ID O73732_XENLA Unreviewed; 1370 AA. AC O73732; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 02-OCT-2024, entry version 160. DE RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568}; GN Name=rock2.L {ECO:0000313|RefSeq:NP_001080945.1, GN ECO:0000313|Xenbase:XB-GENE-959454}; GN Synonyms=rock2 {ECO:0000313|RefSeq:NP_001080945.1, GN ECO:0000313|Xenbase:XB-GENE-959454}, rocka-a GN {ECO:0000313|RefSeq:NP_001080945.1}, xROK GN {ECO:0000313|RefSeq:NP_001080945.1}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAC06351.1}; RN [1] {ECO:0000313|EMBL:AAC06351.1, ECO:0000313|RefSeq:NP_001080945.1} 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). RN [2] {ECO:0000313|RefSeq:NP_001080945.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19924810; RA Reed R.A., Womble M.A., Dush M.K., Tull R.R., Bloom S.K., Morckel A.R., RA Devlin E.W., Nascone-Yoder N.M.; RT "Morphogenesis of the primitive gut tube is generated by Rho/ROCK/myosin RT II-mediated endoderm rearrangements."; RL Dev. Dyn. 238:3111-3125(2009). RN [3] {ECO:0000313|RefSeq:NP_001080945.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22278918; RA Langdon Y., Tandon P., Paden E., Duddy J., Taylor J.M., Conlon F.L.; RT "SHP-2 acts via ROCK to regulate the cardiac actin cytoskeleton."; RL Development 139:948-957(2012). RN [4] {ECO:0000313|RefSeq:NP_001080945.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23278717; RA Terayama K., Kataoka K., Morichika K., Orii H., Watanabe K., Mochii M.; RT "Developmental regulation of locomotive activity in Xenopus primordial germ RT cells."; RL Dev. Growth Differ. 55:217-228(2013). RN [5] {ECO:0000313|RefSeq:NP_001080945.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (JUN-2024) 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|ARBA:ARBA00001433, CC 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|ARBA:ARBA00000775, CC 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: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000256|ARBA:ARBA00004300}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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 EMBL; AF037073; AAC06351.1; -; mRNA. DR RefSeq; NP_001080945.1; NM_001087476.1. DR GeneID; 394289; -. DR KEGG; xla:394289; -. DR AGR; Xenbase:XB-GENE-959454; -. DR CTD; 394289; -. DR Xenbase; XB-GENE-959454; rock2.L. DR OrthoDB; 4221785at2759; -. DR Proteomes; UP000186698; Chromosome 5L. DR Bgee; 394289; Expressed in heart and 19 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0031267; F:small 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:UniProtKB-UniRule. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro. DR CDD; cd20875; C1_ROCK2; 1. DR CDD; cd11638; HR1_ROCK2; 1. DR CDD; cd01242; PH_ROCK; 1. DR CDD; cd22250; ROCK_SBD; 1. DR CDD; cd05621; STKc_ROCK2; 1. DR Gene3D; 1.20.5.340; -; 1. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.20.5.730; Single helix bin; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR046349; C1-like_sf. 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; IPR050839; Rho-assoc_Ser/Thr_Kinase. DR InterPro; IPR020684; ROCK1/ROCK2. DR InterPro; IPR029878; ROCK2_cat. DR InterPro; IPR037311; ROCK2_HR1. DR InterPro; IPR015008; ROCK_Rho-bd_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1. DR PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1. 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; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF103652; G protein-binding domain; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-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; PS51860; REM_1; 1. DR PROSITE; PS51859; RHO_BD; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037568}; KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108}; 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|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR037568}; KW Membrane {ECO:0000256|ARBA:ARBA00022475}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR037568}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR037568}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000186698}; 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 78..340 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 343..411 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT DOMAIN 485..561 FT /note="REM-1" FT /evidence="ECO:0000259|PROSITE:PS51860" FT DOMAIN 967..1035 FT /note="RhoBD" FT /evidence="ECO:0000259|PROSITE:PS51859" FT DOMAIN 1134..1331 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 1242..1297 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT REGION 495..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 524..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1330..1370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 629..1001 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1044..1089 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1347..1363 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 200 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1" FT BINDING 107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" 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 //