ID H3AV73_LATCH Unreviewed; 2508 AA.
AC H3AV73;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:ENSLACP00000013544.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013544.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013544.1}
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 EMBL; AFYH01125579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000013544; -.
DR Ensembl; ENSLACT00000013640.1; ENSLACP00000013544.1; ENSLACG00000011925.1.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158267; -.
DR HOGENOM; CLU_000815_0_0_1; -.
DR InParanoid; H3AV73; -.
DR OMA; FIVECMV; -.
DR TreeFam; TF313679; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000011925; Expressed in muscle tissue and 4 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-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
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; IPR025875; Leu-rich_rpt_4.
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; 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; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR Pfam; PF19056; WD40_2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 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; 3.
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 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:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1310..1492
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1808..2117
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 868..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2508 AA; 283457 MW; 70C418382C28358E CRC64;
MADGEKLEDN LKKLIVRLKN VQEGKEVDTV VQILEDLLAL TFVDFASELF EDKNTQMPLL
VVLDSYITVP VIQQQIGWSL LCRLIEIHPT IVDNLAGPQD VGKDWDVLGV HQQILKMLST
YNAKDELMTV GLQALAGLLK SDKIALLLLE EEAADIFFLV IEAMRIFSAN DIQKFGCQAL
QILLQKVPDE QLIEFVESKD HTVILNALKQ FEDNEEIVLN ALCALLPLAG PSSNVEVLMS
GSEKCYNLVV NAMMKFPDSE KVQEIGCCIF QKFTVGNFYN ILVLNGAQEV LVKAVMRDPA
NAKLQKAALS SLALLTEAIV LNKDLEERKD EDDLCWLEAS CKALELHRVN VDVQEAACWA
LNNLLIYQHD LPEKIGDEDK EDLVHRHVMT AMLLHSSSKE VFQAAASALA TLSEQSVVIR
KLLLAKGIHI NTLDIMKKHL NSSDVAESAC KLLNRLFQGS ILNLDVMTLA LSGIISAMRK
HESVSSVQLE ALRVILHFTH TGLTRNTLND VQNMIFLQII KNQCLLEGAH VLVLEALNKF
IGNPAIQKCG LKILHSVAEC SGAIGLLTQQ GASDTVLHSL QMYPDNQEIQ LIGLSLLRCL
ISKKNLSAAS LYLLATVFVA ALRRFENVVE IQIQGLCAAL TLLELSQNAA NVLEQESFET
ILFHQMTIWF TEKRDQQFQS LCCRCLAKMS DDNEIKHKML EKACVENNVI MAECLLLLGA
DVNKKTKTNS LIYQVCEKGN NPCLVEVVLN GAREQDVRKA LSISIKRGDS RIINLLLKKL
GLDRTNNSIC LGGFRLGKIE PSWLSPLFPE NKSPNLRRQT SAGGTLARMV LRYQMKQSSD
VRCSDDEEPA VRSGDWIILP DPHLDSGFYI SEDNDSDGSE SSVFGRRISN SIPVSEPHRD
SGKRENIFAK QRSHNPLNPD GDAEPVVRQQ RNLFQSSSSI PRSPILPSLS KRSESYSSLS
FEREFIKSLD LSANELENVD SISQTCCLTD HLEHLQKLEL HQNNLTEFSQ HLCETLKCLA
YLDLHSNKFT TFPSCLLEMH CIAYLDVSRN DIGPSLTLDL RIRCPTLKQF SISYNQLVVF
PESLVSAANK LEELHLEGNK ISEINYLLCL TELRLLSLNN NNISAISENF LINCPKMETL
TASTNFLSAL PILPSKITTL KLSHNKFTKI SEAILCLPHL RTLDLSNNEI GELPGPVHWE
SLNLRELILN CNKISVLDLS KEAYKWSRLE KLHLSNNKLK EIPPQIGQLA NITSLDVSYN
PDLRSFPNEI GKLIKVWDLP LDGLHLDLDL KHIGSKTKDI IRFLQQRLKK SVPYYRMKLM
IVGNAGSGKT TLLQHLMRCK HSDVREKATV GIDVKDWVIP VKVKVKKELI LNVWDFAGQE
EFYSTHPHFM TQRALYLVVY DLSKGATEVD AIKPWLFNIK ARASSSPVIL VGTHLDVSDE
KQRKACSIKI TKELFHQRGF PTIRDFHCVN ATEESDSLGK LRKTIVMESL NFKIRDQPVM
GQLIPDSYLE LEKRILKERK NVPTEFPVVS HHRLLELVQL SQLELDENEL PHAVHFLNES
GVLLHFEDPA LQLRDLYFVE PQWLCKMMAQ ILTMKLRGFQ KYPKGIIQRS DVEKFLSQKS
VFPKNYMCQY FKLLEKFQIA LPLGEEQLLV PSSLSDQRPV IDLPYCENSE ITVRLYEMPY
FPMGFWSRLI NRLLEISPYM LSGRATERAV RPNRIYWRQG IYLNWSPEAY CLVESAVLDN
KTESYLKITV PCRRKGFILL GQVVDHIDSL MEEWFPGLLE TDVCGEGETL LKKWALYSFE
DGQDYEKILL DELLQKAKEG DVLVNPNDAR LRIPIAQIAP DLVLADLPRN IMLNNDELEI
DQTPEFLLVD NTFLSLQKAI YKTVLFFNKR ISLLFVVQEL AVLSHLHHPS LISLLAAGVR
PRMLVMELAP KGSLDHFLQH DKVNITRTLQ HRIALHVADG LRYLHSSMII YRDLKPHNVL
LFTLYPNSAI IAKIADYGIA QYCCRMGIKT SEGTPGFRAP EVARGNVIYN QQADIYSFGL
LLYDILTAGD RILAGIKYPN EFDEMAIQGK LPDPVKEYHC SPWPGVQSLI KDCLKENPEE
RPTSAQVFVF LNSAELLCLM KEVLLPTSWA AECMVATHYT SKKPGIWIGN GKRDVAQLTF
LHTDTGGHSI EDIGESRILC LVLVSLPDEK ENWILAGTQS GSLLVINSED MKNNHQLKRM
SDSVTCLFCP SHSRHSKERK FVLVGTADGK LAIFEDTAIK CKDAEPIKIV SIGNISTPLM
CLNESLYSSE KDTIWAGCGT NIISFSSDFS IQKSIDTKNR QLFLQKSFPN SNIITMAIDK
YIYFAKKDSH FVEIWDKKAE KPCELLDCAH FLKIKAAKLN ERKVNEVFHS ARVKVLYLQK
NTALWVGTGG GHVLLIDLSK CWPIRIISQL CDSIRSMVTT QVEKGSPKNV MLILGNTYKS
SHDTQQPKEV QSHLFVWDIN LPHEIQNLEK HIELRQEMAD KMKSCSFE
//
