ID UFO_HUMAN Reviewed; 894 AA. AC P30530; Q8N5L2; Q9UD27; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 4. DT 27-MAR-2024, entry version 233. DE RecName: Full=Tyrosine-protein kinase receptor UFO; DE EC=2.7.10.1 {ECO:0000269|PubMed:28076778}; DE AltName: Full=AXL oncogene; DE Flags: Precursor; GN Name=AXL; Synonyms=UFO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2247464; DOI=10.1073/pnas.87.22.8913; RA Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.; RT "Putative tyrosine kinases expressed in K-562 human leukemia cells."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND ROLE IN MYELOID LEUKEMIA. RC TISSUE=Fibroblast; RX PubMed=1656220; DOI=10.1128/mcb.11.10.5016-5031.1991; RA O'Bryan J.P., Frye R.A., Cogswell P.C., Neubauer A., Kitch B., Prokop C., RA Espinosa R., le Beau M.M., Earp H., Liu E.T.; RT "AXL, a transforming gene isolated from primary human myeloid leukemia RT cells, encodes a novel receptor tyrosine kinase."; RL Mol. Cell. Biol. 11:5016-5031(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). RX PubMed=1834974; RA Janssen J.W.G., Schulz A.S., Steenvoorden A.C.M., Schmidberger M., RA Strehl S., Ambros P., Bartram C.R.; RT "A novel putative tyrosine kinase receptor with oncogenic potential."; RL Oncogene 6:2113-2120(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 674-730. RX PubMed=8247543; RA Lee S.-T., Strunk K.M., Spritz R.A.; RT "A survey of protein tyrosine kinase mRNAs expressed in normal human RT melanocytes."; RL Oncogene 8:3403-3410(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 677-730, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Colon tumor; RX PubMed=7896447; DOI=10.1002/ijc.2910600611; RA Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., RA Varnum B., Liu E.T., Cance W.G.; RT "Receptor tyrosine kinases expressed in metastatic colon cancer."; RL Int. J. Cancer 60:791-797(1995). RN [8] RP INTERACTION WITH LIGAND GAS6. RX PubMed=7854420; DOI=10.1038/373623a0; RA Varnum B.C., Young C., Elliott G., Garcia A., Bartley T.D., Fridell Y.W., RA Hunt R.W., Trail G., Clogston C., Toso R.J., Yanagihara D., Bennett L., RA Silber M., Merewether L.A., Tseng A., Escobar E., Liu E.T., Yamane H.K.; RT "Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein RT encoded by growth-arrest-specific gene 6."; RL Nature 373:623-626(1995). RN [9] RP INTERACTION WITH GAS6, AND ACTIVITY REGULATION. RX PubMed=8621659; DOI=10.1074/jbc.271.16.9785; RA Mark M.R., Chen J., Hammonds R.G., Sadick M., Godowski P.J.; RT "Characterization of Gas6, a member of the superfamily of G domain- RT containing proteins, as a ligand for Rse and Axl."; RL J. Biol. Chem. 271:9785-9789(1996). RN [10] RP PHOSPHORYLATION AT TYR-779; TYR-821 AND TYR-866, AND INTERACTION WITH GRB2; RP LCK; PIK3R1; PIK3R2 AND PLCG1. RX PubMed=9178760; DOI=10.1038/sj.onc.1201123; RA Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., RA Ullrich A., Bartram C.R., Janssen J.W.; RT "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is RT mediated mainly by a multi-substrate docking-site."; RL Oncogene 14:2619-2631(1997). RN [11] RP ROLE IN PROSTATIC CARCINOMA. RX PubMed=10403904; DOI=10.1046/j.1525-1500.1999.99034.x; RA Jacob A.N., Kalapurakal J., Davidson W.R., Kandpal G., Dunson N., RA Prashar Y., Kandpal R.P.; RT "A receptor tyrosine kinase, UFO/Axl, and other genes isolated by a RT modified differential display PCR are overexpressed in metastatic prostatic RT carcinoma cell line DU145."; RL Cancer Detect. Prev. 23:325-332(1999). RN [12] RP ROLE IN BREAST CANCER. RX PubMed=11484958; DOI=10.1023/a:1011126330233; RA Berclaz G., Altermatt H.J., Rohrbach V., Kieffer I., Dreher E., RA Andres A.C.; RT "Estrogen dependent expression of the receptor tyrosine kinase axl in RT normal and malignant human breast."; RL Ann. Oncol. 