P35566 (MRP_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MARCKS-related protein

Alternative name(s):
MARCKS-like protein 1
Macrophage myristoylated alanine-rich C kinase substrate
Short name=Mac-MARCKS
Short name=MacMARCKS

Gene names

Name:	MARCKSL1
Synonyms:	MLP, MRP

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems By similarity.
Subunit structure	Binds to filamentous actin (F-actin), but not to monomeric G-actin, independently of its phosphorylation status By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity. Note: Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca2+/calmodulin By similarity.
Post-translational modification	Phosphorylation at Ser-120 and Thr-182 are non-redundantly catalyzed by MAPK8 in vivo. Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8 By similarity.
Sequence similarities	Belongs to the MARCKS family.

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)
Biological_process	positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara
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 – 199	199	MARCKS-related protein		PRO_0000157154
Regions
	Region	87 – 110	24	Effector domain involved in lipid-binding By similarity
	Region	87 – 100	14	Calmodulin-binding (PSD)
Amino acid modifications
	Modified residue	22	1	Phosphoserine By similarity
	Modified residue	36	1	Phosphoserine By similarity
	Modified residue	48	1	Phosphoserine By similarity
	Modified residue	71	1	Phosphoserine By similarity
	Modified residue	85	1	Phosphothreonine By similarity
	Modified residue	93	1	Phosphoserine; by PKC By similarity
	Modified residue	101	1	Phosphoserine; by PKC By similarity
	Modified residue	104	1	Phosphoserine; by PKC By similarity
	Modified residue	120	1	Phosphoserine; by MAPK8 By similarity
	Modified residue	135	1	Phosphoserine By similarity
	Modified residue	148	1	Phosphothreonine; by MAPK8 By similarity
	Modified residue	151	1	Phosphoserine By similarity
	Modified residue	170	1	Phosphothreonine By similarity
	Modified residue	182	1	Phosphothreonine; by MAPK8 By similarity
	Modified residue	184	1	Phosphoserine By similarity
	Modified residue	191	1	Phosphothreonine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35566 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: D8C40706EF86CDE5	FASTA	199	19,766
	10 20 30 40 50 60 MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL TPKGEGESPP VNGTDEAAGA 70 80 90 100 110 120 TGDAIEPAPP SQGAEAKGDA PPKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS 130 140 150 160 170 180 PTEEEQEQGE IGACSEEGTA PEGKAAATPE SQEPQAKGAE AGAACKGGDT EEEAGPPAEP 190 STPSGPESGP TPAGAEQNE

References

[1]	"MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates." Li J., Aderem A. Cell 70:791-801(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Macrophage.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S43921 mRNA. Translation: AAB23156.1.
PIR	A43341.
RefSeq	NP_001075787.1. NM_001082318.1.
UniGene	Ocu.3309.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000007731.
Proteomic databases
PRIDE	P35566.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009158.
Organism-specific databases
CTD	65108.
Phylogenomic databases
eggNOG	NOG38974.
HOGENOM	HOG000059262.
HOVERGEN	HBG003515.
OrthoDB	EOG4TB4CR.
Family and domain databases
InterPro	IPR002101. MARCKS. [Graphical view]
PANTHER	PTHR14353. PTHR14353. 1 hit.
Pfam	PF02063. MARCKS. 2 hits. [Graphical view]
PRINTS	PR00963. MARCKS.
PROSITE	PS00826. MARCKS_1. 1 hit. PS00827. MARCKS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MRP_RABIT

Accession

Primary (citable) accession number: P35566

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program