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MERTK (c-mer proto-oncogene tyrosine kinase)

Identity

Other namesC-mer
EC 2.7.10.1
MER
MGC133349
RP38
c-mer
Eyk (chicken)
mer
MerTK
Nyk
Tyro-12 (rat)
HGNC (Hugo) MERTK
LocusID (NCBI) 10461
Location 2q13
Location_base_pair Starts at 112656191 and ends at 112786945 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  DNA structure of the MERTK gene aligned with the corresponding functional protein domains. The open ended boxes for exons 1 and 19 indicate untranslated regions which are not depicted here.
Description The human MERTK gene is located on chromosome 2q14.1 and contains 19 exons. Exons 1-9 encode the extracellular domain, exon 10 encodes the transmembrane domain, and exons 11-19 encode the intracellular domain. Within the extracellular domain, two immunoglobulin (Ig) domains and two fibronectin type III (FNIII) domains are present. The Ig domains are encoded by exons 2-5 and the FNIII domains are encoded by exons 6-9. Within the intracellular region, exons 13-19 encode the tyrosine kinase domain (Gal et al., 2000).
Transcription Tissue analysis of MERTK expression has demonstrated a 4.4 kilobase message in a spectrum of tissues including the testis, ovary, prostate, lung, kidney, spleen, placenta, thymus, small intestine, colon, and liver. A larger transcript (approximately 5.5 to 6.5 kilobase message) has been detected in testis and ovary. A potential alternatively spliced transcript is generated by the insertion of a novel exon between exons 7 and exon 8. This alternative transcript may encode a soluble MERTK (Graham et al., 1994).

Protein

 
  The diagram above depicts the domain structure of the Mer receptor tyrosine kinase protein. The conserved sequence within the kinase domain is depicted. The diagram below depicts the domain structure of the ligands, Gas6 and Protein S. Gas6 and Protein S have the same domain structure with the exception of thrombin cleavage sites which are present in the loop region of Protein S but not Gas6. Vitamin-K dependent carboxylation of the Gamma-carboxyglutamic acid (Gla) domain is required for biologic activity of these ligands. The crystal structure of a Gas6/Axl complex suggests that the laminin G-like (LG) domains mediate binding to the Ig-like domains of MERTK.
Description The MERTK receptor is synthesized as a protein containing 999 amino acids. Although the predicted molecular weight of MERTK is approximately 110 kD, the extracellular domain of MERTK possesses sites for NH2-linked glycosylation and the mature, fully glycosylated form of MERTK is approximately 205 kD (Sather et al., 2007). Depending on the cell type, underglycosylated forms of MERTK protein may also be produced leading to a range in MERTK protein sizes from 160 to 205 kD. The extracellular component of the MERTK receptor encodes two Ig domains (aa 112-186 for domain 1 and aa 197-280 for domain 2) and two FNIII domains (aa 284-378 for domain 1 and 386-478 for domain 2). The two Ig domains and two FNIII domains define MERTK as part of a family of receptor tyrosine kinases (RTKs) which contains only two other members, AXL and Tyro-3. Together, Tyro-3, Axl, and Mer constitute the TAM family of receptor tyrosine kinases (Linger et al., 2008). The extracellular domain of MERTK serves as the ligand binding region for the ligands GAS6 (Chen et al., 1997) and Protein S (Prasad et al., 2006). Specifically, Gas6 has been shown to bind TAM receptors in the immunologlobulin domains (Sasaki et al., 2006).
The intracellular component of the MERTK receptor includes the tyrosine kinase domain (aa 600-848). Within this tyrosine kinase domain is a signature motif, KWIAIES, which is only found in the TAM receptor tyrosine kinases (Graham et al., 1994). Following ligand binding to the extracellular domain, MERTK receptor dimerization and tyrosine autophosphorylation occurs. Three tyrosine residues (Y749, Y753, and Y754) within the activation loop of the kinase domain have been identified as the primary sites of autophosphorylation (Ling et al., 1996). These three residues are also conserved in the same sequence context in Axl and Tyro-3. Another residue within the kinase domain, Y872, is part of consensus GRB2 binding site, YXNX, and the corresponding sequence in murine MERTK has been shown to bind Grb2, recruit and activate PI3K as well as transcriptionally activate NF-kB (Georgescu et al., 1999). Phosphorylation and activation of PLCgamma may occur through direct binding of one of its SH2 domains to endogenous phospho-MERTK (Sen et al., 2007). Similarly, there is evidence that PI3K may interact with MERTK via a SH2 domain (Sen et al., 2007). Finally, VAV1 has been shown to constitutively interact with MERTK, and the release of VAV1 upon ligand-dependent MERTK activation leads to activation of Rho family members (Mahajan et al., 2003).
The extracellular domain of MERTK is also constitutively shed via cleavage due to a metalloproteinase. The resulting soluble MERTK consists of both Ig domains and both FNIII domains, and is believed to function as a decoy receptor for MERTK ligands (Sather et al., 2007).
Expression Within hematopoietic lineages, MERTK is expressed in macrophages, dendritic cells, NK cells, NKT cells, megakaryocytes, and platelets (Graham et al., 1994; Angelillo-Scherrer et al., 2001; Behrens et al., 2003). High levels of MERTK expression are also detected in ovary, prostate, testis, lung, retina, and kidney. Lower levels of Mer are found in heart, brain, and skeletal muscle (Graham et al., 1994). Upregulation or ectopic Mer expression is found in a spectrum of malignant cells (Linger et al., 2008).
Localisation MERTK is a transmembrane receptor tyrosine kinase.
Function The activation of MERTK and downstream signaling via PI3K/Akt, PLCGamma, VAV1, and MAPK/ERK are thought to mediate MERTK's cellular functions in cell survival, proinflammatory cytokine production, and actin reorganization/cell migration. Overexpression or ectopic expression of MERTK has been implicated in oncogenesis (Linger et al., 2008).
Homology The two Ig domains and two FNIII domains are shared with Axl and Tyro-3, the other two members of the TAM RTK family. The protein sequences of TAM receptors are 31-36% identical (52-57% similar) in the extracellular regions. The intracellular domains share 54-59% sequence identity (72-75% similarity) with higher homology in the tyrosine kinase domain (Graham et al., 1995).