12:819-824(2001). RN [13] RP INTERACTION WITH NCK2; PIK3R3; SOCS1 AND TNS2. RX PubMed=12470648; DOI=10.1016/s0006-291x(02)02718-3; RA Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.; RT "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 RT domain-containing protein with homology to tensin."; RL Biochem. Biophys. Res. Commun. 299:793-800(2002). RN [14] RP FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY. RX PubMed=12364394; DOI=10.1161/01.res.0000036753.50601.e9; RA D'Arcangelo D., Gaetano C., Capogrossi M.C.; RT "Acidification prevents endothelial cell apoptosis by Axl activation."; RL Circ. Res. 91:E4-12(2002). RN [15] RP ROLE IN THYROID CARCINOMAS. RX PubMed=12490074; DOI=10.1089/105072502320908303; RA Ito M., Nakashima M., Nakayama T., Ohtsuru A., Nagayama Y., Takamura N., RA Demedchik E.P., Sekine I., Yamashita S.; RT "Expression of receptor-type tyrosine kinase, Axl, and its ligand, Gas6, in RT pediatric thyroid carcinomas around Chernobyl."; RL Thyroid 12:971-975(2002). RN [16] RP INTERACTION WITH CBL AND GAS6, AND UBIQUITINATION. RX PubMed=15958209; DOI=10.1016/j.bbrc.2005.05.086; RA Valverde P.; RT "Effects of Gas6 and hydrogen peroxide in Axl ubiquitination and RT downregulation."; RL Biochem. Biophys. Res. Commun. 333:180-185(2005). RN [17] RP ACTIVITY REGULATION, AND FUNCTION. RX PubMed=15507525; DOI=10.1182/blood-2004-04-1469; RA Gallicchio M., Mitola S., Valdembri D., Fantozzi R., Varnum B., RA Avanzi G.C., Bussolino F.; RT "Inhibition of vascular endothelial growth factor receptor 2-mediated RT endothelial cell activation by Axl tyrosine kinase receptor."; RL Blood 105:1970-1976(2005). RN [18] RP FUNCTION IN PLATELET ACTIVATION AND THROMBOTIC RESPONSE REGULATION. RX PubMed=15733062; DOI=10.1111/j.1538-7836.2005.01186.x; RA Gould W.R., Baxi S.M., Schroeder R., Peng Y.W., Leadley R.J., RA Peterson J.T., Perrin L.A.; RT "Gas6 receptors Axl, Sky and Mer enhance platelet activation and regulate RT thrombotic responses."; RL J. Thromb. Haemost. 3:733-741(2005). RN [19] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=17005688; DOI=10.1128/jvi.01157-06; RA Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T., RA 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 [20] RP INTERACTION WITH GRB2; PIK3R1 AND PIK3R2, AND PHOSPHORYLATION AT TYR-779; RP TYR-821 AND TYR-866. RX PubMed=18346204; DOI=10.1111/j.1471-4159.2008.05343.x; RA Weinger J.G., Gohari P., Yan Y., Backer J.M., Varnum B., Shafit-Zagardo B.; RT "In brain, Axl recruits Grb2 and the p85 regulatory subunit of PI3 kinase; RT in vitro mutagenesis defines the requisite binding sites for downstream Akt RT activation."; RL J. Neurochem. 106:134-146(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [22] RP FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY. RX PubMed=18840707; DOI=10.1182/blood-2008-05-157073; RA Park I.K., Giovenzana C., Hughes T.L., Yu J., Trotta R., Caligiuri M.A.; RT "The Axl/Gas6 pathway is required for optimal cytokine signaling during RT human natural killer cell development."; RL Blood 113:2470-2477(2009). RN [23] RP INTERACTION WITH GRB2 AND TNK2. RX PubMed=19815557; DOI=10.1074/jbc.m109.072660; RA Pao-Chun L., Chan P.M., Chan W., Manser E.; RT "Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is RT mediated by Grb2: an analysis of ACK1 effects on Axl signaling."; RL J. Biol. Chem. 284:34954-34963(2009). RN [24] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=21501828; DOI=10.1016/j.chom.2011.03.012; RA Morizono K., Xie Y., Olafsen T., Lee B., Dasgupta A., Wu A.M., Chen I.S.; RT "The soluble serum protein Gas6 bridges virion envelope phosphatidylserine RT to the TAM receptor tyrosine kinase Axl to mediate viral entry."; RL Cell Host Microbe 9:286-298(2011). RN [25] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=22156524; DOI=10.1128/jvi.06451-11; RA Shimojima M., Stroher U., Ebihara H., Feldmann H., Kawaoka Y.; RT "Identification of cell surface molecules involved in dystroglycan- RT independent Lassa virus cell entry."; RL J. Virol. 