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proto-oncogene tyrosine-protein kinase MER; C-mer; receptor tyrosine kinase MerTK (MERTK, MER)
Function:
- receptor tyrosine kinase encoded by a transforming gene expressed in neoplastic T-cells & B-cells
- appears to be necessary for phagocytosis & efficient clearance of apoptotic cells
Structure:
- belongs to the protein kinase superfamily, tyrosine protein kinase family, AXL/UFO subfamily
- contains 2 fibronectin F3 modules
- contains 2 Ig-like C2-type domains (immunoglobulin-like)
- contains 1 protein kinase domain
Compartment: membrane
Expression:
- not expressed in normal B- & T-lymphocytes but is expressed in numerous neoplastic B- & T-cell lines
Pathology:
1) defects in MERTK are a cause of retinitis pigmentosa
2) in case of filovirus infection, MERTK seems to function as a cell entry factor
Laboratory:
- MER Ab in serum/plasma
General
proto oncogene protein
tyrosine kinase receptor (RTK)
Properties
SIZE: entity length = 999 aa
MW = 110 kD
COMPARTMENT: cellular membrane
STATE: active state
MOTIF: signal sequence {1-20}
immunoglobulin superfamily domain {81-186}
MOTIF: N-glycosylation site {N114}
cysteine residue {C115}
MODIFICATION: cysteine residue {C175}
N-glycosylation site {N170}
cysteine residue {C175}
MODIFICATION: cysteine residue {C115}
immunoglobulin superfamily domain {197-273}
MOTIF: N-glycosylation site {N207}
N-glycosylation site {N215}
cysteine residue {C218}
MODIFICATION: cysteine residue {C262}
N-glycosylation site {N234}
cysteine residue {C262}
MODIFICATION: cysteine residue {C218}
fibronectin type III domain or F3 module {284-379}
MOTIF: N-glycosylation site {N294}
N-glycosylation site {N316}
N-glycosylation site {N329}
N-glycosylation site {N336}
N-glycosylation site {N354}
fibronectin type III domain or F3 module {383-482}
MOTIF: N-glycosylation site {N389}
N-glycosylation site {N395}
N-glycosylation site {N442}
N-glycosylation site {N454}
transmembrane domain {506-526}
kinase domain
SITE: 587-858
MOTIF: ATP-binding site
NAME: ATP-binding site
SITE: 593-601
ATP-binding site
NAME: ATP-binding site
SITE: 615-615
aspartate residue {D723}
Tyr phosphorylation site {Y754}
Database Correlations
OMIM correlations
MORBIDMAP 604705
UniProt Q12866
PFAM correlations
Kegg hsa:1046
ENZYME 2.7.10.1
References
- UniProt :accession Q12866
- Mutations of the MERTK gene
Retina International's Scientific Newsletter
http://www.retina-international.com/sci-news/mertkmut.htm
- Varnum BC et al
Axl receptor tyrosine kinase stimulated by the vitamin K-
dependent protein encoded by growth-arrest-specific gene 6.
Nature 373:623 1995
PMID: 7854420
- Scott RS et al.
Phagocytosis and clearance of apoptotic cells is mediated by
MER.
Nature 411:207-11 2001
PMID: 11346799