Citron Rho-interacting kinase is an enzyme that in humans is encoded by the CIT gene.
Citron is a 183 kDa protein that contains a C6H2 zinc finger, a PH domain, and a long coiled-coil forming region including 4 leucine zippers and a rho/rac binding site. It was discovered as a rho/rac effector in 1995, interacting only with the GTP bound forms of rho and rac 1. Displaying a distinctive protein organization, this protein defines a separate class of rho partners. Using a cloning approach based on the polymerase chain reaction (PCR), a splice variant of citron, citron kinase (citron-K) has been identified with an alternative amino terminus. This N-terminal extension contains a protein kinase domain that has approximately 50% sequence identity to the sequences of ROCK, ROK, myotonic dystrophy protein kinase (MDPK) and the Cdc42 effector known as MRCK or GEK. Citron kinase, which resembles the ROCK family of kinases and by comparison to it, is therefore a multiple domain protein containing an N-terminal kinase domain, an internal coiled-coil (CC) domain with Rho/Rac interacting site, and a C-terminal region consisting of a Zn finger, a pleckstrin homology (PH) domain, a Citron homology domain (CNH), a putative SH3 binding domain, and a PDZ-targeting motif. Its fly (Drosophila) ortholog is called Sticky. the importance of different domains of citron-K in its localization at different stages is discussed below.