86:2067-2078(2012). RN [26] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=22673088; DOI=10.1292/jvms.12-0176; RA Shimojima M., Kawaoka Y.; RT "Cell surface molecules involved in infection mediated by lymphocytic RT choriomeningitis virus glycoprotein."; RL J. Vet. Med. Sci. 74:1363-1366(2012). RN [27] RP FUNCTION (MICROBIAL INFECTION), AND REVIEW. RX PubMed=25277499; DOI=10.1016/j.virol.2014.09.009; RA Moller-Tank S., Maury W.; RT "Phosphatidylserine receptors: enhancers of enveloped virus entry and RT infection."; RL Virology 468:565-580(2014). RN [28] RP FUNCTION (MICROBIAL INFECTION), MUTAGENESIS OF LYS-567, CATALYTIC ACTIVITY, RP AND SUBCELLULAR LOCATION. RX PubMed=28076778; DOI=10.1016/j.celrep.2016.12.045; RA Meertens L., Labeau A., Dejarnac O., Cipriani S., Sinigaglia L., RA Bonnet-Madin L., Le Charpentier T., Hafirassou M.L., Zamborlini A., RA Cao-Lormeau V.M., Coulpier M., Misse D., Jouvenet N., Tabibiazar R., RA Gressens P., Schwartz O., Amara A.; RT "Axl Mediates ZIKA Virus Entry in Human Glial Cells and Modulates Innate RT Immune Responses."; RL Cell Rep. 18:324-333(2017). RN [29] RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=29379210; DOI=10.1038/s41564-017-0092-4; RA Chen J., Yang Y.F., Yang Y., Zou P., Chen J., He Y., Shui S.L., Cui Y.R., RA Bai R., Liang Y.J., Hu Y., Jiang B., Lu L., Zhang X., Liu J., Xu J.; RT "AXL promotes Zika virus infection in astrocytes by antagonizing type I RT interferon signalling."; RL Nat. Microbiol. 3:302-309(2018). RN [30] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=31311882; DOI=10.1128/mbio.01372-19; RA Strange D.P., Jiyarom B., Pourhabibi Zarandi N., Xie X., Baker C., RA Sadri-Ardekani H., Shi P.Y., Verma S.; RT "Axl Promotes Zika Virus Entry and Modulates the Antiviral State of Human RT Sertoli Cells."; RL MBio 10:0-0(2019). RN [31] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-227 IN COMPLEX WITH GAS6, RP MUTAGENESIS OF GLU-63; GLU-66 AND THR-84, AND SUBUNIT. RX PubMed=16362042; DOI=10.1038/sj.emboj.7600912; RA Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Goehring W., Ullrich A., RA Timpl R., Hohenester E.; RT "Structural basis for Gas6-Axl signalling."; RL EMBO J. 25:80-87(2006). RN [32] RP VARIANTS [LARGE SCALE ANALYSIS] MET-112; TRP-295; CYS-499 AND GLY-515. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the CC extracellular matrix into the cytoplasm by binding growth factor GAS6 CC and which is thus regulating many physiological processes including CC cell survival, cell proliferation, migration and differentiation. CC Ligand binding at the cell surface induces dimerization and CC autophosphorylation of AXL. Following activation by ligand, AXL binds CC and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, CC PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other CC downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. CC Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory CC subunits by AXL leads to the downstream activation of the AKT kinase. CC GAS6/AXL signaling plays a role in various processes such as CC endothelial cell survival during acidification by preventing apoptosis, CC optimal cytokine signaling during human natural killer cell CC development, hepatic regeneration, gonadotropin-releasing hormone CC neuron survival and migration, platelet activation, or regulation of CC thrombotic responses. Also plays an important role in inhibition of CC Toll-like receptors (TLRs)-mediated innate immune response. CC {ECO:0000269|PubMed:10403904, ECO:0000269|PubMed:11484958, CC ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:12490074, CC ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:15733062, CC ECO:0000269|PubMed:1656220, ECO:0000269|PubMed:18840707}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for lassa virus and CC lymphocytic choriomeningitis virus, possibly through GAS6 binding to CC phosphatidyl-serine at the surface of virion envelope. CC {ECO:0000269|PubMed:17005688, ECO:0000269|PubMed:21501828, CC ECO:0000269|PubMed:22156524, ECO:0000269|PubMed:25277499}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus, CC possibly through GAS6 binding to phosphatidyl-serine at the surface of CC virion envelope. {ECO:0000269|PubMed:22673088}. CC -!