Mutations

Germinal Germline mutations in the second exon of MERTK are well characterized and lead to retinitis pigmentosa and retinal dystrophy. The first description of this mutation was in the Royal College of Surgeon (RCS) rat and details a deletion that leads to a frameshift and early translation termination codon, resulting in an aberrant non-functional protein product (D'Cruz et al., 2000). A similar retinal dystrophy phenotype is found in the merkd mouse, which contains a targeted disruption of the MERTK gene (Duncan et al., 2003). In humans several different mutations that affect the MERTK region have been described in individuals suffering from retinal dystrophy.

Implicated in

Entity Retinitis pigmentosa and retinal dystrophy
Disease Retinitis pigementosa is a disorder that affects 1 in 3500 people and stems from loss of functional photoreceptor cells in the retina, and eventual visual loss. Loss of functional MERTK protein leads to ineffective phagocytosis and clearance of apoptotic cells, with resultant buildup of the retinal pigmented epithelium leading to visual loss and is one known genetic cause of retinal dystrophy (Shuster et al., 1990; Gal et al., 2000; Tada et al., 2006; Tschernutter et al., 2006).
  
Entity Malignancy
Disease MERTK and its family members have been implicated in a number of malignant conditions. MERTK is not expressed on the normal lymphocytes but has been found to be expressed in a majority of lymphoblasts from patients with T-cell leukemia, certain subsets of B-cell leukemia, and mantle cell lymphoma (Yeoh et al., 2002; Graham et al., 2006). Forced overexpression of MERTK in a murine model leads to T-cell leukemia and lymphoma (Keating et al., 2006). MERTK has also been associated with a variety of other non-hematologic malignancies including: glioblastoma multiforme (Ling et al., 1995), gastric cancer (Wu et al., 2002), and prostate cancer (Mahajan et al., 2005). MERTK is known to play a role in several oncogenic mechanisms, including angiogenesis, migration and invasion, and cell survival signaling as reviewed in Linger et al (2008).
  
