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Database: UniProt
Entry: Q12866
LinkDB: Q12866
Original site: Q12866 
ID   MERTK_HUMAN             Reviewed;         999 AA.
AC   Q12866; Q9HBB4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   29-OCT-2014, entry version 167.
DE   RecName: Full=Tyrosine-protein kinase Mer;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene c-Mer;
DE   AltName: Full=Receptor tyrosine kinase MerTK;
DE   Flags: Precursor;
GN   Name=MERTK; Synonyms=MER;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-118.
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=8086340;
RA   Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.;
RT   "Cloning and mRNA expression analysis of a novel human protooncogene,
RT   c-mer.";
RL   Cell Growth Differ. 5:647-657(1994).
RN   [2]
RP   ERRATUM.
RA   Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.;
RL   Cell Growth Differ. 5:1022-1022(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-999, VARIANTS RP38 LYS-540;
RP   CYS-661 AND THR-871, AND VARIANTS SER-20; ASN-118; THR-282; HIS-293;
RP   LYS-466; SER-498; VAL-518 AND VAL-871.
RX   PubMed=11062461; DOI=10.1038/81555;
RA   Gal A., Li Y., Thompson D.A., Weir J., Orth U., Jacobson S.G.,
RA   Apfelstedt-Sylla E., Vollrath D.;
RT   "Mutations in MERTK, the human orthologue of the RCS rat retinal
RT   dystrophy gene, cause retinitis pigmentosa.";
RL   Nat. Genet. 26:270-271(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   PHOSPHORYLATION AT TYR-749; TYR-753 AND TYR-754.
RX   PubMed=8702477; DOI=10.1074/jbc.271.31.18355;
RA   Ling L., Templeton D., Kung H.J.;
RT   "Identification of the major autophosphorylation sites of Nyk/Mer, an
RT   NCAM-related receptor tyrosine kinase.";
RL   J. Biol. Chem. 271:18355-18362(1996).
RN   [6]
RP   INTERACTION WITH GAS6.
RX   PubMed=9160883; DOI=10.1038/sj.onc.1201039;
RA   Chen J., Carey K., Godowski P.J.;
RT   "Identification of Gas6 as a ligand for Mer, a neural cell adhesion
RT   molecule related receptor tyrosine kinase implicated in cellular
RT   transformation.";
RL   Oncogene 14:2033-2039(1997).
RN   [7]
RP   INTERACTION WITH VAV1.
RX   PubMed=12920122; DOI=10.1074/jbc.M305817200;
RA   Mahajan N.P., Earp H.S.;
RT   "An SH2 domain-dependent, phosphotyrosine-independent interaction
RT   between Vav1 and the Mer receptor tyrosine kinase: a mechanism for
RT   localizing guanine nucleotide-exchange factor action.";
RL   J. Biol. Chem. 278:42596-42603(2003).
RN   [8]
RP   INTERACTION WITH TNK2.
RX   PubMed=16288044; DOI=10.1158/0008-5472.CAN-05-1127;
RA   Mahajan N.P., Whang Y.E., Mohler J.L., Earp H.S.;
RT   "Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role
RT   of Ack1 in polyubiquitination of tumor suppressor Wwox.";
RL   Cancer Res. 65:10514-10523(2005).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-442.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [10]
RP   REVIEW ON FUNCTION.
RX   PubMed=16737840; DOI=10.1016/j.cytogfr.2006.04.004;
RA   Hafizi S., Dahlback B.;
RT   "Signalling and functional diversity within the Axl subfamily of
RT   receptor tyrosine kinases.";
RL   Cytokine Growth Factor Rev. 17:295-304(2006).
RN   [11]
RP   FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
RX   PubMed=17005688; DOI=10.1128/JVI.01157-06;
RA   Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K.,
RA   Irimura T., Jones S., Feldmann H., Kawaoka Y.;
RT   "Tyro3 family-mediated cell entry of Ebola and Marburg viruses.";
RL   J. Virol. 80:10109-10116(2006).
RN   [12]
RP   REVIEW ON FUNCTION.
RX   PubMed=18421305; DOI=10.1038/nri2303;
RA   Lemke G., Rothlin C.V.;
RT   "Immunobiology of the TAM receptors.";
RL   Nat. Rev. Immunol. 8:327-336(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-935, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [14]
RP   INTERACTION WITH LGALS3.
RX   PubMed=21792939; DOI=10.1002/jcp.22955;
RA   Caberoy N.B., Alvarado G., Bigcas J.L., Li W.;
RT   "Galectin-3 is a new MerTK-specific eat-me signal.";
RL   J. Cell. Physiol. 227:401-407(2012).
RN   [15]
RP   STRUCTURE BY NMR OF 366-483.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structures of the FN3 domain of human proto-oncogene
RT   tyrosine-protein kinase MER precursor.";
RL   Submitted (DEC-2006) to the PDB data bank.
