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Leucine rich repeat kinase 2

 F1PHH4_CANLF            Unreviewed;      2527 AA.
F1PHH4;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 2.
22-NOV-2017, entry version 61.
SubName: Full=Leucine rich repeat kinase 2 {ECO:0000313|Ensembl:ENSCAFP00000014627};
Name=LRRK2 {ECO:0000313|Ensembl:ENSCAFP00000014627};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000014627, ECO:0000313|Proteomes:UP000002254};
[1] {ECO:0000313|Ensembl:ENSCAFP00000014627, ECO:0000313|Proteomes:UP000002254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000014627,
ECO:0000313|Proteomes:UP000002254};
PubMed=16341006; DOI=10.1038/nature04338;
Broad Sequencing Platform;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2] {ECO:0000313|Ensembl:ENSCAFP00000014627}
IDENTIFICATION.
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000014627};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- CAUTION: The sequence shown here is derived from an Ensembl
automatic analysis pipeline and should be considered as
preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000014627}.
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EMBL; AAEX03015138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_013964022.1; XM_014108547.1.
RefSeq; XP_543734.3; XM_543734.5.
ProteinModelPortal; F1PHH4; -.
STRING; 9615.ENSCAFP00000014627; -.
PaxDb; F1PHH4; -.
Ensembl; ENSCAFT00000015801; ENSCAFP00000014627; ENSCAFG00000009926.
GeneID; 486608; -.
KEGG; cfa:486608; -.
CTD; 120892; -.
eggNOG; KOG0192; Eukaryota.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG1100; LUCA.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00530000063477; -.
InParanoid; F1PHH4; -.
KO; K08844; -.
OMA; FKIRDQP; -.
OrthoDB; EOG091G003N; -.
TreeFam; TF313679; -.
Reactome; R-CFA-8857538; PTK6 promotes HIF1A stabilization.
Proteomes; UP000002254; Chromosome 27.
Bgee; ENSCAFG00000009926; -.
GO; GO:0044753; C:amphisome; IEA:Ensembl.
GO; GO:0044754; C:autolysosome; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0099400; C:caveola neck; IEA:Ensembl.
GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0097487; C:multivesicular body, internal vesicle; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:1904713; F:beta-catenin destruction complex binding; IEA:Ensembl.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0034211; F:GTP-dependent protein kinase activity; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0036479; F:peroxidase inhibitor activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0017048; F:Rho GTPase binding; IBA:GO_Central.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
GO; GO:0000186; P:activation of MAPKK activity; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IBA:GO_Central.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IEA:Ensembl.
GO; GO:1903125; P:negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0070997; P:neuron death; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IEA:Ensembl.
GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IEA:Ensembl.
GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IEA:Ensembl.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IBA:GO_Central.
GO; GO:0035564; P:regulation of kidney size; IEA:Ensembl.
GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
GO; GO:0035751; P:regulation of lysosomal lumen pH; IEA:Ensembl.
GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:1902692; P:regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0014041; P:regulation of neuron maturation; IEA:Ensembl.
GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl.
GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IBA:GO_Central.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:1902803; P:regulation of synaptic vesicle transport; IBA:GO_Central.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
GO; GO:1904887; P:Wnt signalosome assembly; IEA:Ensembl.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.80.10.10; -; 4.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032171; COR.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR020859; ROC_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16095; COR; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51450; LRR; 11.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51424; ROC; 1.
4: Predicted;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002254};
Leucine-rich repeat {ECO:0000256|SAAS:SAAS00537711};
Reference proteome {ECO:0000313|Proteomes:UP000002254};
Repeat {ECO:0000256|SAAS:SAAS00537628}.
DOMAIN 1328 1511 Roc. {ECO:0000259|PROSITE:PS51424}.
DOMAIN 1879 2146 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
COILED 320 347 {ECO:0000256|SAM:Coils}.
