COL9A3

COL9A3 (Collagen Type IX Alpha 3 Chain) is a Protein Coding gene. Diseases associated with COL9A3 include Epiphyseal Dysplasia, Multiple, 3 and Intervertebral Disc Disease. Among its related pathways are Integrin Pathway and ERK Signaling. Gene Ontology (GO) annotations related to this gene include extracellular matrix structural constituent conferring tensile strength. An important paralog of this gene is COL9A2.

Full Name

Collagen Type IX Alpha 3 Chain

Function

Structural component of hyaline cartilage and vitreous of the eye.

Biological Process

Collagen fibril organization Source: Reactome
Extracellular matrix organization Source: GO_Central
Female gonad development Source: GO_Central
Male gonad development Source: GO_Central

Cellular Location

Extracellular matrix

Involvement in disease

Multiple epiphyseal dysplasia 3 (EDM3):
A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.
Intervertebral disc disease (IDD):
Disease susceptibility is associated with variants affecting the gene represented in this entry. Susceptibility to intervertebral disk disease is conferred by variant p.Arg103Trp (PubMed:11308397). A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.

PTM

Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.