RN   [16]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-20; ASN-118; MET-185; THR-282;
RP   LYS-289; HIS-293; GLY-446; LEU-452; LYS-466; SER-498; VAL-518;
RP   GLU-662; SER-708; GLN-823; TRP-865 AND ILE-870.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [17]
RP   VARIANTS VAL-214 AND LEU-958.
RX   PubMed=21602930; DOI=10.1371/journal.pone.0019458;
RA   Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q.,
RA   Hejtmancik J.F.;
RT   "Detection of variants in 15 genes in 87 unrelated Chinese patients
RT   with Leber congenital amaurosis.";
RL   PLoS ONE 6:E19458-E19458(2011).
CC   -!- FUNCTION: Receptor tyrosine kinase that transduces signals from
CC       the extracellular matrix into the cytoplasm by binding to several
CC       ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many
CC       physiological processes including cell survival, migration,
CC       differentiation, and phagocytosis of apoptotic cells
CC       (efferocytosis). Ligand binding at the cell surface induces
CC       autophosphorylation of MERTK on its intracellular domain that
CC       provides docking sites for downstream signaling molecules.
CC       Following activation by ligand, interacts with GRB2 or PLCG2 and
CC       induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK
CC       signaling plays a role in various processes such as macrophage
CC       clearance of apoptotic cells, platelet aggregation, cytoskeleton
CC       reorganization and engulfment. Functions in the retinal pigment
CC       epithelium (RPE) as a regulator of rod outer segments fragments
CC       phagocytosis. Plays also an important role in inhibition of Toll-
CC       like receptors (TLRs)-mediated innate immune response by
CC       activating STAT1, which selectively induces production of
CC       suppressors of cytokine signaling SOCS1 and SOCS3.
CC       {ECO:0000269|PubMed:17005688}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
CC   -!- SUBUNIT: Interacts (upon activation) with TNK2; stimulates TNK2
CC       autophosphorylation. Interacts (via N-terminus) with extracellular
CC       ligands LGALS3, TUB, TULP1 and GAS6 (By similarity). Interacts
CC       with VAV1 in a phosphotyrosine-independent manner. {ECO:0000250,
CC       ECO:0000269|PubMed:12920122, ECO:0000269|PubMed:16288044,
CC       ECO:0000269|PubMed:21792939, ECO:0000269|PubMed:9160883}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Not expressed in normal B- and T-lymphocytes
CC       but is expressed in numerous neoplastic B- and T-cell lines.
CC       Highly expressed in testis, ovary, prostate, lung, and kidney,
CC       with lower expression in spleen, small intestine, colon, and
CC       liver.
CC   -!- PTM: Autophosphorylated on Tyr-749, Tyr-753 and Tyr-754 in the
CC       activation loop allowing full activity. Autophosphorylated on Tyr-
CC       872 leading to recruitment of downstream partners of the signaling
CC       cascade such as PLCG2 (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Retinitis pigmentosa 38 (RP38) [MIM:613862]: A retinal
CC       dystrophy belonging to the group of pigmentary retinopathies.
CC       Retinitis pigmentosa is characterized by retinal pigment deposits
CC       visible on fundus examination and primary loss of rod
CC       photoreceptor cells followed by secondary loss of cone
CC       photoreceptors. Patients typically have night vision blindness and
CC       loss of midperipheral visual field. As their condition progresses,
CC       they lose their far peripheral visual field and eventually central
CC       vision as well. {ECO:0000269|PubMed:11062461}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org//Genes/MERTKID41339ch2q13.html";
CC   -!- WEB RESOURCE: Name=Mutations of the MERTK gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="http://www.retina-international.org/files/sci-news/mertkmut.htm";
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DR   EMBL; U08023; AAB60430.1; -; mRNA.
DR   EMBL; AH010001; AAG33129.1; -; Genomic_DNA.
DR   EMBL; AC093675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS2094.1; -.
DR   PIR; I38547; I38547.
DR   RefSeq; NP_006334.2; NM_006343.2.
DR   UniGene; Hs.306178; -.
DR   PDB; 2DBJ; NMR; -; A=373-483.
DR   PDB; 2P0C; X-ray; 2.40 A; A/B=570-864.
DR   PDB; 3BPR; X-ray; 2.80 A; A/B/C/D=570-864.
DR   PDB; 3BRB; X-ray; 1.90 A; A/B=570-864.
DR   PDB; 3TCP; X-ray; 2.69 A; A/B=570-864.
DR   PDB; 4M3Q; X-ray; 2.72 A; A/B=570-864.
DR   PDB; 4MH7; X-ray; 2.51 A; A/B=570-864.
DR   PDB; 4MHA; X-ray; 2.59 A; A/B=570-864.
