ID O73732_XENLA Unreviewed; 1370 AA. AC O73732; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 31-JUL-2019, entry version 138. DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568}; GN Name=rock2 {ECO:0000313|Xenbase:XB-GENE-959454}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Xenopus. OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAC06351.1}; RN [1] {ECO:0000313|EMBL:AAC06351.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=9468537; DOI=10.1074/jbc.273.8.4740; RA Farah S., Agazie Y., Ohan N., Ngsee J.K., Liu X.J.; RT "A rho-associated protein kinase, ROKalpha, binds insulin receptor RT substrate-1 and modulates insulin signaling."; RL J. Biol. Chem. 273:4740-4746(1998). 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 EMBL; AF037073; AAC06351.1; -; mRNA. DR RefSeq; NP_001080945.1; NM_001087476.1. DR GeneID; 394289; -. DR KEGG; xla:394289; -. DR CTD; 394289; -. DR Xenbase; XB-GENE-959454; rock2. DR KO; K17388; -. DR OrthoDB; 759391at2759; -. 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:0010825; P:positive regulation of centrosome duplication; IEA:InterPro. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro. DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro. DR CDD; cd00029; C1; 1. DR CDD; cd11638; HR1_ROCK2; 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; IPR037311; ROCK2_HR1. 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR037568, KW ECO:0000256|SAAS:SAAS00593399}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037568}; KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR037568}; KW Kinase {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00593820, KW ECO:0000313|EMBL:AAC06351.1}; 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 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 78 340 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 343 411 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT DOMAIN 1134 1331 PH. {ECO:0000259|PROSITE:PS50003}. FT DOMAIN 1242 1297 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT REGION 495 518 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 524 543 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1330 1370 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 54 74 {ECO:0000256|SAM:Coils}. FT COILED 629 677 {ECO:0000256|SAM:Coils}. FT COILED 682 702 {ECO:0000256|SAM:Coils}. FT COILED 710 790 {ECO:0000256|SAM:Coils}. FT COILED 812 853 {ECO:0000256|SAM:Coils}. FT COILED 868 1001 {ECO:0000256|SAM:Coils}. FT COILED 1044 1089 {ECO:0000256|SAM:Coils}. FT COMPBIAS 1347 1363 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT ACT_SITE 200 200 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR037568-1}. FT BINDING 107 107 ATP. {ECO:0000256|PIRSR:PIRSR037568-2}. SQ SEQUENCE 1370 AA; 159285 MW; 882639150AB6452D CRC64; MSPRQDEYMG TRWQTLEAIL RDPRSPINVE GLLDGLNSIV LDLDFPALRK NKNIDNFLNR YEKIVREVRK LQMKAEDYDV VKVIGRGAFG EVQLVRHKSS QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LFCAFQDEKH LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY TAEVVLALNA IHSMGLIHRD VKPDNMLLDK YGHLKLADFG TCMKMDQTGM VRCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFL FEMLVGDTPF YADSLVGTYS KIMDHKNSLN FPEDVEISAH AKNLICAFLT DREVRLGRNG IEDIKQHPFF KNDQWNWDNI RETVAPVVPE LASDIDTSNF DDIEDDKGDA ETFQIPKAFA GNQLPFVGFT YYRENLLLSE SSQNCKEKKI LCPTNERAVS TSCKKSINKL EEQLHNEMQT KDELEQKFRA VNLRLEKIVK ELDEEASSRK NIESTTRQLE REKALLQHKN TEYQRKAEND ADKKRSLENE VNSLKDQLED MKRRNQNSQI SNEKMNQLQR QLDEANAQLR TESDAAARLR KTQTEMSKQI QQLETNNREF QDKTCMLENA KLKLEKDFIN LQSALESERR DRTQGSEVIS DLQGRISVLE EDLKKGKELL ARADAEKQQL HERLAILEKE KSNMEIDMTY KLKALQQSVE KEESEHKATK ARLADKNKIY QSIEETKSEA MKDMEKKLQE ERVAKQRLEN NLLETEKQYS MLDCDLKQAK QKINELEALK DKLSEDIKNL TLKAEQETQK RSLSQNDLKM QLQQVNCLKM SEKQLKQEVN HLTEIKLNLE KQNNELRKER VDADGQMKEL QDQLEAEQYF STLYKTQVRE LKEECEVKGK MYKEVQQKVQ ELQDERDSLA AQLEITLTKA DSEQLARSIA EEQYSDLEKE KIMKELEIKE MMARHKQELA EKYATITSLE ETNKTLTIDV GNLANEKEDL NNRLKEAHEQ IQRLKEEENS VVTIKTQFEK QLLTERTLKT QAVNKLAEIM NRKLPTKRGP DTDVRRKEKE NRKLQLDLKS EREKFTQLVI KYQREMNDMQ AQIADENQVR IELQMALDSK DSDIEQLRSQ MLGLDSTSIG SGHGDTDAED GFPESRLEGW LSLPLRNAKK FGWNKKYVVV SSRKILFYDS EQDKELSNPS MVLDIDKLFH VRPVTQTDVY RADAKEIPRI FQILYANEGE SKKEQEFQVD PLEKSNYICH KGHEFIPTLY HFPTSCDACM KPLWHMFKPP AALECRRCHI KCHKDHMDKK EEIIAPCKVN YDISTAKNLL LLANSTEEQQ KWVSRLVKKI PKKPPASEHQ ARSSPRPPAK ASLNQSMRRP SRQLPPNKPS //