ID   ALK_MOUSE               Reviewed;        1621 AA.
AC   P97793; E9QKV3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=ALK tyrosine kinase receptor {ECO:0000305};
DE            EC=2.7.10.1 {ECO:0000250|UniProtKB:Q9UM73};
DE   AltName: Full=Anaplastic lymphoma kinase {ECO:0000303|PubMed:9053841};
DE   AltName: CD_antigen=CD246;
DE   Flags: Precursor;
GN   Name=Alk {ECO:0000303|PubMed:9053841, ECO:0000312|MGI:MGI:103305};
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   TISSUE=Brain, and Testis;
RX   PubMed=9053841; DOI=10.1038/sj.onc.1200849;
RA   Iwahara T., Fujimoto J., Wen D., Cupples R., Bucay N., Arakawa T., Mori S.,
RA   Ratzkin B., Yamamoto T.;
RT   "Molecular characterization of ALK, a receptor tyrosine kinase expressed
RT   specifically in the nervous system.";
RL   Oncogene 14:439-449(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION, INTERACTION WITH CBL; IRS1; PIK3R1; PLCG1 AND SHC1, AND
RP   FUNCTION IN PHOSPHORYLATION OF CBL; IRS1 AND SHC1.
RX   PubMed=15226403; DOI=10.1242/jcs.01183;
RA   Motegi A., Fujimoto J., Kotani M., Sakuraba H., Yamamoto T.;
RT   "ALK receptor tyrosine kinase promotes cell growth and neurite outgrowth.";
RL   J. Cell Sci. 117:3319-3329(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=16458083; DOI=10.1016/j.modgep.2005.11.006;
RA   Vernersson E., Khoo N.K., Henriksson M.L., Roos G., Palmer R.H.,
RA   Hallberg B.;
RT   "Characterization of the expression of the ALK receptor tyrosine kinase in
RT   mice.";
RL   Gene Expr. Patterns 6:448-461(2006).
RN   [5]
RP   INTERACTION WITH IRS1 AND SHC, PHOSPHORYLATION AT TYR-1096, AND FUNCTION.
RX   PubMed=16878150; DOI=10.1038/sj.onc.1209840;
RA   Kuo A.H., Stoica G.E., Riegel A.T., Wellstein A.;
RT   "Recruitment of insulin receptor substrate-1 and activation of NF-kappaB
RT   essential for midkine growth signaling through anaplastic lymphoma
RT   kinase.";
RL   Oncogene 26:859-869(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17487225; DOI=10.1038/sj.npp.1301446;
RA   Bilsland J.G., Wheeldon A., Mead A., Znamenskiy P., Almond S., Waters K.A.,
RA   Thakur M., Beaumont V., Bonnert T.P., Heavens R., Whiting P.,
RA   McAllister G., Munoz-Sanjuan I.;
RT   "Behavioral and neurochemical alterations in mice deficient in anaplastic
RT   lymphoma kinase suggest therapeutic potential for psychiatric
RT   indications.";
RL   Neuropsychopharmacology 33:685-700(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=19200234; DOI=10.1111/j.1460-9568.2008.06593.x;
RA   Degoutin J., Brunet-de Carvalho N., Cifuentes-Diaz C., Vigny M.;
RT   "ALK (Anaplastic Lymphoma Kinase) expression in DRG neurons and its
RT   involvement in neuron-Schwann cells interaction.";
RL   Eur. J. Neurosci. 29:275-286(2009).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22079349; DOI=10.1016/j.pbb.2011.10.024;
RA   Weiss J.B., Xue C., Benice T., Xue L., Morris S.W., Raber J.;
RT   "Anaplastic lymphoma kinase and leukocyte tyrosine kinase: functions and
RT   genetic interactions in learning, memory and adult neurogenesis.";
RL   Pharmacol. Biochem. Behav. 100:566-574(2012).
RN   [9]
RP   REVIEW ON FUNCTION.