- FUNCTION: (Microbial infection) Promotes Zika virus entry in glial CC cells, Sertoli cells and astrocytes (PubMed:28076778, PubMed:29379210, CC PubMed:31311882). Additionally, Zika virus potentiates AXL kinase CC activity to antagonize type I interferon signaling and thereby promotes CC infection (PubMed:28076778). Interferon signaling inhibition occurs via CC an SOCS1-dependent mechanism (PubMed:29379210). CC {ECO:0000269|PubMed:28076778, ECO:0000269|PubMed:29379210, CC ECO:0000269|PubMed:31311882}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, CC ECO:0000269|PubMed:28076778}; CC -!- ACTIVITY REGULATION: Activated by GAS6-binding and subsequent CC autophosphorylation. {ECO:0000269|PubMed:15507525, CC ECO:0000269|PubMed:8621659}. CC -!- SUBUNIT: Heterodimer and heterotetramer with ligand GAS6. Interacts CC with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1 and CC TNS2. Part of a complex including AXL, TNK2 and GRB2, in which GRB2 CC promotes AXL recruitment by TNK2. {ECO:0000269|PubMed:12470648, CC ECO:0000269|PubMed:15958209, ECO:0000269|PubMed:16362042, CC ECO:0000269|PubMed:18346204, ECO:0000269|PubMed:19815557, CC ECO:0000269|PubMed:7854420, ECO:0000269|PubMed:8621659, CC ECO:0000269|PubMed:9178760}. CC -!- INTERACTION: CC P30530; P00533: EGFR; NbExp=4; IntAct=EBI-2850927, EBI-297353; CC P30530; P29317: EPHA2; NbExp=2; IntAct=EBI-2850927, EBI-702104; CC P30530; Q14393-2: GAS6; NbExp=8; IntAct=EBI-2850927, EBI-21517417; CC P30530; P62993: GRB2; NbExp=4; IntAct=EBI-2850927, EBI-401755; CC P30530; P08238: HSP90AB1; NbExp=3; IntAct=EBI-2850927, EBI-352572; CC P30530; P27986: PIK3R1; NbExp=3; IntAct=EBI-2850927, EBI-79464; CC P30530; P0DTC2: S; Xeno; NbExp=9; IntAct=EBI-2850927, EBI-25474821; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28076778, CC ECO:0000269|PubMed:29379210, ECO:0000269|PubMed:7896447}; Single-pass CC type I membrane protein {ECO:0000269|PubMed:7896447}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P30530-1; Sequence=Displayed; CC Name=Short; CC IsoId=P30530-2; Sequence=VSP_005017; CC -!- TISSUE SPECIFICITY: Highly expressed in metastatic colon tumors. CC Expressed in primary colon tumors. Weakly expressed in normal colon CC tissue. {ECO:0000269|PubMed:7896447}. CC -!- PTM: Monoubiquitinated upon GAS6-binding. A very small proportion of CC the receptor could be subjected to polyubiquitination in a very CC transient fashion. {ECO:0000269|PubMed:15958209}. CC -!- PTM: Phosphorylated at tyrosine residues by autocatalysis, which CC activates kinase activity. {ECO:0000269|PubMed:18346204, CC ECO:0000269|PubMed:9178760}. CC -!- DISEASE: Note=AXL and its ligand GAS6 are highly expressed in thyroid CC carcinoma tissues, and might thus be involved in thyroid tumorigenesis. CC Overexpression of AXL and its ligand was also detected in many other CC cancers such as myeloproliferative disorders, prostatic carcinoma CC cells, or breast cancer. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/733/AXL"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M76125; AAA61243.1; -; mRNA. DR EMBL; S65125; AAB20305.1; -; mRNA. DR EMBL; X57019; CAA40338.1; -; mRNA. DR EMBL; AC011510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032229; AAH32229.1; -; mRNA. DR CCDS; CCDS12574.1; -. [P30530-2] DR CCDS; CCDS12575.1; -. [P30530-1] DR PIR; A41527; A41527. DR RefSeq; NP_001690.2; NM_001699.5. [P30530-2] DR RefSeq; NP_068713.2; NM_021913.4. [P30530-1] DR PDB; 2C5D; X-ray; 3.30 A; C/D=33-227. DR PDB; 4RA0; X-ray; 3.07 A; C/D=33-227. DR PDB; 5U6B; X-ray; 2.84 A; A/B/C/D=514-818. DR PDB; 5VXZ; X-ray; 2.30 A; C/D=34-135. DR PDBsum; 2C5D; -. DR PDBsum; 4RA0; -. DR PDBsum; 5U6B; -. DR PDBsum; 5VXZ; -. DR AlphaFoldDB; P30530; -. DR SMR; P30530; -. DR BioGRID; 107036; 399. DR CORUM; P30530; -. DR IntAct; P30530; 241. DR MINT; P30530; -. DR STRING; 9606.ENSP00000301178; -. DR BindingDB; P30530; -. DR ChEMBL; CHEMBL4895; -. