ID   O73732_XENLA            Unreviewed;      1370 AA.
AC   O73732;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   29-APR-2015, entry version 108.
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: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00128273}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037568};
CC   -!- ENZYME 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   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000256|RuleBase:RU003350}.
CC   -!- SIMILARITY: Contains AGC-kinase C-terminal domain.
CC       {ECO:0000256|SAAS:SAAS00128355}.
CC   -!- SIMILARITY: Contains protein kinase domain.
CC       {ECO:0000256|SAAS:SAAS00105938}.
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   UniGene; Xl.265; -.
DR   ProteinModelPortal; O73732; -.
DR   SMR; O73732; 14-403, 964-1033.
DR   MINT; MINT-1532295; -.
DR   GeneID; 394289; -.
DR   KEGG; xla:394289; -.
DR   CTD; 9475; -.
DR   Xenbase; XB-GENE-959454; rock2.
DR   HOVERGEN; HBG053111; -.
DR   KO; K04514; -.
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: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   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR017892; Pkinase_C.
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; IPR029878; ROCK2.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988:SF24; PTHR22988:SF24; 1.
DR   Pfam; PF02185; HR1; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 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|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00128419};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037568};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR037568};
KW   Kinase {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00128365};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR037568};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00105960};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00128193};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00128360};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00128072}; Zinc {ECO:0000256|SAAS:SAAS00105847};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00128318}.
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
//