RX   PubMed=19459784; DOI=10.1042/bj20090387;
RA   Palmer R.H., Vernersson E., Grabbe C., Hallberg B.;
RT   "Anaplastic lymphoma kinase: signalling in development and disease.";
RL   Biochem. J. 420:345-361(2009).
RN   [10]
RP   FUNCTION.
RX   PubMed=30497772; DOI=10.1016/j.neuron.2018.10.051;
RA   Tang C., Wang M., Wang P., Wang L., Wu Q., Guo W.;
RT   "Neural Stem Cells Behave as a Functional Niche for the Maturation of
RT   Newborn Neurons through the Secretion of PTN.";
RL   Neuron 101:32-44(2019).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP   FEEDING.
RX   PubMed=32442405; DOI=10.1016/j.cell.2020.04.034;
RA   Orthofer M., Valsesia A., Maegi R., Wang Q.P., Kaczanowska J.,
RA   Kozieradzki I., Leopoldi A., Cikes D., Zopf L.M., Tretiakov E.O.,
RA   Demetz E., Hilbe R., Boehm A., Ticevic M., Noukas M., Jais A., Spirk K.,
RA   Clark T., Amann S., Lepamets M., Neumayr C., Arnold C., Dou Z., Kuhn V.,
RA   Novatchkova M., Cronin S.J.F., Tietge U.J.F., Mueller S., Pospisilik J.A.,
RA   Nagy V., Hui C.C., Lazovic J., Esterbauer H., Hagelkruys A., Tancevski I.,
RA   Kiefer F.W., Harkany T., Haubensak W., Neely G.G., Metspalu A., Hager J.,
RA   Gheldof N., Penninger J.M.;
RT   "Identification of ALK in Thinness.";
RL   Cell 181:1246-1262.e22(2020).
CC   -!- FUNCTION: Neuronal receptor tyrosine kinase that is essentially and
CC       transiently expressed in specific regions of the central and peripheral
CC       nervous systems and plays an important role in the genesis and
CC       differentiation of the nervous system (PubMed:15226403,
CC       PubMed:16458083, PubMed:16878150, PubMed:19200234, PubMed:30497772).
CC       Also acts as a key thinness protein involved in the resistance to
CC       weight gain: in hypothalamic neurons, controls energy expenditure
CC       acting as a negative regulator of white adipose tissue lipolysis and
CC       sympathetic tone to fine-tune energy homeostasis (PubMed:32442405).
CC       Following activation by ALKAL2 ligand at the cell surface, transduces
CC       an extracellular signal into an intracellular response. In contrast,
CC       ALKAL1 is not a potent physiological ligand for ALK. Ligand-binding to
CC       the extracellular domain induces tyrosine kinase activation, leading to
CC       activation of the mitogen-activated protein kinase (MAPK) pathway.
CC       Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-
CC       Y-Y motif. Induces tyrosine phosphorylation of CBL, FRS2, IRS1 and
CC       SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. ALK
CC       activation may also be regulated by pleiotrophin (PTN) and midkine
CC       (MDK). PTN-binding induces MAPK pathway activation, which is important
CC       for the anti-apoptotic signaling of PTN and regulation of cell
CC       proliferation. MDK-binding induces phosphorylation of the ALK target
CC       insulin receptor substrate (IRS1), activates mitogen-activated protein
CC       kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation
CC       induction. Drives NF-kappa-B activation, probably through IRS1 and the
CC       activation of the AKT serine/threonine kinase. Recruitment of IRS1 to
CC       activated ALK and the activation of NF-kappa-B are essential for the
CC       autocrine growth and survival signaling of MDK (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UM73, ECO:0000269|PubMed:15226403,
CC       ECO:0000269|PubMed:16458083, ECO:0000269|PubMed:16878150,
CC       ECO:0000269|PubMed:19200234, ECO:0000269|PubMed:30497772,
CC       ECO:0000269|PubMed:32442405}.