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB12141; Gilteritinib. DR DrugCentral; P30530; -. DR GuidetoPHARMACOLOGY; 1835; -. DR GlyConnect; 1983; 12 N-Linked glycans (4 sites). DR GlyCosmos; P30530; 8 sites, 12 glycans. DR GlyGen; P30530; 9 sites, 9 N-linked glycans (3 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P30530; -. DR PhosphoSitePlus; P30530; -. DR BioMuta; AXL; -. DR DMDM; 239938818; -. DR CPTAC; CPTAC-1766; -. DR CPTAC; CPTAC-2791; -. DR EPD; P30530; -. DR jPOST; P30530; -. DR MassIVE; P30530; -. DR MaxQB; P30530; -. DR PaxDb; 9606-ENSP00000301178; -. DR PeptideAtlas; P30530; -. DR ProteomicsDB; 54712; -. [P30530-1] DR ProteomicsDB; 54713; -. [P30530-2] DR Pumba; P30530; -. DR ABCD; P30530; 23 sequenced antibodies. DR Antibodypedia; 30709; 1382 antibodies from 44 providers. DR CPTC; P30530; 2 antibodies. DR DNASU; 558; -. DR Ensembl; ENST00000301178.9; ENSP00000301178.3; ENSG00000167601.12. [P30530-1] DR Ensembl; ENST00000359092.7; ENSP00000351995.2; ENSG00000167601.12. [P30530-2] DR GeneID; 558; -. DR KEGG; hsa:558; -. DR MANE-Select; ENST00000301178.9; ENSP00000301178.3; NM_021913.5; NP_068713.2. DR UCSC; uc010ehj.5; human. [P30530-1] DR AGR; HGNC:905; -. DR CTD; 558; -. DR DisGeNET; 558; -. DR GeneCards; AXL; -. DR GeneReviews; AXL; -. DR HGNC; HGNC:905; AXL. DR HPA; ENSG00000167601; Low tissue specificity. DR MalaCards; AXL; -. DR MIM; 109135; gene. DR neXtProt; NX_P30530; -. DR OpenTargets; ENSG00000167601; -. DR PharmGKB; PA25197; -. DR VEuPathDB; HostDB:ENSG00000167601; -. DR eggNOG; ENOG502QQQ3; Eukaryota. DR GeneTree; ENSGT00940000160232; -. DR InParanoid; P30530; -. DR OMA; WTIMSTL; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P30530; -. DR TreeFam; TF317402; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; P30530; -. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR SignaLink; P30530; -. DR SIGNOR; P30530; -. DR BioGRID-ORCS; 558; 17 hits in 1198 CRISPR screens. DR ChiTaRS; AXL; human. DR EvolutionaryTrace; P30530; -. DR GeneWiki; AXL_receptor_tyrosine_kinase; -. DR GenomeRNAi; 558; -. DR Pharos; P30530; Tchem. DR PRO; PR:P30530; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P30530; Protein. DR Bgee; ENSG00000167601; Expressed in synovial joint and 206 other cell types or tissues. DR ExpressionAtlas; P30530; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0032036; F:myosin heavy chain binding; IEA:Ensembl. DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl. DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB. DR GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0001618; F:virus receptor activity; IDA:FlyBase. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl. DR GO; GO:0048469; P:cell maturation; IEP:UniProtKB. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB. DR GO; GO:0097028; P:dendritic cell differentiation; IEP:UniProtKB. DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0021885; P:forebrain cell migration; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0001779; P:natural killer cell differentiation; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central. DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:UniProtKB. DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Ensembl. DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl. DR GO; GO:0032689; P:negative regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0097350; P:neutrophil clearance; IEA:Ensembl. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0006909; P:phagocytosis; IDA:UniProtKB. