ID A0A3P8RM62_AMPPE Unreviewed; 1364 AA. AC A0A3P8RM62; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 19-JAN-2022, entry version 16. DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568}; OS Amphiprion percula (Orange clownfish) (Lutjanus percula). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Pomacentridae; Amphiprion. OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000001286, ECO:0000313|Proteomes:UP000265080}; RN [1] {ECO:0000313|Ensembl:ENSAPEP00000001286, ECO:0000313|Proteomes:UP000265080} RP NUCLEOTIDE SEQUENCE. RA Lehmann R.; RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome RT of the orange clownfish Amphiprion percula."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPEP00000001286} RP IDENTIFICATION. RG Ensembl; RL Submitted (DEC-2018) to UniProtKB. CC -!- FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton CC and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}. 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|PIRNR:PIRNR037568}; 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|PIRNR:PIRNR037568}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRNR:PIRNR037568}; CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632. CC {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903, CC ECO:0000256|PIRNR:PIRNR037568}. 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 STRING; 161767.ENSAPEP00000001286; -. DR Ensembl; ENSAPET00000001319; ENSAPEP00000001286; ENSAPEG00000000855. DR GeneTree; ENSGT01030000234517; -. DR OMA; XETLATQ; -. DR Proteomes; UP000265080; Chromosome 10. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0003347; P:epicardial cell to mesenchymal cell transition; IEA:Ensembl. DR GO; GO:1903392; P:negative regulation of adherens junction organization; IEA:Ensembl. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule. DR CDD; cd00029; C1; 1. DR CDD; cd11639; HR1_ROCK1; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011072; HR1_rho-bd. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR020684; ROCK1/ROCK2. DR InterPro; IPR037310; ROCK1_HR1. DR InterPro; IPR015008; ROCK_Rho-bd_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08912; Rho_Binding; 1. DR PIRSF; PIRSF037568; Rho_kinase; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS51860; REM_1; 1. DR PROSITE; PS51859; RHO_BD; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037568}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE- KW ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, KW ECO:0000256|PIRNR:PIRNR037568}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037568}; KW Magnesium {ECO:0000256|PIRNR:PIRNR037568}; KW Membrane {ECO:0000256|ARBA:ARBA00022475}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037568}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR037568}; KW Reference proteome {ECO:0000313|Proteomes:UP000265080}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR037568}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037568}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 76..338 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 341..409 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT DOMAIN 476..560 FT /note="REM-1" FT /evidence="ECO:0000259|PROSITE:PS51860" FT DOMAIN 956..1022 FT /note="RhoBD" FT /evidence="ECO:0000259|PROSITE:PS51859" FT DOMAIN 1128..1327 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 1238..1293 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT REGION 407..429 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 568..598 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1321..1364 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 752..786 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 801..849 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 857..898 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 931..993 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1028..1073 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1081..1115 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1331..1364 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 198 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1" FT BINDING 105 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1364 AA; 158462 MW; 663C897E2637FB85 CRC64; MSAGESMEAR FEKIDAMLKD PKSEINTDCL LDGLDALVYD LDFPALRKNK SIDNFLNRYK ETISKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKATSK VYAMKLLSKF EMIKRSDSAF FWEERDIMAF ANSSWVVQLF FAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA EVVLALDGIH SMGFIHRDVK PDNMLLDKAG HLKLADFGTC MKMNKDGMVR CDTAVGTPDY ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNALTFP DDSDISNDAK NLICAFLTDR EVRLGRNGVD EIKRHPFFKN DQWTWENIRE TAAPVVPELS SDIDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFVGFTYY SNQHPLRSST ATKTSDKRSS STKEDKSHLE NLQKRIYQLE EQLHSEMQLK DELEQKCRTS NTKIEKIMKE LDEEANLRKS AEASVSLLEK DKIMLQHRFT EYQRKADQEA EKRRNLENEV STLKEQLEDM KKISQNSQAS NDKIAQLQSQ LEEANDLLRA ESDTAARLRK SHTEVAKSMS QLESLNRDLQ ERSRAADGEK AQLEKELLLL QSTLDSERRN YSQGSEEIRE LQARMAGLQE DNKNLKLSLS KVETERKQAQ ERSNNLEKEK NNLEIDLNYK LKTLQQRLEQ EHTEHRVTRA QLTDKYESIE EAKSAAMTAV QQKMSEENGA RMRAESRVVE VEKQCSMLEF DLKQSVQKME QLMKQKERLE DEVKILRIQV EQESSKRGLT QNELKSRMQE VDRLRCSEKQ LKQEINTALE SKRSLEFQLA QLTKQYRGNE GQMRELQDQL EAEQYFSTLY KTQVKELKEE IEERNRQVQE AHKRMQDLNS ERDSLSAQLD LTVTKAESEQ LARALQEEQY FELSQENKKA VTRHKQEIGE KESTITRLEE SNKTLTKDVE NLSKEKTELN EKLRTQEEEY AAQKEEIANT IKANYEKVLN TERTLKTQAV NKLAEIMNRK DMKLDQKKKG STADLRKKEK ENRKLQLELN QEKEKFNHMA IKYQKELSEM QAQLSEECTY RNELQMQLDS KESDIEQLRE KLNDLQQRMD NSSVTSLQTD ETDSNIAESR LEGWLSIPNR ANIKRYGWKK QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPRIFQILY ANEGECRKEA EMETVPQGDK TNCLPHKGHE FIPTLYHFPS NCEACAKPLW HVFKPPPALE CRRCHVKCHK DHLDKKEDVI PPCKVNYDVT SARDMLLLAL TQDEQKKWIG HLGKKIPKTP PSTFSRASPR SMSTRSGPNQ SFRKNPKSNT GKLS //