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:0000250|UniProtKB:Q9UM73, ECO:0000255|PROSITE-
CC         ProRule:PRU10028};
CC   -!- ACTIVITY REGULATION: Activated upon ALKAL2 ligand-binding. ALKAL2-
CC       driven activation is coupled with heparin-binding (By similarity).
CC       Following ligand-binding, homodimerizes and autophosphorylates,
CC       activating its kinase activity (By similarity). Inactivated through
CC       dephosphorylation by receptor protein tyrosine phosphatase beta and
CC       zeta complex (PTPRB/PTPRZ1) when there is no stimulation by a ligand
CC       (By similarity). {ECO:0000250|UniProtKB:Q9UM73}.
CC   -!- SUBUNIT: Homodimer; homodimerizes following heparin- and ligand-binding
CC       (By similarity). Interacts with CBL, IRS1, PIK3R1 and PLCG1
CC       (PubMed:15226403, PubMed:16878150). Interacts with FRS2 and SHC1
CC       (PubMed:15226403, PubMed:16878150). Interacts with PTN and MDK (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UM73,
CC       ECO:0000269|PubMed:15226403, ECO:0000269|PubMed:16878150}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM73};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UM73}.
CC       Note=Membrane attachment is essential for promotion of neuron-like
CC       differentiation and cell proliferation arrest through specific
CC       activation of the MAP kinase pathway. {ECO:0000250|UniProtKB:Q9UM73}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in central nervous system (CNS)
CC       and other parts of the brain such as the paraventricular nucleus (PVN)
CC       of the hypothalamus. Expression is also found in peripheral nervous
CC       systems, eye, nasal epithelium, olfactory nerve, tongue, skin, tissue
CC       surrounding the esophagus, stomach, midgut, as well as testis and
CC       ovary. {ECO:0000269|PubMed:16458083, ECO:0000269|PubMed:32442405}.
CC   -!- INDUCTION: In the hypothalamus, expression is induced in response to
CC       feeding. {ECO:0000269|PubMed:32442405}.
CC   -!- DOMAIN: The EGF-like region drives the cytokine specificity for ALKAL2.
CC       {ECO:0000250|UniProtKB:Q9UM73}.
CC   -!- DOMAIN: The heparin-binding region binds heparin glycosaminoglycan.
CC       Heparin-binding is required for ALKAL2-driven activation.
CC       {ECO:0000250|UniProtKB:Q9UM73}.
CC   -!- PTM: Phosphorylated at tyrosine residues by autocatalysis, which
CC       activates kinase activity. In cells not stimulated by a ligand,
CC       receptor protein tyrosine phosphatase beta and zeta complex
CC       (PTPRB/PTPRZ1) dephosphorylates ALK at the sites in ALK that are
CC       undergoing autophosphorylation through autoactivation.
CC       {ECO:0000250|UniProtKB:Q9UM73}.
CC   -!- DISRUPTION PHENOTYPE: Mice display a decrease in newborn neurons and
CC       defects in brain function (PubMed:17487225, PubMed:22079349). Mice show
CC       an age-dependent increase in basal hippocampal progenitor proliferation
CC       and alterations in behavioral tests (PubMed:17487225). Mice lacking
CC       both Alk and Ltk show a strong reduction in newborn neurons
CC       (PubMed:22079349). Mutants develop a thin phenotype at the age of 5
CC       weeks, persisting into adulthood with reduced body adiposity, elevated
CC       adiponectin levels and improved glucose homeostasis, while having
CC       unaltered food intake and activity (PubMed:32442405). They show a
CC       marked resistance to diet- and leptin-mutation-induced obesity and
CC       exhibit increased adipose tissue lipolysis (PubMed:32442405).
CC       {ECO:0000269|PubMed:17487225, ECO:0000269|PubMed:22079349,
CC       ECO:0000269|PubMed:32442405}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; D83002; BAA11673.1; -; mRNA.
DR   EMBL; AC122746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS37688.1; -.
DR   PIR; T30200; T30200.
DR   RefSeq; NP_031465.2; NM_007439.2.
DR   AlphaFoldDB; P97793; -.