DR   PDBsum; 2DBJ; -.
DR   PDBsum; 2P0C; -.
DR   PDBsum; 3BPR; -.
DR   PDBsum; 3BRB; -.
DR   PDBsum; 3TCP; -.
DR   PDBsum; 4M3Q; -.
DR   PDBsum; 4MH7; -.
DR   PDBsum; 4MHA; -.
DR   ProteinModelPortal; Q12866; -.
DR   SMR; Q12866; 103-281, 283-492, 575-900.
DR   BioGrid; 115724; 8.
DR   IntAct; Q12866; 4.
DR   STRING; 9606.ENSP00000295408; -.
DR   BindingDB; Q12866; -.
DR   ChEMBL; CHEMBL3137284; -.
DR   GuidetoPHARMACOLOGY; 1837; -.
DR   MEROPS; I43.001; -.
DR   PhosphoSite; Q12866; -.
DR   DMDM; 160332297; -.
DR   MaxQB; Q12866; -.
DR   PaxDb; Q12866; -.
DR   PRIDE; Q12866; -.
DR   Ensembl; ENST00000295408; ENSP00000295408; ENSG00000153208.
DR   Ensembl; ENST00000421804; ENSP00000389152; ENSG00000153208.
DR   GeneID; 10461; -.
DR   KEGG; hsa:10461; -.
DR   UCSC; uc002thk.1; human.
DR   CTD; 10461; -.
DR   GeneCards; GC02P112656; -.
DR   GeneReviews; MERTK; -.
DR   H-InvDB; HIX0002374; -.
DR   HGNC; HGNC:7027; MERTK.
DR   HPA; HPA036196; -.
DR   MIM; 604705; gene.
DR   MIM; 613862; phenotype.
DR   neXtProt; NX_Q12866; -.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA30759; -.
DR   eggNOG; COG0515; -.
DR   GeneTree; ENSGT00760000119065; -.
DR   HOGENOM; HOG000231685; -.
DR   HOVERGEN; HBG006346; -.
DR   InParanoid; Q12866; -.
DR   KO; K05117; -.
DR   OMA; NEIGWSA; -.
DR   OrthoDB; EOG77DJ5C; -.
DR   PhylomeDB; Q12866; -.
DR   TreeFam; TF317402; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   Reactome; REACT_12051; Cell surface interactions at the vascular wall.
DR   SignaLink; Q12866; -.
DR   ChiTaRS; MERTK; human.
DR   EvolutionaryTrace; Q12866; -.
DR   GeneWiki; MERTK; -.
DR   GenomeRNAi; 10461; -.
DR   NextBio; 39667; -.
DR   PRO; PR:Q12866; -.
DR   Bgee; Q12866; -.
DR   CleanEx; HS_MERTK; -.
DR   ExpressionAtlas; Q12866; baseline and differential.
DR   Genevestigator; Q12866; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0016028; C:rhabdomere; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
DR   GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Ensembl.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; TAS:GOC.
DR   GO; GO:0006909; P:phagocytosis; IMP:BHF-UCL.
DR   GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0032940; P:secretion by cell; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Disease mutation;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene;
KW   Receptor; Reference proteome; Repeat; Retinitis pigmentosa; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    999       Tyrosine-protein kinase Mer.
FT                                /FTId=PRO_0000024443.
FT   TOPO_DOM     21    505       Extracellular. {ECO:0000255}.
FT   TRANSMEM    506    526       Helical. {ECO:0000255}.
FT   TOPO_DOM    527    999       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       81    186       Ig-like C2-type 1.
FT   DOMAIN      197    273       Ig-like C2-type 2.
FT   DOMAIN      286    381       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      386    484       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      587    858       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     593    601       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    723    723       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING     615    615       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     543    543       Phosphoserine.
FT                                {ECO:0000269|PubMed:19369195}.
FT   MOD_RES     749    749       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:8702477}.
FT   MOD_RES     753    753       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:8702477}.
FT   MOD_RES     754    754       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:8702477}.
FT   MOD_RES     872    872       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     935    935       Phosphoserine.
FT                                {ECO:0000269|PubMed:19369195}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    170    170       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    234    234       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    294    294       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    316    316       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    329    329       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    336    336       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    354    354       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    389    389       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    395    395       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    442    442       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    454    454       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    115    175       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    218    262       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VARIANT      20     20       R -> S (in dbSNP:rs35898499).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021039.
FT   VARIANT     118    118       S -> N (in dbSNP:rs13027171).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:8086340}.
FT                                /FTId=VAR_021040.
FT   VARIANT     185    185       V -> M (in dbSNP:rs56205303).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041741.
FT   VARIANT     214    214       F -> V (found in a patient with Leber
FT                                congenital amaurosis).
FT                                {ECO:0000269|PubMed:21602930}.