Entity Autoimmune Disease
Disease Animal models that lack functional MERTK protein have macrophages that are unable to appropriately engulf apoptotic cells. This inefficient clearance of dead cells can lead to activation of inflammation and development of autoimmunity (Scott et al., 2001). This mechanism has been suggested for systemic lupus erythematosis, but no human cases have been reported.
  

External links

Nomenclature
HGNC (Hugo)MERTK   7027
Cards
AtlasMERTKID41339ch2q13
Entrez_Gene (NCBI)MERTK  10461  MER proto-oncogene, tyrosine kinase
GeneCards (Weizmann)MERTK
Ensembl (Hinxton)ENSG00000153208 [Gene_View]  chr2:112656191-112786945 [Contig_View]  MERTK [Vega]
ICGC DataPortalENSG00000153208
AceView (NCBI)MERTK
Genatlas (Paris)MERTK
WikiGenes10461
SOURCE (Princeton)NM_006343
Genomic and cartography
GoldenPath (UCSC)MERTK  -  2q13   chr2:112656191-112786945 +  2q14.1   [Description]    (hg19-Feb_2009)
EnsemblMERTK - 2q14.1 [CytoView]
Mapping of homologs : NCBIMERTK [Mapview]
OMIM604705   613862   
Gene and transcription
Genbank (Entrez)AK026681 AK294196 AK308695 AK316584 AL705756
RefSeq transcript (Entrez)NM_006343
RefSeq genomic (Entrez)AC_000134 NC_000002 NC_018913 NG_011607 NT_005403 NW_001838840 NW_004929304
Consensus coding sequences : CCDS (NCBI)MERTK
Cluster EST : UnigeneHs.306178 [ NCBI ]
CGAP (NCI)Hs.306178
Alternative Splicing : Fast-db (Paris)GSHG0016773
Alternative Splicing GalleryENSG00000153208
Gene ExpressionMERTK [ NCBI-GEO ]     MERTK [ SEEK ]   MERTK [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ12866 (Uniprot)
NextProtQ12866  [Medical]
With graphics : InterProQ12866
Splice isoforms : SwissVarQ12866 (Swissvar)
Catalytic activity : Enzyme2.7.10.1 [ Enzyme-Expasy ]   2.7.10.12.7.10.1 [ IntEnz-EBI ]   2.7.10.1 [ BRENDA ]   2.7.10.1 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)FN3 (PS50853)    IG_LIKE (PS50835)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)   
Domains : Interpro (EBI)Fibronectin_type3    Ig-like_dom    Ig-like_fold    Ig_I-set    Ig_sub    Kinase-like_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser-Thr/Tyr_kinase_cat_dom    Tyr_kinase_AS    Tyr_kinase_cat_dom   
Related proteins : CluSTrQ12866
Domain families : Pfam (Sanger)fn3 (PF00041)    I-set (PF07679)    Pkinase_Tyr (PF07714)   
Domain families : Pfam (NCBI)pfam00041    pfam07679    pfam07714   
Domain families : Smart (EMBL)FN3 (SM00060)  IG (SM00409)  TyrKc (SM00219)  
DMDM Disease mutations10461
Blocks (Seattle)Q12866
PDB (SRS)2DBJ    2P0C    3BPR    3BRB    3TCP    4M3Q   
PDB (PDBSum)2DBJ    2P0C    3BPR    3BRB    3TCP    4M3Q   
PDB (IMB)2DBJ    2P0C    3BPR    3BRB    3TCP    4M3Q   
PDB (RSDB)2DBJ    2P0C    3BPR    3BRB    3TCP    4M3Q   
Human Protein AtlasENSG00000153208
Peptide AtlasQ12866
HPRD05269
IPIIPI00029756   IPI00873918   IPI00917839   IPI00917977   IPI00915893   
Protein Interaction databases
DIP (DOE-UCLA)Q12866
IntAct (EBI)Q12866
FunCoupENSG00000153208
BioGRIDMERTK
InParanoidQ12866
Interologous Interaction database Q12866
IntegromeDBMERTK
STRING (EMBL)MERTK
Ontologies - Pathways
Ontology : AmiGOphotoreceptor outer segment  natural killer cell differentiation  transmembrane receptor protein tyrosine kinase activity  protein binding  ATP binding  extracellular space  cytoplasm  plasma membrane  integral component of plasma membrane  protein phosphorylation  phagocytosis  cell surface receptor signaling pathway  cell-cell signaling  spermatogenesis  blood coagulation  rhabdomere  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  platelet activation  secretion by cell  substrate adhesion-dependent cell spreading  apoptotic cell clearance  protein kinase B signaling  positive regulation of phagocytosis  leukocyte migration  negative regulation of lymphocyte activation  retina development in camera-type eye  vagina development  