DR   BMRB; P97793; -.
DR   SMR; P97793; -.
DR   BioGRID; 198070; 17.
DR   STRING; 10090.ENSMUSP00000083840; -.
DR   BindingDB; P97793; -.
DR   ChEMBL; CHEMBL5771; -.
DR   GlyCosmos; P97793; 16 sites, No reported glycans.
DR   GlyGen; P97793; 16 sites.
DR   iPTMnet; P97793; -.
DR   PhosphoSitePlus; P97793; -.
DR   MaxQB; P97793; -.
DR   PaxDb; 10090-ENSMUSP00000083840; -.
DR   ProteomicsDB; 296099; -.
DR   Antibodypedia; 2099; 1775 antibodies from 41 providers.
DR   DNASU; 11682; -.
DR   Ensembl; ENSMUST00000086639.6; ENSMUSP00000083840.5; ENSMUSG00000055471.8.
DR   GeneID; 11682; -.
DR   KEGG; mmu:11682; -.
DR   UCSC; uc008dnb.1; mouse.
DR   AGR; MGI:103305; -.
DR   CTD; 238; -.
DR   MGI; MGI:103305; Alk.
DR   VEuPathDB; HostDB:ENSMUSG00000055471; -.
DR   eggNOG; KOG1095; Eukaryota.
DR   GeneTree; ENSGT00940000159280; -.
DR   HOGENOM; CLU_001878_2_2_1; -.
DR   InParanoid; P97793; -.
DR   OMA; NTACERQ; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; P97793; -.
DR   TreeFam; TF351636; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   Reactome; R-MMU-201556; Signaling by ALK.
DR   BioGRID-ORCS; 11682; 4 hits in 82 CRISPR screens.
DR   ChiTaRS; Alk; mouse.
DR   PRO; PR:P97793; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P97793; Protein.
DR   Bgee; ENSMUSG00000055471; Expressed in inferior vagus X ganglion and 124 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR   GO; GO:0032991; C:protein-containing complex; 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:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR   GO; GO:0030298; F:receptor signaling protein tyrosine kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:MGI.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR   GO; GO:1900006; P:positive regulation of dendrite development; IMP:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0090648; P:response to environmental enrichment; IMP:MGI.
DR   GO; GO:0036269; P:swimming behavior; IMP:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd06263; MAM; 2.
DR   CDD; cd05036; PTKc_ALK_LTK; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR000998; MAM_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   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF276; ALK TYROSINE KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF12810; Gly_rich; 1.
DR   Pfam; PF00629; MAM; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50060; MAM_2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
DR   Genevisible; P97793; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1621
FT                   /note="ALK tyrosine kinase receptor"
FT                   /id="PRO_0000016741"
FT   TOPO_DOM        19..1042
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1043..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1064..1621
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          268..431
FT                   /note="MAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          441..477
FT                   /note="LDL-receptor class A"
FT   DOMAIN          482..640
FT                   /note="MAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          1120..1396
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          48..70
FT                   /note="Heparin-binding region"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   REGION          991..1029
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   REGION          1412..1556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         1126..1134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1201..1203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1082
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   MOD_RES         1096
