ID F1LNJ1_RAT Unreviewed; 2526 AA.
AC F1LNJ1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 3.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Lrrk2 {ECO:0000313|Ensembl:ENSRNOP00000005438.7,
GN ECO:0000313|RGD:1561168};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000005438.7, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000005438.7, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005438.7,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000005438.7}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005438.7};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 RefSeq; XP_006242252.1; XM_006242190.3.
DR AlphaFoldDB; F1LNJ1; -.
DR SMR; F1LNJ1; -.
DR IntAct; F1LNJ1; 2.
DR STRING; 10116.ENSRNOP00000005438; -.
DR iPTMnet; F1LNJ1; -.
DR PhosphoSitePlus; F1LNJ1; -.
DR PaxDb; 10116-ENSRNOP00000005438; -.
DR ABCD; F1LNJ1; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000005438.8; ENSRNOP00000005438.7; ENSRNOG00000004048.8.
DR AGR; RGD:1561168; -.
DR CTD; 120892; -.
DR RGD; 1561168; Lrrk2.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158267; -.
DR HOGENOM; CLU_000815_0_0_1; -.
DR InParanoid; F1LNJ1; -.
DR OMA; FIVECMV; -.
DR OrthoDB; 148126at2759; -.
DR TreeFam; TF313679; -.
DR Reactome; R-RNO-8857538; PTK6 promotes HIF1A stabilization.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004048; Expressed in lung and 19 other cell types or tissues.
DR GO; GO:0044753; C:amphisome; ISO:RGD.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0099400; C:caveola neck; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0097487; C:multivesicular body, internal vesicle; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:1990909; C:Wnt signalosome; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1904713; F:beta-catenin destruction complex binding; ISO:RGD.
DR GO; GO:0030276; F:clathrin binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0034211; F:GTP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:RGD.
DR GO; GO:0036479; F:peroxidase inhibitor activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:1903351; P:cellular response to dopamine; ISO:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0035640; P:exploration behavior; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0046039; P:GTP metabolic process; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007254; P:JNK cascade; ISO:RGD.
DR GO; GO:0035641; P:locomotory exploration behavior; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0051646; P:mitochondrion localization; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:RGD.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0140058; P:neuron projection arborization; IMP:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; IMP:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; ISO:RGD.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; ISO:RGD.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0035564; P:regulation of kidney size; ISO:RGD.
DR GO; GO:0040012; P:regulation of locomotion; ISO:RGD.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; ISO:RGD.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; ISO:RGD.
DR GO; GO:0014041; P:regulation of neuron maturation; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; ISO:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:ParkinsonsUK-UCL.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:1902803; P:regulation of synaptic vesicle transport; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0021756; P:striatum development; IEP:RGD.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; ISO:RGD.
