Myristoylated alanine-rich C-kinase substrate

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P12624 (MARCS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Myristoylated alanine-rich C-kinase substrate
Short name=MARCKS

Alternative name(s):
ACAMP-81

Gene names

Name:	MARCKS
Synonyms:	MACS

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
Subcellular location	Cell membrane; Lipid-anchor. Cytoplasm Ref.6.
Post-translational modification	Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity. Myristoylation is found on 70-80% of the protein chains.
Sequence similarities	Belongs to the MARCKS family.
Sequence caution	The sequence AAA30635.1 differs from that shown. Reason: Frameshift at positions 141 and 151.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Actin-binding Calmodulin-binding
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

Myristoylated alanine-rich C-kinase substrate

PRO_0000157147

Regions

Region

151 – 175

Calmodulin-binding (PSD)

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.8

Modified residue

100

Phosphoserine Ref.8

Modified residue

117

Phosphoserine; by MAPK Probable

Modified residue

134

Phosphoserine Ref.8

Modified residue

142

Phosphothreonine By similarity

Modified residue

144

Phosphoserine By similarity

Modified residue

146

Phosphoserine By similarity

Modified residue

149

Phosphothreonine By similarity

Modified residue

158

Phosphoserine; by PKC Ref.7

Modified residue

162

Phosphoserine; by PKC Ref.7

Modified residue

166

Phosphoserine; by PKC Ref.7

Modified residue

169

Phosphoserine; by PKC Ref.7

Modified residue

264

Phosphoserine By similarity

Lipidation

N-myristoyl glycine Ref.8

Experimental info

Sequence conflict

99 – 100

AS → H in AAA30635. Ref.2

Sequence conflict

111

E → G Ref.1

Sequence conflict

111

E → G in AAA30635. Ref.2

Sequence conflict

132

T → S Ref.1

Sequence conflict

132

T → S in AAA30635. Ref.2

Sequence conflict

254 – 256

SEE → RRG in AAA30635. Ref.2

Sequence conflict

279

G → GAAG in AAA30635. Ref.2

Sequence conflict

290 – 299

VPPEQEAAPA → CPRAGGAPR Ref.1

Sequence conflict

290 – 299

VPPEQEAAPA → CPRAGGAPR in AAA30635. Ref.2

Sequence conflict

304 – 306

AAP → PPR Ref.1

Sequence conflict

304 – 306

AAP → PPR in AAA30635. Ref.2

Sequence conflict

304 – 306

AAP → PPR Ref.4

Sequence conflict

312

A → S Ref.1

Sequence conflict

312

A → S in AAA30635. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P12624 [UniParc].

Last modified May 29, 2007. Version 6.
Checksum: 2F9E895274058062
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FASTA

333

31,665

        10         20         30         40         50         60 
MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA 

        70         80         90        100        110        120 
NGSAPAADKE EPAAAGSGAA SPAAAEKDEP AAAAPDAGAS PVEKEAPVEG EAAEPGSPTA 

       130        140        150        160        170        180 
AEGEAASAAS STSSPKAEDG ATPSPSNETP KKKKKRFSFK KSFKLSGFSF KKNKKEAGEG 

       190        200        210        220        230        240 
GEAEGAAGAS AEGGKDEASG GAAAAAGEAG AAPGEPTAAP GEEAAAGEEG AAGGDPQEAK 

       250        260        270        280        290        300 
PEEAAVAPEK PPASEEAKAV EEPSKAEEKA EEAGVSAAGC EAPSAAGPGV PPEQEAAPAE 

       310        320        330 
EAAAAPASSA CAAPSQEAQP ECSPEAPPAE AAE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA for the bovine myristoylated alanine-rich C kinase substrate (MARCKS)." Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J. Nucleic Acids Res. 17:3987-3988(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning, characterization, and expression of a cDNA encoding the '80- to 87-kDa' myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C." Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J. Proc. Natl. Acad. Sci. U.S.A. 86:4012-4016(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.
[4]	"Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species." Herget T., Brooks S.F., Broad S., Rozengurt E. Eur. J. Biochem. 209:7-14(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-322.
[5]	"Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I." Mizutani A., Tokumitsu H., Hidaka H. Biochem. Biophys. Res. Commun. 182:1395-1401(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[6]	"Isolation of the non-myristoylated form of a major substrate of protein kinase C (MARCKS) from bovine brain." Manenti S., Sorokine O., van Dorsselaer A., Taniguchi H. J. Biol. Chem. 268:6878-6881(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-12, IDENTIFICATION OF A NON-MYRISTOYLATED FORM, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[7]	"Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C." Graff J.M., Stumpo D.J., Blackshear P.J. J. Biol. Chem. 264:11912-11919(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-158; SER-162; SER-166 AND SER-169.
[8]	"Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s). A mass spectroscopic analysis of the post-translational modifications." Taniguchi H., Manenti S., Suzuki M., Titani K. J. Biol. Chem. 269:18299-18302(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-27; SER-46; SER-81; SER-100; SER-117 AND SER-134, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane." Thelen M., Rosen A., Nairn A.C., Aderem A. Nature 351:320-322(1991) [PubMed] [Europe PMC] [Abstract] Cited for: REVERSIBLE ASSOCIATION WITH THE MEMBRANE.
[10]	"MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin." Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., Aderem A. Nature 356:618-622(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIN-FILAMENT CROSS-LINKING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24638 Genomic DNA. Translation: AAA30635.1. Frameshift. BC115989 mRNA. Translation: AAI15990.1.
IPI	IPI00760436.
PIR	S08341.
RefSeq	NP_001069744.1. NM_001076276.1.
UniGene	Bt.101114.
3D structure databases
ProteinModelPortal	P12624.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000002691.
Proteomic databases
PaxDb	P12624.
PRIDE	P12624.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	613548.
KEGG	bta:613548.
Organism-specific databases
CTD	4082.
Phylogenomic databases
eggNOG	NOG44640.
HOGENOM	HOG000113482.
HOVERGEN	HBG081955.
InParanoid	P12624.
KO	K12561.
Family and domain databases
InterPro	IPR002101. MARCKS. [Graphical view]
PANTHER	PTHR14353. PTHR14353. 1 hit.
Pfam	PF02063. MARCKS. 1 hit. [Graphical view]
PRINTS	PR00963. MARCKS.
PROSITE	PS00826. MARCKS_1. 1 hit. PS00827. MARCKS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20898633.

Entry information

Entry name

MARCS_BOVIN

Accession

Primary (citable) accession number: P12624
Secondary accession number(s): Q1LZI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	May 29, 2007
Last modified:	April 3, 2013
This is version 110 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents