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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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 199198MARCKS-related proteinPRO_0000157155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei85 – 851PhosphothreonineBy similarity
Modified residuei93 – 931Phosphoserine; by PKCBy similarity
Modified residuei101 – 1011Phosphoserine; by PKCBy similarity
Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei120 – 1201Phosphoserine; by MAPK8By similarity
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei148 – 1481Phosphothreonine; by MAPK8By similarity
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei183 – 1831Phosphothreonine; by MAPK8By similarity

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.
PhosphoSiteiQ9EPH2.

Expressioni

Gene expression databases

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 interaction.
STRINGi10116.ENSRNOP00000065286.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 11024Effector domain involved in lipid-bindingBy similarityAdd
BLAST
Regioni87 – 10014Calmodulin-binding (PSD)Add
BLAST

Sequence similaritiesi

Belongs to the MARCKS family.Curated

Phylogenomic databases

eggNOGiENOG410IDYZ. Eukaryota.
ENOG410Z8K4. LUCA.
GeneTreeiENSGT00730000111349.
HOGENOMiHOG000059262.
HOVERGENiHBG003515.
InParanoidiQ9EPH2.
KOiK13536.
OMAiEIGACGE.
OrthoDBiEOG7W41DW.
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 interaction.
STRINGi10116.ENSRNOP00000065286.

PTM databases

iPTMnetiQ9EPH2.
PhosphoSiteiQ9EPH2.

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.
OrthoDBiEOG7W41DW.
PhylomeDBiQ9EPH2.
TreeFamiTF332815.

Miscellaneous databases

PROiQ9EPH2.

Gene expression databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Rat Mac-MARCKS protein."
    Jess U., El Far O., Betz H.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

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: June 8, 2016
This is version 91 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.