006936 Genomic DNA. Translation: DAA07228.1.

PIR

MCBY. A25060.

RefSeq

NP_009667.1. NM_001178457.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F54	NMR	-	A	2-78	[»]
1F55	NMR	-	A	2-78	[»]
1LKJ	NMR	-	A	2-147	[»]

ProteinModelPortal

P06787.

SMR

P06787. Positions 2-147.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-536N.

IntAct

P06787. 52 interactions.

MINT

MINT-655049.

STRING

P06787.

Proteomic databases

PeptideAtlas

P06787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR109C; YBR109C; YBR109C.

GeneID

852406.

KEGG

sce:YBR109C.

NMPDR

fig|4932.3.peg.366.

Organism-specific databases

CYGD

YBR109c.

SGD

S000000313. CMD1.

Phylogenomic databases

eggNOG

fuNOG08610.

GeneTree

EFGT00050000003660.

HOGENOM

HBG746798.

OMA

FLALMSR.

OrthoDB

EOG4WQ4C0.

Gene expression databases

ArrayExpress

P06787.

Genevestigator

P06787.

GermOnline

YBR109C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 2 hits.

KO

K02183.

Pfam

PF00036. efhand. 2 hits.
[Graphical view]

SMART

SM00054. EFh. 3 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

971249.

Entry information

Entry name

CALM_YEAST

Accession

Primary (citable) accession number: P06787
Secondary accession number(s): D6VQA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 25, 2012
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program