ID A0A3Q4GH06_NEOBR Unreviewed; 1361 AA. AC A0A3Q4GH06; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 16-OCT-2019, entry version 6. 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, ECO:0000313|Proteomes:UP000261580} RP NUCLEOTIDE SEQUENCE. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSNBRP00000008196, ECO:0000313|Proteomes:UP000261580} RP NUCLEOTIDE SEQUENCE. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). RN [3] {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 CC cytoskeleton and cell polarity. {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|PIRNR:PIRNR037568}; CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y- CC 27632. {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000256|PIRNR:PIRNR037568, CC ECO:0000256|SAAS:SAAS00784564}. 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 Ensembl; ENSNBRT00000008431; ENSNBRP00000008196; ENSNBRG00000006322. DR GeneTree; ENSGT00950000182698; -. DR Proteomes; UP000261580; Whole Genome Shotgun Assembly. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0017048; F:Rho 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:0035556; P:intracellular signal transduction; IEA:InterPro. 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 CDD; cd00029; C1; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR000961; AGC-kinase_C. 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; IPR015008; Rho-bd_dom. DR InterPro; IPR020684; ROCK1/ROCK2. 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; PS50081; ZF_DAG_PE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593399}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000261580}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037568}; KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR037568}; KW Kinase {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00593820}; KW Magnesium {ECO:0000256|PIRNR:PIRNR037568}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00253054}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593601}; KW Reference proteome {ECO:0000313|Proteomes:UP000261580}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593706}; KW Transferase {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00592725}; Zinc {ECO:0000256|SAAS:SAAS00253075}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00795753}. FT DOMAIN 76 338 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 341 409 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT DOMAIN 1125 1324 PH. {ECO:0000259|PROSITE:PS50003}. FT DOMAIN 1235 1290 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT REGION 557 579 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1020 1039 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1318 1361 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 419 488 {ECO:0000256|SAM:Coils}. FT COILED 749 790 {ECO:0000256|SAM:Coils}. FT COILED 826 846 {ECO:0000256|SAM:Coils}. FT COILED 854 895 {ECO:0000256|SAM:Coils}. FT COILED 928 976 {ECO:0000256|SAM:Coils}. FT COILED 1078 1112 {ECO:0000256|SAM:Coils}. FT COMPBIAS 557 574 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 1328 1361 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT ACT_SITE 198 198 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR037568-1}. FT BINDING 105 105 ATP. {ECO:0000256|PIRSR:PIRSR037568-2}. 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 //