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:16878150"
FT   MOD_RES         1100
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   MOD_RES         1135
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   MOD_RES         1282
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   MOD_RES         1516
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        713
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        812
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        868
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        890
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        990
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        692..705
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   DISULFID        787..798
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   DISULFID        910..932
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   DISULFID        991..999
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   DISULFID        994..1010
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   DISULFID        1012..1025
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM73"
FT   CONFLICT        138..139
FT                   /note="KL -> NV (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="M -> L (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        857
FT                   /note="T -> R (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1075..1076
FT                   /note="ME -> IQ (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1522
FT                   /note="E -> A (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1586
FT                   /note="G -> P (in Ref. 1; BAA11673)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1621 AA;  174948 MW;  72D1022E117F303E CRC64;
     MGAAGFLWLL PPLLLAAASY SGAATDQRAG SPASGPPLQP REPLSYSRLQ RKSLAVDFVV
     PSLFRVYARD LLLPQPRSPS EPEAGGLEAR GSLALDCEPL LRLLGPLPGI SWADGASSPS
     PEAGPTLSRV LKGGSVRKLR RAKQLVLELG EETILEGCIG PPEEVAAVGI LQFNLSELFS
     WWILHGEGRL RIRLMPEKKA SEVGREGRLS SAIRASQPRL LFQIFGTGHS SMESPSETPS
     PPGTFMWNLT WTMKDSFPFL SHRSRYGLEC SFDFPCELEY SPPLHNHGNQ SWSWRHVPSE
     EASRMNLLDG PEAEHSQEMP RGSFLLLNTS ADSKHTILSP WMRSSSDHCT LAVSVHRHLQ
     PSGRYVAQLL PHNEAGREIL LVPTPGKHGW TVLQGRVGRP ANPFRVALEY ISSGNRSLSA
     VDFFALKNCS EGTSPGSKMA LQSSFTCWNG TVLQLGQACD FHQDCAQGED EGQLCSKLPA
     GFYCNFENGF CGWTQSPLSP HMPRWQVRTL RDAHSQGHQG RALLLSTTDI LASEGATVTS
     ATFPAPMKNS PCELRMSWLI RGVLRGNVSL VLVENKTGKE QSRTVWHVAT DEGLSLWQHT
     VLSLLDVTDR FWLQIVTWWG PGSRATVGFD NISISLDCYL TISGEEKMSL NSVPKSRNLF
     EKNPNKESKS WANISGPTPI FDPTVHWLFT TCGASGPHGP TQAQCNNAYQ NSNLSVVVGS
     EGPLKGVQIW KVPATDTYSI SGYGAAGGKG GKNTMMRSHG VSVLGIFNLE KGDTLYILVG
     QQGEDACPRA NQLIQKVCVG ENNVIEEEIR VNRSVHEWAG GGGGGGGATY VFKMKDGVPV
     PLIIAAGGGG RAYGAKTETF HPERLESNSS VLGLNGNSGA AGGGGGWNDN TSLLWAGKSL
     LEGAAGGHSC PQAMKKWGWE TRGGFGGGGG GCSSGGGGGG YIGGNAASNN DPEMDGEDGV
     SFISPLGILY TPALKVMEGH GEVNIKHYLN CSHCEVDECH MDPESHKVIC FCDHGTVLAD
     DGVSCIVSPT PEPHLPLSLI LSVVTSALVA ALVLAFSGIM IVYRRKHQEL QAMQMELQSP
     EYKLSKLRTS TIMTDYNPNY CFAGKTSSIS DLKEVPRKNI TLIRGLGHGA FGEVYEGQVS
     GMPNDPSPLQ VAVKTLPEVC SEQDELDFLM EALIISKFNH QNIVRCIGVS LQALPRFILL
     ELMAGGDLKS FLRETRPRPN QPTSLAMLDL LHVARDIACG CQYLEENHFI HRDIAARNCL
     LTCPGAGRIA KIGDFGMARD IYRASYYRKG GCAMLPVKWM PPEAFMEGIF TSKTDTWSFG
     VLLWEIFSLG YMPYPSKSNQ EVLEFVTSGG RMDPPKNCPG PVYRIMTQCW QHQPEDRPNF
     AIILERIEYC TQDPDVINTA LPIEYGPVVE EEEKVPMRPK DPEGMPPLLV SPQPAKHEEA
     SAAPQPAALT APGPSVKKPP GAGAGAGAGA GAGPVPRGAA DRGHVNMAFS QPNPPPELHK
     GPGSRNKPTS LWNPTYGSWF TEKPAKKTHP PPGAEPQARA GAAEGGWTGP GAGPRRAEAA
     LLLEPSALSA TMKEVPLFRL RHFPCGNVNY GYQQQGLPLE ATAAPGDTML KSKNKVTQPG
     P
//