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Protein

MARCKS-related protein

Gene

Marcksl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MARCKS-related protein
Alternative name(s):
Brain protein F52
MARCKS-like protein 1
Macrophage myristoylated alanine-rich C kinase substrate
Short name:
Mac-MARCKS
Short name:
MacMARCKS
Gene namesi
Name:Marcksl1
Synonyms:Mlp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621197. Marcksl1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity; Lipid-anchor 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001571552 – 199MARCKS-related proteinAdd BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei14PhosphothreonineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei71PhosphoserineBy similarity1
Modified residuei85PhosphothreonineBy similarity1
Modified residuei93Phosphoserine; by PKCBy similarity1
Modified residuei101Phosphoserine; by PKCBy similarity1
Modified residuei104Phosphoserine; by PKCBy similarity1
Modified residuei119PhosphoserineBy similarity1
Modified residuei120Phosphoserine; by MAPK8By similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei135PhosphoserineBy similarity1
Modified residuei148Phosphothreonine; by MAPK8By similarity1
Modified residuei151PhosphoserineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei165PhosphoserineBy similarity1
Modified residuei183Phosphothreonine; by MAPK8By similarity1

Post-translational modificationi

Phosphorylation at Ser-120 and Thr-183 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).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ9EPH2.
PRIDEiQ9EPH2.

PTM databases

iPTMnetiQ9EPH2.
PhosphoSitePlusiQ9EPH2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000009113.
GenevisibleiQ9EPH2. RN.

Interactioni

Subunit structurei

Binds to filamentous actin (F-actin), but not to monomeric G-actin, independently of its phosphorylation status.By similarity

Protein-protein interaction databases

BioGridi249517. 1 interactor.
STRINGi10116.ENSRNOP00000065286.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 110Effector domain involved in lipid-bindingBy similarityAdd BLAST24
Regioni87 – 100Calmodulin-binding (PSD)Add BLAST14

Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiQ9EPH2.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG091G0ULD.
PhylomeDBiQ9EPH2.
TreeFamiTF332815.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 1 hit.
PfamiPF02063. MARCKS. 2 hits.
[Graphical view]
PRINTSiPR00963. MARCKS.
PROSITEiPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EPH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL TPKGEGESPP
60 70 80 90 100
VNGADEAAGA TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL
110 120 130 140 150
SGLSFKRNRK EGGGDSSASS PTEEEQEQGE ISACSDEGTA QEGKAAATPE
160 170 180 190
SQEPQAKGAE ASAVSKGGDA EEEAGPQAAE PSTPSGPESG PASASAENE
Length:199
Mass (Da):19,847
Last modified:January 23, 2007 - v3
Checksum:i5107095D4ACD6298
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ301677 mRNA. Translation: CAC18528.1.
BC081789 mRNA. Translation: AAH81789.1.
RefSeqiNP_110489.1. NM_030862.2.
UniGeneiRn.2486.

Genome annotation databases

EnsembliENSRNOT00000012663; ENSRNOP00000012663; ENSRNOG00000009113.
GeneIDi81520.
KEGGirno:81520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ301677 mRNA. Translation: CAC18528.1.
BC081789 mRNA. Translation: AAH81789.1.
RefSeqiNP_110489.1. NM_030862.2.
UniGeneiRn.2486.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249517. 1 interactor.
STRINGi10116.ENSRNOP00000065286.

PTM databases

iPTMnetiQ9EPH2.
PhosphoSitePlusiQ9EPH2.

Proteomic databases

PaxDbiQ9EPH2.
PRIDEiQ9EPH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012663; ENSRNOP00000012663; ENSRNOG00000009113.
GeneIDi81520.
KEGGirno:81520.

Organism-specific databases

CTDi65108.
RGDi621197. Marcksl1.

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiQ9EPH2.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG091G0ULD.
PhylomeDBiQ9EPH2.
TreeFamiTF332815.

Miscellaneous databases

PROiQ9EPH2.

Gene expression databases

BgeeiENSRNOG00000009113.
GenevisibleiQ9EPH2. RN.

Family and domain databases

InterProiIPR002101. MARCKS.
[Graphical view]
PANTHERiPTHR14353. PTHR14353. 1 hit.
PfamiPF02063. MARCKS. 2 hits.
[Graphical view]
PRINTSiPR00963. MARCKS.
PROSITEiPS00826. MARCKS_1. 1 hit.
PS00827. MARCKS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMRP_RAT
AccessioniPrimary (citable) accession number: Q9EPH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.