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-MAY-2013, entry version 151.
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 AUTOPHOSPHORYLATION 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, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
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.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (By similarity).
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).
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. Note=The disease is caused by mutations affecting
CC the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. AXL/UFO subfamily.
CC -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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 IPI; IPI00029756; -.
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=574-864.
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 PDBsum; 2DBJ; -.
DR PDBsum; 2P0C; -.
DR PDBsum; 3BPR; -.
DR PDBsum; 3BRB; -.
DR PDBsum; 3TCP; -.
DR ProteinModelPortal; Q12866; -.
DR IntAct; Q12866; 3.
DR STRING; 9606.ENSP00000295408; -.
DR MEROPS; I43.001; -.
DR PhosphoSite; Q12866; -.
DR DMDM; 160332297; -.
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 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 HOGENOM; HOG000231685; -.
DR HOVERGEN; HBG006346; -.
DR InParanoid; Q12866; -.
DR KO; K05117; -.
DR OMA; TGPKHIP; -.
DR OrthoDB; EOG4Z8XW3; -.
DR PhylomeDB; Q12866; -.
DR BRENDA; 2.7.10.1; 2681.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; Q12866; -.
DR BindingDB; Q12866; -.
DR ChEMBL; CHEMBL5331; -.
DR ChiTaRS; MERTK; human.
DR EvolutionaryTrace; Q12866; -.
DR GenomeRNAi; 10461; -.
DR NextBio; 39667; -.
DR ArrayExpress; Q12866; -.
DR Bgee; Q12866; -.
DR CleanEx; HS_MERTK; -.
DR Genevestigator; Q12866; -.
DR GermOnline; ENSG00000153208; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Compara.
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:Compara.
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:Compara.
DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Compara.
DR GO; GO:0006909; P:phagocytosis; IMP:BHF-UCL.
DR GO; GO:0030168; P:platelet activation; IEA:Compara.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling cascade; IEA:Compara.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Compara.
DR GO; GO:0032940; P:secretion by cell; IEA:Compara.
DR GO; GO:0007283; P:spermatogenesis; IEA:Compara.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Compara.
DR GO; GO:0060068; P:vagina development; IEA:Compara.
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_cat_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; FN_III-like; 2.
DR SUPFAM; SSF56112; Kinase_like; 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 Potential.
FT CHAIN 21 999 Tyrosine-protein kinase Mer.
FT /FTId=PRO_0000024443.
FT TOPO_DOM 21 505 Extracellular (Potential).
FT TRANSMEM 506 526 Helical; (Potential).
FT TOPO_DOM 527 999 Cytoplasmic (Potential).
FT DOMAIN 81 186 Ig-like C2-type 1.
FT DOMAIN 197 273 Ig-like C2-type 2.
FT DOMAIN 284 379 Fibronectin type-III 1.
FT DOMAIN 383 482 Fibronectin type-III 2.
FT DOMAIN 587 858 Protein kinase.
FT NP_BIND 593 601 ATP (By similarity).
FT ACT_SITE 723 723 Proton acceptor (By similarity).
FT BINDING 615 615 ATP (By similarity).
FT MOD_RES 543 543 Phosphoserine.
FT MOD_RES 749 749 Phosphotyrosine; by autocatalysis.
FT MOD_RES 753 753 Phosphotyrosine; by autocatalysis.
FT MOD_RES 754 754 Phosphotyrosine; by autocatalysis.
FT MOD_RES 872 872 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 935 935 Phosphoserine.
FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 170 170 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 207 207 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 215 215 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 234 234 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 294 294 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 329 329 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 336 336 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 354 354 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 389 389 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 395 395 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 442 442 N-linked (GlcNAc...).
FT CARBOHYD 454 454 N-linked (GlcNAc...) (Potential).
FT DISULFID 115 175 By similarity.
FT DISULFID 218 262 By similarity.
FT VARIANT 20 20 R -> S (in dbSNP:rs35898499).
FT /FTId=VAR_021039.
FT VARIANT 118 118 S -> N (in dbSNP:rs13027171).
FT /FTId=VAR_021040.
FT VARIANT 185 185 V -> M (in dbSNP:rs56205303).
FT /FTId=VAR_041741.
FT VARIANT 214 214 F -> V (found in a patient with Leber
FT congenital amaurosis).
FT /FTId=VAR_067194.
FT VARIANT 282 282 A -> T (in dbSNP:rs7588635).
FT /FTId=VAR_021041.
FT VARIANT 289 289 E -> K.
FT /FTId=VAR_041742.
FT VARIANT 293 293 R -> H (in dbSNP:rs34072093).
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 /FTId=VAR_041743.
FT VARIANT 452 452 V -> L (in dbSNP:rs34010621).
FT /FTId=VAR_041744.
FT VARIANT 466 466 R -> K (in dbSNP:rs7604639).
FT /FTId=VAR_021043.
FT VARIANT 498 498 N -> S (in dbSNP:rs35858762).
FT /FTId=VAR_021044.
FT VARIANT 518 518 I -> V (in dbSNP:rs2230515).
FT /FTId=VAR_021045.
FT VARIANT 540 540 E -> K (in RP38).
FT /FTId=VAR_021046.
FT VARIANT 661 661 S -> C (in RP38).
FT /FTId=VAR_021047.
FT VARIANT 662 662 Q -> E (in dbSNP:rs56209758).
FT /FTId=VAR_041745.
FT VARIANT 708 708 A -> S (in a head & Neck squamous cell
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_041746.
FT VARIANT 823 823 E -> Q (in dbSNP:rs55924349).
FT /FTId=VAR_041747.
FT VARIANT 865 865 R -> W (in dbSNP:rs2230516).
FT /FTId=VAR_020285.
FT VARIANT 870 870 V -> I (in dbSNP:rs2230517).
FT /FTId=VAR_029237.
FT VARIANT 871 871 I -> T (in RP38).
FT /FTId=VAR_021048.
FT VARIANT 871 871 I -> V.
FT /FTId=VAR_021049.
FT VARIANT 958 958 P -> L (found in a patient with Leber
FT congenital amaurosis).
FT /FTId=VAR_067195.
FT CONFLICT 140 140 A -> G (in Ref. 1; AAB60430).
FT CONFLICT 143 143 A -> R (in Ref. 1; AAB60430).
FT CONFLICT 247 247 S -> G (in Ref. 1; AAB60430).
FT CONFLICT 274 274 K -> Q (in Ref. 1; AAB60430).
FT CONFLICT 328 328 S -> G (in Ref. 1; AAB60430).
FT CONFLICT 628 628 Q -> H (in Ref. 1; AAB60430).
FT CONFLICT 794 794 A -> R (in Ref. 1; AAB60430).
FT CONFLICT 888 888 S -> P (in Ref. 1; AAB60430).
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 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
//