DR GO; GO:1904887; P:Wnt signalosome assembly; ISO:RGD.
DR CDD; cd09914; RocCOR; 1.
DR CDD; cd14068; STKc_LRRK2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF13; SERINE_THREONINE-PROTEIN KINASE DDB_G0278509-RELATED; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51424; ROC; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1327..1510
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1878..2145
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 956..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2526 AA; 284831 MW; DB5CA86E1E96E716 CRC64;
MASGACQGCD EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDILVFTYS DRASKLFEGK
NVHVPLLIVL DSYMRVASVQ QVGWSLLCKL IEVCPGTLQS LIGPQDIGND WEVLGIHRLI
LKMLTVHHAN VNLSIVGLKA LDLLLDSGKI TLLILDEECD VFLLIFDAMH RYSANEEVQK
LACKALHVLF ERVSEEQLTE FVENKDYMTL LSTFRSFKRD EEIVHHVLCC LHSLAVTCSN
VEVLMSGNVR CYNIVVEAMK TFPTSENIQE VSCSLLHKLT LGNFFNILVL NEVHVFVVKA
VQRYPENVAL QISALSCLAL LTETIFLNQD LEERSETQEN SDEDSEKPFW LEPCYKALMR
HRKNKHVQEA ACWALNNLLM YQSSLHEKIG DEDGQFPAHR EVMLSMLMHS SSKDVFQAAA
HALSTLLEQN VNFRKILLAK GVYLNVLELM QRHAQVPEVA ESGCKMLSHL FEGSNPSLDT
VAAVIPKILT VMRTHGTSLS VQLEALRALL HFVVPGVSED SRDDSRCQPN VLRTQCFRTD
IHKLVLAALN RFIGNPGIQK CGLKVISSFA HLPDALEMLS LHGAVDSVLH TLQMYPDDQE
IQCLGLHLMG CLMTKKNFCI GTGHLLAKIL ASTLQRFKDV AEVQTTGLQT VLSMLDLSVS
FSKLLVHYSF DVVMFHQMSS GVLEQKDEQF LNLCCKCFAK VAVDDELKSK MLERACDQNN
SIMVECLLLL GADANQAKGA TSLIYQVCEK ESSPKLVELL LNSGCREQDV RKALTVSIQK
GDNQVISLLL RRLALDLANN SICLGGFCIG KLDPSWLGPL FPDKSSNLRK QTNAGSVLAR
KVLRYQMRNT LQEGVASGSE GNFSEDALAK FGEWTFIPDS SMDSVFGQSD DLDSEGSESS
FLVKKKSNSV SVGEVYRDLA LQRCSPNAQR HSSSLGPVFD HEDLLRRKRK ILSSDESLRS
SRLQSHTRQS DSSSSLASER EHITSLDLSA NELKDIDALG QKCCLSSHLE HLTKLELHQN
SLTSFPQQLC ETLKCLTHLD LHSNKFATFP SFMLKMPSVI HLDASRNDIG PTVVLDPVVK
CPSLKQFNLS YNQLSSIPEN LDQVVEKLEQ LLLEGNKISG ICSPLSLKEL KILNLSKNHI
PSLPEDFLEA CPKVESFSAR MNFLAAMPAL PSSITSLKLS QNSFTCIPEA IFSLPHLRSL
DMSHNNIEHL PGPAHWKSLN LRELIFSKNQ ISTLDLSENP HIWSRVEKLH LSHNKLKEIP
PEIGRLENLT SLDVSYNLEL RSFPNEMGKL SKIWDLPLDG LHLNFDFKHI GCKAKDIIRF
LQQRLKKAVP YNRMKLMIVG NTGSGKTTLL QQLMKMKKSE LGMQGATVGI DVRDWPIQIR
GKRKKDLVLN VWDFAGREEF YSTHPHFMTQ RALYLAVYDL SKGQAEVDAM KPWLFNIKAR
ASSSPVILVG THLDVSDEKQ RKACIGKITK ELLNKRGFPT IRDYHFVNAT EESDALAKLR
KTIINESLNF KIRDQPVVGQ LIPDCYVELE KIILSERKAV PTEFPVINRK HLLQLVKEHQ
LQLDENELPH AVHFLNESGV LLHFQDPALQ LSDLYFVEPK WLCKVMAQIL TVKVDGCLKH
PKGIISRRDV EKFLSKKKRF PKNYMAQYFK LLEKFQIALP IGEEYLLVPS SLSDHRPVIE
LPHCENSEII IRLYEMPYFP MGFWSRLINR LLEISPFMLS GRERALRPNR MYWRQGIYLN
WSPEAYCLVG SEVLDSRPES FLKITVPSCR KGCILLGRVV DHIDSLMEEW FPGLLEIDIC
GEGETLLKKW ALYSFNDGEE HQKILLDELM KKAEEGDLLI NPDQPRLTIP ISQIAPDLIL
ADLPRNIMLN NDELEFEEAP EFLLGDGSFG SVYRAAYEGE EVAVKIFNKH TSLRLLRQEL
VVLCHLHHPS LISLLAAGIR PRMLVMELAS KGSLDRLLQQ DKASLTRTLQ HRIALHVADG
LRYLHSAMII YRDLKPHNVL LFTLYPNAAI IAKIADYGIA QYCCRMGIKT SEGTPGFRAP
EVARGNVIYN QQADVYSFGL LLHDIWTTGN RIMEGLRFPN EFDELAIQGK LPDPVKEYGC
APWPMVEKLI TKCLKENPQE RPTSAQVFDI LNSAELICLM RHIFIPKDIT VECIAATNLN
SKRATLWLGC GNTEKGQLSL LDLNTERYSY EEVTDSRILC LALVHLAAEK ESWVVCGTQS
GALLVINAED ETRRHTLDKM TDSVTCLYCN SFAKQSKQSH FLLVGTADGN LMIFEDKTIK
CKGAAPLKTL HIGDVSTPLM CLSESMNSSE RHITWGGCGT KIFSFSNDFT IQKLIETRTN
QLFSYSAFSD SNIIAVAVDT ALYIAKKNSP VVEVWDKKTE KLCELIDCVH FLKEVMVKIN
KDSKHKLSYS GRVKALCLQK NTALWIGTGG GHILLLDLST RRVIRTIHNF CDSVRAMATA
QLGSLKNVML VLGYKRKSTE GTQEQKEIQS CLSIWDLNLP HEVQNLEKHI EVRTELADKM
RKTSVE
//
