ROR2 contains 9 exons and is 227561 base pairs (via GeneLoc).

Five (5) alternative splice variants have been identified for ROR2.

The ROR2 protein product is 943 amino acids with the molecular weight estimated to be 104.76 kDa.

ROR2 is a developmentally expressed kinase with high expression normally seen throughout the body including the face, limb buds, heart, lungs and brain (Takeuchi et al., 2000; Matsuda et al., 2001). Expression of ROR2 begins to abate at approximately day 16 of development (Yoda et al., 2003).
In adult tissues, ROR2 is normally undetectable or expressed at very low levels. Functional ROR2 expression has been confirmed in the mouse cycling and pregnant uterus (Hatta et al., 2010). In humans, ROR2 cDNA has been detected in the uterus as well as the parathyroid and testis (Katoh et al., 2005). ROR2 has further been found to be upregulated as pluripotent cells emerge as pre-osteoblasts, and to be downregulated again as cells differentiate into osteocytes (Billiard et al., 2005).

ROR2 is a single-pass type I membrane protein (Masiakowski et al., 1992) with localization restricted to the membrane.

ROR2 is a tyrosine protein kinase receptor highly implicated in development. It has also been implicated in the early formation of chondrocytes (DeChiara et al., 2000; Takeuchi et al., 2000). ROR2 is thought to play a key role in cartilage and growth plate development (DeChiara et al., 2000). The Wnt signaling pathway has also emerged as a key target of ROR2 activity. More specifically, evidence suggests that Wnt5a utilizes ROR2 as a receptor or co-receptor for its noncanonical Wnt mediated signaling (Minami et al., 2010; Sato et al., 2010). Additionally, recent evidence suggests that ROR2 is expressed and plays a role in various cancer etiologies including gastric cancer, renal cell carcinoma, malignant melanoma, and prostate cancer.

ROR2 is highly conserved across several species - from C. elegans to D. melanogaster to M. musculus to H. sapiens. For example, there is a 92% amino acid identity between mouse and human ROR2 (Yoda et al., 2003).

Robinow syndrome and Brachydactyl type B (BDB) are two genetic disorders that arise from mutations in ROR2:
1) Robinow syndrome is an autosomal recessive disorder that arises from nonsense, missense and frameshift mutations in the kringle, CRD and kinase domains - and is thought to cause a loss of function of ROR2 (Afzal et al., 2000). Those that present with Robinow syndrome have skeletal development defects (van Bokhoven et al., 2000; Afzal et al., 2003; Schwabe et al., 2004). This is seen within developmentally regulated features such as the formation of bones in the face and limbs.
2) BDB is an autosomal dominant disorder that arises from truncations of the kinase domains - either truncation of the serine/threonine domains and proline rich domain just below the Tyr kinase domain; or truncation of the entire intracellular domain right just below the transmembrane domain (Oldridge et al., 2000). Patients that present with BDB have abnormally short digits with the 4^th and 5^th digits particularly affected and have malformed or absent finger and toe nails (Schwabe et al., 2000; Afzal et al., 2003).

Kubo et al. has reported somatic mutations in ROR2 in invasive gastric cancers (Kubo et al., 2009).