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0030168; P:platelet activation; IBA:GO_Central. DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IDA:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central. DR GO; GO:0048549; P:positive regulation of pinocytosis; IMP:CACAO. DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:FlyBase. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0032940; P:secretion by cell; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0060068; P:vagina development; IEA:Ensembl. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0046718; P:viral entry into host cell; IMP:CACAO. DR CDD; cd00063; FN3; 2. DR CDD; cd20966; IgI_1_Axl_like; 1. DR CDD; cd05749; IgI_2_Axl_Tyro3_like; 1. DR CDD; cd05075; PTKc_Axl; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR011009; Kinase-like_dom_sf. 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 PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF323; TYROSINE-PROTEIN KINASE RECEPTOR UFO; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00060; FN3; 2. DR SMART; SM00409; IG; 2. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-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. DR Genevisible; P30530; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Differentiation; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Immunity; KW Immunoglobulin domain; Innate immunity; Kinase; Membrane; KW Nucleotide-binding; Oncogene; Phosphoprotein; Proto-oncogene; Receptor; KW Reference proteome; Repeat; Signal; Transferase; Transmembrane; KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..894 FT /note="Tyrosine-protein kinase receptor UFO" FT /id="PRO_0000024481" FT TOPO_DOM 26..451 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 452..472 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 473..894 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 27..128 FT /note="Ig-like C2-type 1" FT DOMAIN 139..222 FT /note="Ig-like C2-type 2" FT DOMAIN 227..331 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 336..428 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 536..807 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 26..92 FT /note="Interaction with GAS6" FT REGION 823..853 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 866..894 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 672 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 542..550 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 567 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 703 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 779 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:18346204, FT ECO:0000269|PubMed:9178760" FT MOD_RES 821 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:18346204, FT ECO:0000269|PubMed:9178760" FT MOD_RES 866 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:18346204, FT ECO:0000269|PubMed:9178760" FT MOD_RES 884 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 198 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 339 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 345 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 401 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 56..117 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 160..205 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 429..437 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:1656220" FT /id="VSP_005017" FT VARIANT 112 FT /note="T -> M (in dbSNP:rs35202236)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045596" FT VARIANT 266 FT /note="D -> N (in dbSNP:rs7249222)" FT /id="VAR_057990" FT VARIANT 295 FT /note="R -> W (in a lung neuroendocrine carcinoma sample; FT somatic mutation; dbSNP:rs751738506)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045597" FT VARIANT 499 FT /note="R -> C (in a gastric adenocarcinoma sample; somatic FT mutation; dbSNP:rs747576071)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041877" FT