ID H2NPB9_PONAB Unreviewed; 2015 AA.
AC H2NPB9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 63.
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=LRRK1 {ECO:0000313|Ensembl:ENSPPYP00000007741.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007741.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000007741.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000007741.3}
RP IDENTIFICATION.
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};
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DR Ensembl; ENSPPYT00000008058.3; ENSPPYP00000007741.3; ENSPPYG00000006824.3.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160363; -.
DR HOGENOM; CLU_001731_0_0_1; -.
DR InParanoid; H2NPB9; -.
DR OMA; GEEVIWC; -.
DR TreeFam; TF313679; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR CDD; cd14067; STKc_LRRK1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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 InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR020859; ROC_dom.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR PANTHER; PTHR48055:SF13; LEUCINE-RICH REPEAT SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00364; LRR_BAC; 8.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
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; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 632..826
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1242..1525
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2015 AA; 225378 MW; BAA3F27311FA7D22 CRC64;
MAGMSQRPPS MYWCVGPEES AVCPERAMEM LNGAGDMGSK PSTPGGAPTA QPHGTEGIRA
AYRRGDRGGA RDLLKEACDR CASQREKGQL LSIPAAYGDL EMVRYLLSKR LVELPTEPTD
DNPAVVAAYF GHTAVVQELL ESLPGPCSPQ RLLNWMLALA CQQGHLGVVK LLVLTHGADP
ESYAVRKNEF PVIVRLPLYA AIKSGNEDIA IFLLRHGAYF CSYILLDSPD PSKHLLRKYF
IEASPLPSSY PGKTALRVKW SHLRLPWVDL DWLIDISCQI TELDLSANCL ATLPSVIPWG
LINLRKLNLS NNHLGELPGV QSSDEIICSR LLEIDISSNK LSHLPPGFLH LSKLQKLTAS
KNCLEKLFEE ENATNWIGLR KLQELDISDN KLTELPALFL HSFKSLNSLN VSRNNLKVFP
DPWACPLKCC KASRNALECL PDKMAVFWKN HLKDVDFSEN ALKEVPLGLF QLDALMFLRL
QGNQLAVLPP QEKWTCRQLK TLDLSRNQLG KNEDGLKTKR IAFFTTRGRQ RSGTEAACVL
EFPAFLSESL EVLCLNDNHL DTVPPSVCVL KSLSELYLGN NPGLRELPPE LGQLGNLWQL
DTEDLTISNV PAEIRKEGPK AMLSYLRAQL RKAEKCKLMK MIIVGPPRQG KSTLLEILQT
GRAPQVVHGE ATIRTTKWEL QRPAGSRAKV ESVEFNVWDI GGPASMATVN QCFFTDKALY
VVVWNLALGE EAVANLQFWL LNIEAKAPNA VVLVVGTHLD LIEAKFRVER IATLRAYVLA
LCRSPSGSRA MGFPDITFKH LYEISCKSLE GQEGLRQLIF HVTCSMKDVG STIGCQRLAG
RLIPRSYLSL QEAVLAEQQR RSLDDNVQYL TDRQLEQLVE QTPDNDIKDY EDLQSAISFL
IETGTLLHFP DTSHGLRNLY FLDPIWLSEC LQRIFNIKGS RSVAKNGVIR AEDLRMLLVG
TGFTQQTEEQ YFQFLAKFEI ALPVANDSYL LPHLLPSKPG LDTHGMRHPT ANTIQRVFKM
SFVPVGFWQR FIARMLISLA EMDLQLFENK KNTKSRNRKV TIYSFTGNQR NRCSTFRVKR
NQTIYWQEGL LVTFDGGYLS VESSDVNWKK KKSGGIKIVC QSEMRDFSAM AFITDHVNSL
IDQWFPALTA TESDGTPLME QYVPCPVCET AWAQHTDPSE KSEDVQYFDM EDCVLTAIER
DFISCPRHPD LPVPLQELVP ELFMTDFPAR LFLENSKLEH SEDEGSVLGQ GGSGTVIYRA
RYQGQPVAVK RFHIKKFKNF ANVPADTMLR HLRATDAMKN FSEFRQEASM LHALQHPCIV
ALIGISIHPL CFALELAPLS SLNTVLSENA RDSSFIPLGH MLTQKIAYQI ASGLAYLHKK
NVIFCDLKSD NILVWSLDVK EHVNIKLSDY GISRQSFHEG ALGVEGTPGY QAPEIRPRIV
YDEKVDMFSY GMVLYELLSG QRPALGHHQL QIAKKLSKGI RPVLGQPEEV QFQRLQALMM
ECWDTKPEKR PLALSVVSQM KDPTFATFMY ELRCGKQTAF FSSQGQEYTV VFWDGKEESR
NYTVVNTEKG LMEVQRMCCP GMKVSCQLQV QRSLWTATED QKIYIYTLKG MCPLNTPQRA
LDTPAVVTCF LAVPVIKKNS YLVLAGLADG LVAVFPVVRG APKDSCSYLC SHTANRSKFS
IADEDARQNP YPVKAMEVVN SGSEVWYSNG PGLLVIDCAS LEICRRLEPY VAPSVVTSVV
CSSEGRGEEV VWCLDDKANS LVMYHSTTYQ LCARYFCGDP SPLRDMFPVR ALDTEPPEAS
HTANPKVPEG DSIADVSIMY SEELGTQILI HQESLTDYCS MSSYSSSPPC QAARSPSSLP
SSPASSSSVP FSTDCEDSDM LHEPCAASDR SEHDLTPMDG ETFSHHLQAV KILAVRDLIW
VPRRGGDVIV IGLEKDSGAQ RGRVIAVLKA RELTPHGVLV DAAVVAKDTV VCTFENENTE
WCLAVWRGWG AREFDIFYQS YEELGRLEAC ARKRR
//