FT                                /FTId=VAR_067194.
FT   VARIANT     282    282       A -> T (in dbSNP:rs7588635).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021041.
FT   VARIANT     289    289       E -> K. {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041742.
FT   VARIANT     293    293       R -> H (in dbSNP:rs34072093).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021042.
FT   VARIANT     329    329       N -> S (in dbSNP:rs34943572).
FT                                /FTId=VAR_051698.
FT   VARIANT     446    446       A -> G (in a renal clear cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041743.
FT   VARIANT     452    452       V -> L (in dbSNP:rs34010621).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041744.
FT   VARIANT     466    466       R -> K (in dbSNP:rs7604639).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021043.
FT   VARIANT     498    498       N -> S (in dbSNP:rs35858762).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021044.
FT   VARIANT     518    518       I -> V (in dbSNP:rs2230515).
FT                                {ECO:0000269|PubMed:11062461,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_021045.
FT   VARIANT     540    540       E -> K (in RP38; dbSNP:rs113485015).
FT                                {ECO:0000269|PubMed:11062461}.
FT                                /FTId=VAR_021046.
FT   VARIANT     661    661       S -> C (in RP38).
FT                                {ECO:0000269|PubMed:11062461}.
FT                                /FTId=VAR_021047.
FT   VARIANT     662    662       Q -> E (in dbSNP:rs56209758).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041745.
FT   VARIANT     708    708       A -> S (in a head & Neck squamous cell
FT                                carcinoma sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041746.
FT   VARIANT     823    823       E -> Q (in dbSNP:rs55924349).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041747.
FT   VARIANT     865    865       R -> W (in dbSNP:rs2230516).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_020285.
FT   VARIANT     870    870       V -> I (in dbSNP:rs2230517).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_029237.
FT   VARIANT     871    871       I -> T (in RP38).
FT                                {ECO:0000269|PubMed:11062461}.
FT                                /FTId=VAR_021048.
FT   VARIANT     871    871       I -> V. {ECO:0000269|PubMed:11062461}.
FT                                /FTId=VAR_021049.
FT   VARIANT     958    958       P -> L (found in a patient with Leber
FT                                congenital amaurosis; dbSNP:rs201460398).
FT                                {ECO:0000269|PubMed:21602930}.
FT                                /FTId=VAR_067195.
FT   CONFLICT    140    140       A -> G (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    143    143       A -> R (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       S -> G (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    274    274       K -> Q (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       S -> G (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    628    628       Q -> H (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    794    794       A -> R (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   CONFLICT    888    888       S -> P (in Ref. 1; AAB60430).
FT                                {ECO:0000305}.
FT   STRAND      388    394
FT   STRAND      396    406
FT   STRAND      417    428
FT   STRAND      431    441
FT   STRAND      446    449
FT   STRAND      453    459
FT   STRAND      461    467
FT   STRAND      476    479
FT   TURN        577    580
FT   HELIX       584    586
FT   STRAND      587    594
FT   STRAND      601    607
FT   STRAND      613    620
FT   HELIX       628    642
FT   STRAND      654    657
FT   STRAND      667    672
FT   HELIX       679    685
FT   STRAND      688    692
FT   HELIX       697    715
FT   TURN        716    718
FT   HELIX       726    728
FT   STRAND      729    731
FT   STRAND      737    739
FT   HELIX       764    766
FT   HELIX       769    773
FT   HELIX       779    794
FT   HELIX       806    808
FT   HELIX       809    814
FT   STRAND      822    824
FT   HELIX       827    835
FT   HELIX       841    843
FT   HELIX       847    860
SQ   SEQUENCE   999 AA;  110249 MW;  05BC339F05DFD355 CRC64;
     MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL LSLPHASGYQ
     PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV GHIILSEHKG VKFNCSISVP
     NIYQDTTISW WKDGKELLGA HHAITQFYPD DEVTAIIASF SITSVQRSDN GSYICKMKIN
     NEEIVSDPIY IEVQGLPHFT KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE
     QPEKSPSVLT VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI
     LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ ALANYSIGVS
     CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN VDIRWMKPPT KQQDGELVGY
     RISHVWQSAG ISKELLEEVG QNGSRARISV QVHNATCTVR IAAVTRGGVG PFSDPVKIFI
     PAHGWVDYAP SSTPAPGNAD PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE
     EDSELVVNYI AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS
     VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI RLLGVCIEMS
     SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL LKFMVDIALG MEYLSNRNFL
     HRDLAARNCM LRDDMTVCVA DFGLSKKIYS GDYYRQGRIA KMPVKWIAIE SLADRVYTSK
     SDVWAFGVTM WEIATRGMTP YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD
     PLDRPTFSVL RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD
     SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT AEKNSVLPGE
     RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM
//
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