VARIANT 515 FT /note="S -> G (in dbSNP:rs1240393707)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041878" FT MUTAGEN 63 FT /note="E->R: Slightly reduced affinity for GAS6." FT /evidence="ECO:0000269|PubMed:16362042" FT MUTAGEN 66 FT /note="E->R: Reduced affinity for GAS6." FT /evidence="ECO:0000269|PubMed:16362042" FT MUTAGEN 84 FT /note="T->R: Reduced affinity for GAS6." FT /evidence="ECO:0000269|PubMed:16362042" FT MUTAGEN 567 FT /note="K->M: Catalytically inactive mutant." FT /evidence="ECO:0000269|PubMed:28076778" FT CONFLICT 303 FT /note="T -> P (in Ref. 3; AAB20305/CAA40338)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="E -> K (in Ref. 2; AAA61243)" FT /evidence="ECO:0000305" FT CONFLICT 430 FT /note="Q -> E (in Ref. 3; AAB20305/CAA40338)" FT /evidence="ECO:0000305" FT CONFLICT 639 FT /note="D -> G (in Ref. 3; AAB20305/CAA40338)" FT /evidence="ECO:0000305" FT CONFLICT 696 FT /note="K -> I (in Ref. 7; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 764 FT /note="Q -> R (in Ref. 5; AAH32229)" FT /evidence="ECO:0000305" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 52..63 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 94..106 FT /evidence="ECO:0007829|PDB:5VXZ" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:5VXZ" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 201..209 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:4RA0" FT STRAND 515..517 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 524..529 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 533..535 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 536..544 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 546..556 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 558..571 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 576..590 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 602..605 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 616..621 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 628..637 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 638..640 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 646..665 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 675..677 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 678..680 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 686..688 FT /evidence="ECO:0007829|PDB:5U6B" FT STRAND 698..700 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 713..715 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 718..723 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 728..743 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 755..763 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 776..785 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 790..792 FT /evidence="ECO:0007829|PDB:5U6B" FT HELIX 796..809 FT /evidence="ECO:0007829|PDB:5U6B" SQ SEQUENCE 894 AA; 98337 MW; 262D3659218E3202 CRC64; MAWRCPRMGR VPLAWCLALC GWACMAPRGT QAEESPFVGN PGNITGARGL TGTLRCQLQV QGEPPEVHWL RDGQILELAD STQTQVPLGE DEQDDWIVVS QLRITSLQLS DTGQYQCLVF LGHQTFVSQP GYVGLEGLPY FLEEPEDRTV AANTPFNLSC QAQGPPEPVD LLWLQDAVPL ATAPGHGPQR SLHVPGLNKT SSFSCEAHNA KGVTTSRTAT ITVLPQQPRN LHLVSRQPTE LEVAWTPGLS GIYPLTHCTL QAVLSDDGMG IQAGEPDPPE EPLTSQASVP PHQLRLGSLH PHTPYHIRVA CTSSQGPSSW THWLPVETPE GVPLGPPENI SATRNGSQAF VHWQEPRAPL QGTLLGYRLA YQGQDTPEVL MDIGLRQEVT LELQGDGSVS NLTVCVAAYT AAGDGPWSLP VPLEAWRPGQ AQPVHQLVKE PSTPAFSWPW WYVLLGAVVA AACVLILALF LVHRRKKETR YGEVFEPTVE RGELVVRYRV RKSYSRRTTE ATLNSLGISE ELKEKLRDVM VDRHKVALGK TLGEGEFGAV MEGQLNQDDS ILKVAVKTMK IAICTRSELE DFLSEAVCMK EFDHPNVMRL IGVCFQGSER ESFPAPVVIL PFMKHGDLHS FLLYSRLGDQ PVYLPTQMLV KFMADIASGM EYLSTKRFIH RDLAARNCML NENMSVCVAD FGLSKKIYNG DYYRQGRIAK MPVKWIAIES LADRVYTSKS DVWSFGVTMW EIATRGQTPY PGVENSEIYD YLRQGNRLKQ PADCLDGLYA LMSRCWELNP QDRPSFTELR EDLENTLKAL PPAQEPDEIL YVNMDEGGGY PEPPGAAGGA DPPTQPDPKD SCSCLTAAEV HPAGRYVLCP STTPSPAQPA DRGSPAAPGQ EDGA //