ID G9KLM5_MUSPF Unreviewed; 1343 AA. AC G9KLM5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-AUG-2020, entry version 48. DE RecName: Full=Rho-associated protein kinase 2 {ECO:0000256|ARBA:ARBA00014021}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2 {ECO:0000256|ARBA:ARBA00020596}; DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase II {ECO:0000256|ARBA:ARBA00021066}; DE AltName: Full=p164 ROCK-2 {ECO:0000256|ARBA:ARBA00016665}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae; OC Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES05804.1}; RN [1] {ECO:0000313|EMBL:AES05804.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES05804.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M., RA Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(2013). 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 -!- 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; 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 --------------------------------------------------------------------------- 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; JP017206; AES05804.1; -; mRNA. 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|ARBA:ARBA00022840}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AES05804.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022771}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 45..310 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 313..381 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT DOMAIN 1106..1305 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 1216..1271 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT REGION 1301..1343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 405..509 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 513..561 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 569..589 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 597..645 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 650..716 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 724..758 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 766..821 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 836..965 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1012..1057 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1319..1343 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 170 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1" FT BINDING 77 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AES05804.1" FT NON_TER 1343 FT /evidence="ECO:0000313|EMBL:AES05804.1" SQ SEQUENCE 1343 AA; 156053 MW; A9B0684385E5043D CRC64; DGLNSLVLDL DFPALRKNKN IDNFLNRYEK IVKKIRGLQM KAEDYDVVKV IGRGAFGEVQ EVQLVRHKAS QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LFCAFQDDKY LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY TAEVVLALDA IHSMGLIHRD VKPDNMLLDK HGHLKLADFG TCMKMDETGM VHCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFL FEMLVGDTPF YADSLVGTYS KIMDHKNSLC FPEDAEISKH AKNLICAFLT DREVRLGRNG VEEIKQHPFF KNDQWNWDNI RETAAPVVPE LSSDIDSSNF DDIEDDKGDV ETFPIPKAFV GNQLPFIGFT YYRENLLLSD SSPCRENDSV QSRKNEESQE IQKKLYTLEE HLSTEMQAKE ELEQKCKSVN TRLEKVAKEL EEEITLRKSV ESALRQLERE KALLQHKNAE YQRKADHEAD KKRNLENDVN SLKDQLEDLK KRNQNSQIST EKVNQLQRQL DETNALLRTE SDTAARLRKT QAESSKQIQQ LESNNRDLQD KNCLLETAKL KLEKEFMNLQ SVLESERRDR THGSEIINDL QGRISGLEED LKNGKTLLAK AEMEKRQLQE KLTDLEKEKN NMEIDMTYQL KVIQQSLEQE EAEHKATKAR LADKNKIYES IEEAKSEAMK EMEKKLSEER TLKQKVENLL LEAEKRCSIF DCDLKQSQQK INELLKQKDV LNEDVRNLTL KIEQETQKRC LTQNDLKMQT QQVNTLKMSE KQLKQENNHL MEMKMSLEKQ NAELRKERQD ADGQMKELQD QLEAEQYFST LYKTQVRELK EECEEKTKLC KELQQKKQDL QEERDSLAAQ LEITLTKADS EQLARSIAEE QYSDLEKEKI MKELEIKEMM ARHKQELTEK DATIASLEET NRTLTSDVAN LANEKEELNN KLKDAQEQLS RLKDEEISAA AIKAQFEKQL LTERTLKTQA VNKLAEIMNR KEPVKRGSDT DVRRKEKENR KLHMELKSER EKLTQQMIKY QKELNEMQAQ IAEESQIRIE LQMTLDSKDS DIEQLRSQLQ ALHIGLDSSS IGSGPGDAEA DDGFPESRLE GWLSLPVRNN TKKFGWVKKY VIVSSKKILF YDSEQDKEQS NPYMVLDIDK LFHVRPVTQT DVYRADAKEI PRIFQILYAN EGESKKEQEF PVEPVGEKSN YICHKGHEFI PTLYHFPTNC EACMKPLWHM FKPPPALECR RCHIKCHKDH MDKKEEIIAP CKVYYDISTA KNLLLLANST EEQQKWVSRL VKKIPKKPPA PDPFARSSPR TSMKIQQNQS IRRPSRQLAP NKP //