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Proline-rich protein 29, encoded by the PRR29 gene in humans, is a protein whose function is not fully understood. It is located in the human genome at 17q23. Its name is derived from the chain of 5 proline amino acids located toward the end of the protein. The primary domain within the sequence of this protein is known as DUF4587. It is reported to have high levels of expression in tissues pertaining to the circulatory system and the immune system. It is hypothesized that PRR29 is a nuclear protein that facilitates communication between the nucleus and the mitochondria.

Isoforms
There are 4 known isoforms of PRR29.

Paralogs
PRR29 does not have any known paralogs.

Orthologs
This gene has orthologs in other animal species. It has only been found in vertebrates with the oldest being the whitespotted bamboo shark.

Evolution
This gene evolves at a rate higher than that of cytochrome c but lower than that of fibrinogen alpha chain.

Gene
The human gene for PRR29, also referred to as C17of72 spans 6 exons and is located at the genomic coordinates chr17:63,998,351-64,002,516 on the positive DNA strand (hg38). It is 4,166 base pairs in length including introns. After they have been removed, the length is shortened to 3,611 base pairs.

Expression
Its expression is concentrated in related tissues including the spleen, lungs, white blood cells, and heart. In situ hybridization data reveals that expression in the human brain is brain is relatively low in the forebrain but higher in the basal ganglia, midbrain, and hindbrain with the exception of the cerebellar cortex. For comparison, expression in the mouse brain is focused in the isocortex, olfactory region, hippocampus, cortical subplate, and cerebellum.

Transcript-Level Regulation
Prediction of transcription factors that bind to the promoter region for PRR29 include ones involved with the activation of leukocytes and the formation of blood cells. Abundance of the protein relative to others found in the human body is currently unknown.

Physical Properties
The PRR29 protein is estimated to have a molecular weight of 20.7 kDa. Its isoelectric point is predicted to lie at 4.83.

Domains and Motifs
The primary domain of the protein, DUF4587, spans amino acid 39 to 112. It contains one proline-rich region motif that extends from amino acid 39 to 107.

Secondary and Tertiary Structure
The secondary structure is characterized by high confidence in the presence of an alpha helix from amino acid 43 to 70 with the rest consisting of coils. In terms of tertiary structure, predictive tools returned low confidence in all sections of the protein besides the core alpha helix.

Untranslated Regions
The secondary structure of the 5' UTR of PRR29 consists of a singular stem-loop that is almost wholly conserved between orthologs. The 3' UTR is much longer, containing 41 different stem loops in its secondary structure. Any predicted miRNA binding to PRR29 is believed to be nonfunctional. === Sub-Cellular Localization Data on localization of PRR29 within cells shows that it is primarily found in the nucleus, followed by the mitochondria and cytoplasm.

Post-Translational Modification
The most common types of post-translational modification that occur for this protein are phosphorylation, glycosylation, hydroxylation, and sumoylation. They contribute to the stability, structure, and folding of the protein.

Pathology
It is unknown if PRR29 is directly linked to any diseases.

Disease Association
Experiments have been performed on tissue and cell samples in order to observe any potential changes in expression of the protein under different conditions. Samples inflicted with pulmonary sarcoidosis and small cell lung cancer did not experience and significant changes in expression compared to normal cells. Intracranial artery aneurysm did induce change, leading to heightened expression.