ID O73732_XENLA Unreviewed; 1370 AA. AC O73732; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 01-MAY-2013, entry version 92. DE SubName: Full=Rho-associated kinase alpha; GN Name=rock2; 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; RN [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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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 HSSP; Q28021; 1UIX. DR ProteinModelPortal; O73732; -. DR SMR; O73732; 14-403, 964-1033. 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:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; 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; IPR011993; PH_like_dom. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR001849; Pleckstrin_homology. DR InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR020684; Rho-assoc_coiled-coil_kin. DR InterPro; IPR015008; Rho-bd_dom. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22988:SF3; PTHR22988:SF3; 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; Kinase_like; 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; Kinase; Metal-binding; Nucleotide-binding; KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 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 //