Ontology : EGO-EBIphotoreceptor outer segment  natural killer cell differentiation  transmembrane receptor protein tyrosine kinase activity  protein binding  ATP binding  extracellular space  cytoplasm  plasma membrane  integral component of plasma membrane  protein phosphorylation  phagocytosis  cell surface receptor signaling pathway  cell-cell signaling  spermatogenesis  blood coagulation  rhabdomere  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  platelet activation  secretion by cell  substrate adhesion-dependent cell spreading  apoptotic cell clearance  protein kinase B signaling  positive regulation of phagocytosis  leukocyte migration  negative regulation of lymphocyte activation  retina development in camera-type eye  vagina development  
REACTOMEQ12866 [protein]
REACTOME PathwaysREACT_604 Hemostasis [pathway]
Protein Interaction DatabaseMERTK
Wikipedia pathwaysMERTK
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)MERTK
SNP (GeneSNP Utah)MERTK
SNP : HGBaseMERTK
Genetic variants : HAPMAPMERTK
1000_GenomesMERTK 
ICGC programENSG00000153208 
CONAN: Copy Number AnalysisMERTK 
Somatic Mutations in Cancer : COSMICMERTK 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
LOVD (Leiden Open Variation Database)Eye diseases - LOVD
Mutations and Diseases : HGMDMERTK
OMIM604705    613862   
MedgenMERTK
GENETestsMERTK
Disease Genetic AssociationMERTK
Huge Navigator MERTK [HugePedia]  MERTK [HugeCancerGEM]
Genomic VariantsMERTK  MERTK [DGVbeta]
Exome VariantMERTK
dbVarMERTK
ClinVarMERTK
snp3D : Map Gene to Disease10461
General knowledge
Homologs : HomoloGeneMERTK
Homology/Alignments : Family Browser (UCSC)MERTK
Phylogenetic Trees/Animal Genes : TreeFamMERTK
Chemical/Protein Interactions : CTD10461
Chemical/Pharm GKB GenePA30759
Clinical trialMERTK
Cancer Resource (Charite)ENSG00000153208
Other databases
Probes
Litterature
PubMed85 Pubmed reference(s) in Entrez
CoreMineMERTK
iHOPMERTK

Bibliography

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PMID 8086340
 
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Mutation of the receptor tyrosine kinase gene Mertk in the retinal dystrophic RCS rat.
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Mutations in MERTK, the human orthologue of the RCS rat retinal dystrophy gene, cause retinitis pigmentosa.
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Deficiency or inhibition of Gas6 causes platelet dysfunction and protects mice against thrombosis.
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PMID 16675557
 
Lymphoblastic leukemia/lymphoma in mice overexpressing the Mer (MerTK) receptor tyrosine kinase.
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Contributor(s)

Written11-2008Amy K Keating, Rachel MA Linger, Doug K Graham
Department of Pediatrics, University of Colorado at Denver and Health Sciences Center, Aurora, CO, USA

Citation

This paper should be referenced as such :
Keating, AK ; Linger, RMA ; Graham, DK
MERTK (c-mer proto-oncogene tyrosine kinase)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(10):728-732.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/MERTKID41339ch2q13.html

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indexed on : Mon Oct 13 13:34:52 CEST 2014

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