SEQUENCE 2527 AA; 285650 MW; 5146A8D99B12C55C CRC64;
MASGSCQGCE EEDEETLKKL IVRLNNVQEG KQIETLVQIL EDMLVFTYAD HASKLFQGKK
VHVPVLIVLD LYMRVASVQQ VGWSLLCKLI EICPNTMKSL MGPQDIGHDW EVLGVHQLIL
KMLTVHNASV NLLTVGLRAL DLLLTSGKIT LLILDEESDI FLLIFDAMRT FSANDEVQKL
GCKALRVLFE RVSEEQLIEF VENKDYMILL NALKNFKDEE EIVLHVLHCL HSLAIPCNNV
EVLMSGNVRC YNIVVEAMKA FPVHEKIQEV SCCLLHRLTL GNFFNILVLN EVHEFVVKAV
RRYSENATLQ IAALSCLALL TETIFLNQDL EEKNENQEND DEEEEKLFWL EACYKALTWH
RKNKHVQEAA CWALNNLLMY QNSLHEKIGD EDGQFPAHRE VMLSMLMHSS SKEVFQASAN
ALSTLLEQNV NFRKILLSKG IYFNVLELMQ KHIHSPEVAE SGCKLLDHLF EGSDATLDIM
AAVAPKIITV MKSHEASSLV QLEALRAILH FIVPGMPEDS REDTEYQHKL NLVKKQCFKN
DIHKLVLAAL NRFIGIPGIQ KSGLKVISSL AQSPDALEVL SLEGAIDSVL HTLQMYPDDQ
EIQCLGLSLI GCLITKKNLC IGTGHLLAKI LASSLQRFKD MAEVQIKGFQ TILTILELSM
SFGKLLVNHS FDSVIFHQMS SSILESKDQQ FLNLCCKCFA KLAMDDELKS VMLERACDQN
NSIMVECLLL LGADANRTKE ATSLICQVCE KASSPKLVEL LLNGGSREQD VRKALTISIG
KGDSQIISLL LRRLALDLAN NSICLGGFCI GKIEPSWLGP LFPDKTSNLR KETNIGSTLA
RMVLRYQMKS TVEGGAASGS NGNFPEEVLD KLDEWTFIPD SYVDSVFGQS DDLDSEGSEG
SFLVKRKSNS ISVGEFYHDR ALQRCSPNLQ RHSNSLGPIF DHEDFLRRKR KILSSDDSLW
SSKLQSHMRH SDSISSLPSE REYITSLDLS ANELRDIDAL SQKCCISGHL EHLERLELHQ
NALTSFPQQL CEMLKCLTHL DLHSNKFASF PSYLLKMNCI VNLDVSRNDI SPSVVLDPTV
KCPTLKQFNL SYNQLSSFPE NLGDVVEKLE QLILEGNKIP GICSPLSLKE LKILNLSKNH
ITSLAEDFFE ACPKVESFSA RINYLAAMPF LPSSLTSLKL SQNRFTCVPE AILNLPHLRS
LDMSSNEIEY LPSPAHWKSL NLRELLFSFN QISILDLSEK AYVWSRVEKL HLSHNKLKEI
PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD ELRLNFDFKH IGCKAKDIIR
FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLTKTKKS DLGVQSATVG IDVKDWPIQI
RGKGKKDLIL NVWDFAGREE FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA
RASSSPVILV GTHLDVSDEK QRKACISKIT KELLNKRGFP AIRDYHFVNA TEESDALAKL
RKTIINESLN FKIRDQPVVG QLIPDCYVEL EKIILSERKN VPIEFPVIDR KRLLQLVKEN
QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP KWLCKVMAQI LTVKVEGYPK
HPKGIISRRD VEKFLSKKKR FPKNYMSQYF KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI
ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPYML SGRERALRPN RMYWRQGIYL
NWSPEAYCLV GSEVLDNHPE SFLKITVPSC RKGCILLGQV VDHIDSLMEE WFPGLLEIDI
CGEGETLLKK WALYSFNDGE EHQKILLDDL MKKAEEGDLL VNPDQPRLTI PISQIAPDLI
LADLPRNIML NNDELEFEQA PEFLLGDGSF GSVYRAAYEG EEVAVKIFNK HTSLRLLRQE
LVVLCHLHHP SLISLLAAGI RPRMLVMELA SKGSLDRLLQ QDKASLTRTL QHRIALHVAD
GLRYLHSAMI IYRDLKPHNV LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA
PEVARGNVIY NQQADVYSFG LLLYDILTTG GRIAEGLKFP NEFDELAIQG KLPDPVKEYG
CAPWPMVEKL IKKCLKENPQ ERPTSAQVFD ILNSAELICL MRHISIPKNF SVECMVATNH
NSKNASIWLG CGHPNKGQLS FLDLSTEKHT SEEVTDSRIL CLALVHLPVE KESWIVCGTQ
SGMLLVINTE DGAKRHTLEK MTDSVTCLYC NPFPKQSKQR NFLLVGTADG NLAIFEDKTV
KCKGAAPLKI LNIGNVSTPL MCLSESMNST EKNIMWGGCG TKLFSFSDDF TIQKLIETKT
NQLFSYAAFS DSNIIAVVVD TAVYVAKKNS PFVEVRDKKT EKLCELIDCV HFLKEEMVKV
NAESKHKLSY SGRVKTLCLQ KNTALWIGTG GGHILLLDLS TRRIIRIIHN FCDSVRVMMT
AQLGSLKNVM LVLGYIRKNT EGTQPQKEIQ SCLSVWDINL PHEVQNLEKH IEVRKELAEK
MRRISVE


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