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Database: UniProt
Entry: A0A452FK84_CAPHI
LinkDB: A0A452FK84_CAPHI
Original site: A0A452FK84_CAPHI 
ID   A0A452FK84_CAPHI        Unreviewed;      2487 AA.
AC   A0A452FK84;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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:ENSCHIP00000024800.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000024800.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000024800.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000024800.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   EMBL; LWLT01000005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017903409.1; XM_018047920.1.
DR   Ensembl; ENSCHIT00000032662.1; ENSCHIP00000024800.1; ENSCHIG00000021778.1.
DR   GeneID; 102188019; -.
DR   CTD; 120892; -.
DR   GeneTree; ENSGT00940000158267; -.
DR   OMA; FIVECMV; -.
DR   OrthoDB; 148126at2759; -.
DR   Proteomes; UP000291000; Chromosome 5.
DR   Bgee; ENSCHIG00000021778; Expressed in spleen and 16 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
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; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00364; LRR_BAC; 8.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; ARM 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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          1288..1471
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1839..2098
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          280..307
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         1866
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2487 AA;  281790 MW;  7D3AABFC9C422412 CRC64;
     MASGSCQGCE EEDEESLKKL IVRLNNVQEG KQIETLVQIL EDMLVFTYAD HASKLFQDKN
     VHVPLLIVLD SYMRVASVQQ VGWSLLCKLI EICPNTMQSL MGPHDIGHDW EVLGVHQLIL
     KMLTVHNASV NLTTVGLKAL DLLLNSGKIT LLILDEENDI FLLIFDAMRT FAASDEVQKL
     GCKVLHVLFE RVSEEQLTEF VENKDYMILL SALKNFEDEE EIVLHVLHCL HSLAIPCSNV
     EVLMSGNVRC YNIVVEAMKA FPISEKIQEV SCCLLHRLTL AETIFLNQDL EEKNENQEND
     DDEEDKLFWL EACYKALTWH RKNKHVQEAA CWALNNLLMY QNSLHEKIGD EDGQFPAHRE
     VMLSMLMHSS SKEVFQASAN ALSTLLEQNV NFRKILLSKG IYLNVLELMQ KHMHSPEVAE
     SGCKMLNHLF EESSTSLDTM AAVVPKIITV MKSHETSLSV QLEALRAMLH FIVPGIPEEY
     REDTEYQHKL NMIEKQCFRN DIHKLVLGAL NRFIGNPGIQ KCGLKVISSI IHFPDALEVL
     SLEGAIDSVL HTLQMYPDDQ EIQCLGLSLI GCLITKKNLC MGTGHLLAKI LISTLQRFKD
     IGEVQIKGFQ TVLTILELSV SFSKLLVDYS FDSVIFHQLS SSIMEQKDQQ FLNLCCKCFA
     KLAVDNELKS VMLEKACDQN NSIMVECLLL LGADANRAKE ATSLICQVCE KASSPKLVEL
     LLNSGSREQD VRKALTISIG KGNSQIISLL LRRLALDLAN SSICLGGFCM GKIDPSWLGP
     LFPDKTSYLR KETNIGSTLA RMVLRYQMKS SVEEGAGSGS NGNFSEEIVD KFDEWTFIPE
     SYVDSVFGQS DDLDSEGSEG SFLVKKKSNS ISVGEFYRDP ALQRCSPNLQ RHSSSLGPIF
     DHEDLIKRKR KIFSSDDSLR ASKFQSHMKH SESMSSLPSE REYITSLDLS ANELRDVDAL
     SQNSCISGHL EHLEKLELHQ NALTSFPQQL CETLKCLTHL DLHSNKFTSF PTYLLKMNCI
     ASLDVSRNDI GPSVVLDPAV KCPTLKQFNL SYNQISSLPD NIGDVVEKLE QLILEGNKIS
     EICSPLSLKE LKILNLSKNH ISSLSEDFLE TCPKLEILSA KMNFLAAMPF LPSSITSLKL
     SQNRFTCVPE AILHLPHLRS LDMSSNDIRY LPGPVHWRSL NLRELLFSHN QISILDLSEK
     ACAWSRIEKL HLSHNKLKEI PPEIGCLENL TSLDVSYNLD LRSFPNEMGK LSKIWDLPLD
     ELHLNFDFKH VGCKAKDIIR FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLMKIKKS
     DLGMQGATVG IDVKDWPIQI RGKGKKDLIL NVWDFAGREE FYSTHPHFMT QRALYLAVYD
     LSKGQAEVDA MKPWLFNIKA RASSSPVILV GTHLDVTDEK QRKACISKIT KELLNKRGFP
     AIRDYHFVNA TEESDALAKL RKTIINESLN FKIRDQPVVG QLIPDCYVEL ERIILSERKN
     VPIEFPVIDR KRLLQLVREH QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP
     KWLCKVMAQI LTVKVEGFPK HPKGIISRRD VEKFLSKKKR FPKNYMAQYF KLLEKFQIAL
     PIGEEYLLVP SSLSDHRPVI ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPYML
     SGRERALRPN RMYWRQGIYL NWSPEAYCLV GSEVLDHHPE SFLKITVPSC RKGCILLGQV
     VDHIDSLMEE WFPGLLEIDI CGEGETLLKK WALYSFNDGE EHQKILLDNL MKKAEEGDLL
     VNPDQPRLTI PISQIAPDLI LADLPRNIML NNDELEFEQA PEFLLGDGSF GSVYRAAYQG
     EEVAVKIFNK HTSLRLLRQE LVVLCHLHHP SLISLLAAGI RPRMLVMELA SKGSLDRLLQ
     QDKTSLTRTL QHRIVLHVAD GLRYLHSAMI IYRDLKPHNV LLFTLYPNAA IIAKIADYGI
     AQYCCRMGIK TSEGTPGFRA PEVARGNVIY NQQADVYSFG LLLYDILTTG GRIAEGLKFP
     NEFDELAIQG KLPDPVKEYG CAPWPMVEKL IKRCLKENPQ ERPTSAQVFD ILNSAELICL
     MRRISIPKSF TVECMVATNH NSKNVKIWLG CGHTDKGQLS FLDLNTERYT SEEVTDSRIL
     CLALVYLPVE KESWIVSGTQ SGMLLVINTE DGRKRHTLEK MTDSVTCLYC NSFSKQSKQK
     NFLLVGTADG NLAIFEGKTV KCKGASPLKI LNIGNVSTPL MCLSESVNLT EKNIMWGGCG
     TKVFSFSDDF TIQKLIETRT NQRFSYASFC DSNIIAVVVD TALYVAKKNS PFVEVWDKKT
     EKLCELIDCV HFLKEELVRV SKELKHKMSY SGRVKTLCLQ KNTALWIGTG GGHILLLDLS
     TRRIIRIIHN FYDSVRVMMT AQLGSLKNVM LVLGYNRKSA EGTQHQKEIQ SCLSVWDINL
     PHEVQNLEKH IEVRKELAEK MRRISVE
//
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