MARCKS-related protein (MARCKSL1)
The protein contains 195 amino acids for an estimated molecular weight of 19529 Da.
Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation (PubMed:22751924). When unphosphorylated, induces cell migration (By similarity). When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (By similarity). May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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The reference OMIM entry for this protein is 602940
Marcks-like protein 1; marcksl1
Mlp
Marcks-related protein; mrp
Mac-marcks
F52
CLONING
Umekage and Kato (1991) identified a cDNA with homology to MARCKS (PKCSL; 177061) among mouse brain cDNAs with specific brain expression patterns. The myristoylated, alanine-rich protein MARCKS is a widely expressed, prominent substrate for protein kinase C (see 176960), a key enzyme of intracellular signal transduction. The predicted 200-amino acid protein, which they called F52, shares 52% amino acid identity with bovine MARCKS. The similarity between the 2 proteins is found in the consensus myristoylation sequence near the N-terminus and in the 25-amino acid protein kinase C phosphorylation site domain. F52 has a similar amino acid composition to MARCKS, although its alanine content is not as high. It is distributed throughout the mouse brain in a pattern that is distinct from that of MARCKS. By screening a genomic library with portions of the Mrp cDNA, Stumpo et al. (1998) isolated the human homolog, which they designated MLP for 'MARCKS-like protein.' They reported that the sequences of the mouse and human promoters were 71% identical over 433 bp. A transgene containing this 433-bp fragment from mouse linked to a reporter Mrp beta-galactosidase gene produced normal patterns of Mrp expression in the developing mouse embryo. Using Northern hybridization, Lobach et al. (1993) observed Mrp expression in various mouse tissues, with highest levels in testis and uterus.GENE STRUCTURE
Lobach et al. (1993) reported that the mouse F52, or Mrp, gene contains a single intron at a position exactly analogous to that of the single intron in mouse, cow, and human MARCKS.MAPPING
By analysis of an interspecific backcross, Lobach et al. (1993) mapped the Mrp gene to a position on mouse chromosome 4 that was closely linked to the Lck (153390) locus. Based on homology of synteny, they predicted that the human homolog would map to chromosome 1p35-p32. Using somatic cell hybrid analysis and fluorescence in situ hybridization, Stumpo et al. (1998) confirmed that the human MLP gene maps to 1p34.ANIMAL MODEL
Wu et al. (1996) used gene targeting to generate Mrp-deficient mice. They observed severe neural tube defects (NTD) including exencephaly, spina bifida, and tail flexion anomaly in approximately 60% of the homozygous mutants and in approximately 10% of heterozygous animals. The homozygous mutants without exencephaly survived despite brain abnormalities, which appear to occur secondarily to the NTD. Wu et al. (1996) suggested that mutations in Mrp result in isolated NTD and therefore may provide an animal model for common human NTD. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 602940 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).