ID   2.7.11.39
DE   ROCK-subfamily protein kinase.
AN   Rho kinase.
CA   (1) L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).
CA   (2) L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP +
CA   H(+).
CC   -!- The enzyme has wide range known substrates, mostly involved in
CC       cytoskeletal regulation, with a preference for positive charges at P1
CC       to P5.
CC   -!- Requires Mg(2+).
CC   -!- An animal specific kinase that is duplicated in vertebrates (ROCK1,
CC       ROCK2), and with homologs in Drosophila (rok) and Caenorhabditis
CC       elegans (let-502). They are ~1300 amino-acid proteins, with an
CC       N-terminal kinase domain, with the AGC-specific kinase domain tail,
CC       followed by a central coiled-coil region, HR1 domain, Rho-binding
CC       domain (RBD), and PH domain. The PH domain is split by an inserted
CC       CRD (cysteine-rich Zn finger motif).
CC   -!- ROCK is activated by the small GTPase Rho and modulates the
CC       cytoskeleton by phosphorylation of a wide array of other cytoskeletal
CC       proteins. Binding of Rho-GTP to the RBD relieves an intramolecular
CC       inhibition and activates the kinase activity. These kinases modulate
CC       the cytoskeleton in response to Rho GTPase signaling.
CC   -!- Substrates include LIM-kinase (LIMK) which phosphorylates and
CC       inhibits cofilin, blocking its actin-depolymerizing function,
CC       and myosin regulatory light chain (MRLC2/MYL12B) that regulates
CC       Myosin II.
CC   -!- In Drosophila it is involved in the planar cell polarity pathway,
CC       where it is genetically downstream of frizzled and disheveled gene
CC       families, and phosphorylates the non-muscle myosin light chain,
CC       regulating Myosin II. It is activated by Rho1, the single homolog of
CC       human RhoA/B/C, which also activate ROCK.
DR   Q8MIT6, ROCK1_BOVIN;  Q13464, ROCK1_HUMAN;  P70335, ROCK1_MOUSE;
DR   P61584, ROCK1_PANTR;  O77819, ROCK1_RABIT;  Q63644, ROCK1_RAT  ;
DR   Q28021, ROCK2_BOVIN;  O75116, ROCK2_HUMAN;  P70336, ROCK2_MOUSE;
DR   M3TYT0, ROCK2_PIG  ;  Q62868, ROCK2_RAT  ;
//