UFO_MOUSE
ID UFO_MOUSE Reviewed; 888 AA.
AC Q00993; Q80YQ3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Tyrosine-protein kinase receptor UFO;
DE EC=2.7.10.1;
DE AltName: Full=Adhesion-related kinase;
DE Flags: Precursor;
GN Name=Axl; Synonyms=Ark, Ufo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Heart;
RX PubMed=1320243;
RA Faust M., Ebensperger C., Schulz A.S., Schleithoff L., Hameister H.,
RA Bartram C.R., Janssen J.W.G.;
RT "The murine ufo receptor: molecular cloning, chromosomal localization and
RT in situ expression analysis.";
RL Oncogene 7:1287-1293(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840679;
RA Rescigno J., Mansukhani A., Basilico C.;
RT "A putative receptor tyrosine kinase with unique structural topology.";
RL Oncogene 6:1909-1913(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 INTERACTION WITH LIGAND GAS6.
RX PubMed=7867073; DOI=10.1016/0092-8674(95)90520-0;
RA Stitt T.N., Conn G., Gore M., Lai C., Bruno J., Radziejewski C.,
RA Mattsson K., Fisher J., Gies D.R., Jones P.F., Masiakowski P., Ryan T.E.,
RA Tobkes N.J., Chen D.H., DiStefano P.S., Long G.L., Basilico C.,
RA Goldfarb M.P., Lemke G., Glass D.J., Yancopoulos G.D.;
RT "The anticoagulation factor protein S and its relative, Gas6, are ligands
RT for the Tyro 3/Axl family of receptor tyrosine kinases.";
RL Cell 80:661-670(1995).
RN [7]
RP FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.
RX PubMed=18083102; DOI=10.1016/j.cell.2007.10.034;
RA Rothlin C.V., Ghosh S., Zuniga E.I., Oldstone M.B., Lemke G.;
RT "TAM receptors are pleiotropic inhibitors of the innate immune response.";
RL Cell 131:1124-1136(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.
RX PubMed=20363878; DOI=10.1210/en.2009-1498;
RA Sun B., Qi N., Shang T., Wu H., Deng T., Han D.;
RT "Sertoli cell-initiated testicular innate immune response through toll-like
RT receptor-3 activation is negatively regulated by Tyro3, Axl, and mer
RT receptors.";
RL Endocrinology 151:2886-2897(2010).
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:18083102, ECO:0000269|PubMed:20363878}.
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 -!- ACTIVITY REGULATION: Activated by GAS6-binding and subsequent
CC autophosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer and heterotetramer with ligand GAS6 (By
CC similarity). Interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2,
CC PIK3R3, PLCG1, SOCS1 and TNS2. Part of a complex including AXL, TNK2
CC and GRB2, in which GRB2 promotes AXL recruitment by TNK2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In distinct substructures of a broad spectrum of
CC developing tissues (in the late embryogenesis). In cells forming organ
CC capsules as well as in connective tissue structures (in adult).
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 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at tyrosine residues by autocatalysis, which
CC activates kinase activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X63535; CAA45097.1; -; mRNA.
DR EMBL; X59560; CAA42158.1; -; Genomic_DNA.
DR EMBL; AK155567; BAE33327.1; -; mRNA.
DR EMBL; CH466593; EDL24236.1; -; Genomic_DNA.
DR EMBL; BC046618; AAH46618.1; -; mRNA.
DR EMBL; BC050914; AAH50914.1; -; mRNA.
DR CCDS; CCDS20996.1; -.
DR PIR; S23065; S23065.
DR PIR; S23251; S23251.
DR RefSeq; NP_033491.2; NM_009465.4.
DR RefSeq; XP_006540052.1; XM_006539989.3.
DR AlphaFoldDB; Q00993; -.
DR SMR; Q00993; -.
DR BioGRID; 204922; 22.
DR IntAct; Q00993; 2.
DR MINT; Q00993; -.
DR STRING; 10090.ENSMUSP00000002677; -.
DR GlyGen; Q00993; 6 sites.
DR iPTMnet; Q00993; -.
DR PhosphoSitePlus; Q00993; -.
DR MaxQB; Q00993; -.
DR PaxDb; Q00993; -.
DR PeptideAtlas; Q00993; -.
DR PRIDE; Q00993; -.
DR ProteomicsDB; 298194; -.
DR ABCD; Q00993; 22 sequenced antibodies.
DR Antibodypedia; 30709; 1043 antibodies from 43 providers.
DR DNASU; 26362; -.
DR Ensembl; ENSMUST00000002677; ENSMUSP00000002677; ENSMUSG00000002602.
DR GeneID; 26362; -.
