ID A0A3Q4GH06_NEOBR Unreviewed; 1361 AA. AC A0A3Q4GH06; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 19-JAN-2022, entry version 15. DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568}; OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Lamprologini; Neolamprologus. OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008196, ECO:0000313|Proteomes:UP000261580}; RN [1] {ECO:0000313|Ensembl:ENSNBRP00000008196} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2019) 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; 32507.XP_006792165.1; -. DR Ensembl; ENSNBRT00000008431; ENSNBRP00000008196; ENSNBRG00000006322. DR GeneTree; ENSGT01030000234517; -. DR OMA; XETLATQ; -. DR Proteomes; UP000261580; Unplaced. 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 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; 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:UP000261580}; 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 473..557 FT /note="REM-1" FT /evidence="ECO:0000259|PROSITE:PS51860" FT DOMAIN 953..1019 FT /note="RhoBD" FT /evidence="ECO:0000259|PROSITE:PS51859" FT DOMAIN 1125..1324 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 1235..1290 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT REGION 557..579 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1020..1039 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1318..1361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 419..488 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 749..790 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 826..846 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 854..895 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 928..976 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1078..1112 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 557..574 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1328..1361 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 1361 AA; 158647 MW; 0DDF7609A6E81E38 CRC64; MSAGDTMEAR 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 DQWTWDNIRE TAAPVVPELS SDTDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFVGFTYY SNQQSLTRWM SATLSDQLKW NVSVQLENLQ KRIYQLEEQL HSEMQLKDEL EQKCRTSNNK IEKIMKELDE EANLRKSAEA SLSLLEKDKL MQQHRFTEYQ RKADQESEKR RNLENEVSNL KEQLEDMKKI SQNSQASNDK ITQLQNQLEE ANDLLRAESD TAGRLRKSHT EMTKSMAHLE NLNRELQERS RAVEGEKAQL EKELLLLQST LDSERRNYSQ DSEEIRELQA RLSGLQEDNK NLKLSLSKME AERKQAQERS NNLEKEKNNL EIDLNYKLKT LQQRLEQEQT EHRVTRAQLT DKYESIEEAK SAAMSGMSQK MSEETGARMR AESRVVEVEK QCSMLEFDLK QSVQKMEQLM KQKERLEDEV KNLQIQVEQE SSKRIQIQND LKTRMQEMDR LRCSEKQLKQ EINTSLESKR SLEFQLAQLS KQYRGNEGQM RELQDQLEAE QYFSTLYKTQ VKELKEEIEE RNRQIQEANK KVQDLCNERD SLSAQLDLTV TKAESEQLAR ALQEEQYFEL SQENKKAVTR HKQEIGEKEA TIARLEESYK TLTKDVENLS REKTDLSEKL RIQDEEYVAQ KEEIEKSIKA NYEKILYTER TLKTQAVNKL AEIMNRKDMK LDQKKKGSTA DLRKKEKENR KLQLELNQEK EKFNHMAIKY QKELSEMQAQ LAEESTYRNE LQMQLDSKES DIEQLREKLN DLQQRMDNSS VTSLQTDETD SNIAESRLEG WLSIPNRANI KRYGWKKQYV VVSSKKILFY NDEQDKEQSN PSMVLDIDKL FHVRPVTQGD VYRAETDEIP RIFQILYANE GECRKEADLE TVPQGDKTNC LPHKGHEFIP TLYHFPSNCE ACAKPLWHVF KPPPALECRR CHVKCHKDHL DKKEDVIAPC KVNYDVTSAR DMLLLALTQD EQKKWIGHLG KKIPKTPPST FTRASPRSMS TRSGPNQSFR KNPKSNTGKL R //