DR KEGG; mmu:26362; -.
DR UCSC; uc009ftx.2; mouse.
DR CTD; 558; -.
DR MGI; MGI:1347244; Axl.
DR VEuPathDB; HostDB:ENSMUSG00000002602; -.
DR eggNOG; ENOG502QQQ3; Eukaryota.
DR GeneTree; ENSGT00940000160232; -.
DR InParanoid; Q00993; -.
DR OMA; IIRCSVQ; -.
DR OrthoDB; 263089at2759; -.
DR PhylomeDB; Q00993; -.
DR TreeFam; TF317402; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR BioGRID-ORCS; 26362; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Axl; mouse.
DR PRO; PR:Q00993; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q00993; protein.
DR Bgee; ENSMUSG00000002602; Expressed in gonadal ridge and 222 other tissues.
DR ExpressionAtlas; Q00993; baseline and differential.
DR Genevisible; Q00993; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0044228; C:host cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; ISO:MGI.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0097028; P:dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IGI:MGI.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0021885; P:forebrain cell migration; IGI:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0046649; P:lymphocyte activation; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; IGI:MGI.
DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; ISO:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IGI:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IGI:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IGI:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0097350; P:neutrophil clearance; IGI:MGI.
DR GO; GO:0042698; P:ovulation cycle; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IGI:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; ISO:MGI.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:1903902; P:positive regulation of viral life cycle; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
DR GO; GO:0032940; P:secretion by cell; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
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 ATP-binding; Cell membrane; Differentiation; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Innate immunity; Kinase; Membrane;
KW Nucleotide-binding; Oncogene; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..888
FT /note="Tyrosine-protein kinase receptor UFO"
FT /id="PRO_0000024482"
FT TOPO_DOM 19..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..122
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..216
FT /note="Ig-like C2-type 2"
FT DOMAIN 221..325
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 330..422
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..801
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 19..86
FT /note="Interaction with GAS6"
FT /evidence="ECO:0000250"
FT REGION 820..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 666
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 536..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 697
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 773
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P30530"
FT MOD_RES 815
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P30530"
FT MOD_RES 860
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P30530"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
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 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 394
FT /note="A -> R (in Ref. 2; CAA42158)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="G -> P (in Ref. 2; CAA42158)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> V (in Ref. 2; CAA42158)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="C -> F (in Ref. 1; CAA45097)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="A -> S (in Ref. 1; CAA45097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 98191 MW; C5350E3A8995E975 CRC64;
MGRVPLAWWL ALCCWGCAAH KDTQTEAGSP FVGNPGNITG ARGLTGTLRC ELQVQGEPPE
VVWLRDGQIL ELADNTQTQV PLGEDWQDEW KVVSQLRISA LQLSDAGEYQ CMVHLEGRTF
VSQPGFVGLE GLPYFLEEPE DKAVPANTPF NLSCQAQGPP EPVTLLWLQD AVPLAPVTGH
SSQHSLQTPG LNKTSSFSCE AHNAKGVTTS RTATITVLPQ RPHHLHVVSR QPTELEVAWT
PGLSGIYPLT HCNLQAVLSD DGVGIWLGKS DPPEDPLTLQ VSVPPHQLRL EKLLPHTPYH
IRISCSSSQG PSPWTHWLPV ETTEGVPLGP PENVSAMRNG SQVLVRWQEP RVPLQGTLLG
YRLAYRGQDT PEVLMDIGLT REVTLELRGD RPVANLTVSV TAYTSAGDGP WSLPVPLEPW
RPGQGQPLHH LVSEPPPRAF SWPWWYVLLG ALVAAACVLI LALFLVHRRK KETRYGEVFE
PTVERGELVV RYRVRKSYSR RTTEATLNSL GISEELKEKL RDVMVDRHKV ALGKTLGEGE
FGAVMEGQLN QDDSILKVAV KTMKIAICTR SELEDFLSEA VCMKEFDHPN VMRLIGVCFQ
GSDREGFPEP VVILPFMKHG DLHSFLLYSR LGDQPVFLPT QMLVKFMADI ASGMEYLSTK
RFIHRDLAAR NCMLNENMSV CVADFGLSKK IYNGDYYRQG RIAKMPVKWI AIESLADRVY
TSKSDVWSFG VTMWEIATRG QTPYPGVENS EIYDYLRQGN RLKQPVDCLD GLYALMSRCW
ELNPRDRPSF AELREDLENT LKALPPAQEP DEILYVNMDE GGSHLEPRGA AGGADPPTQP
DPKDSCSCLT AADVHSAGRY VLCPSTAPGP TLSADRGCPA PPGQEDGA
