FAM222A
Family with sequence similarity 222 member A is a protein of unknown function. In humans it is encoded by the gene FAM222A. Aggregatin's cellular function is not well understood, however it has been implicated in Alzheimer's disease.[5] GeneFAM222A is also called C12orf34.[6] It is located on chromosome 12 at q24.11.[7] It encompasses 56,672 bp.[7] The mRNA is 3,685 bp while the coding region is 1,359 bp.[7] FAM222A is highly expressed in the brain and spinal cord.[8] It is expressed to a lesser extent in the cerebellum, pituitary gland, adrenal gland and testis.[8] mRNAIt has 3 different splice variants of mRNA.[6] The most common mRNA is 3,685 bp while the coding region is 1,359 bp.[6] The mRNA consists of three exons and has two different isoforms in humans. The Kozak Sequence is not very well conserved in FAM222A and it has a non-canonical polyadenylation site. ProteinFAM222A is a protein made of 452 amino acids.[7] It contains a domain of unknown function called pfam15258 which is 200 amino acids long.[7] It has been found to be part of protein plaques formed in the brains of patients with Alzheimer's disease.[5]  FAM222A has an unusually high amount of prolines with a 6 segment run from amino acids 392 to 397. Structurally, FAM222A has 5 domains which are connected by linker regions.[9][10] Analysis of the amino acid sequence suggests that FAM222A is localized in the nucleus.[11] Expression and regulationFAM222A is highly expressed in the brain and to a lesser extent in the adrenal glands.[8][12] Alzheimer’s disease seems to cause an increase in FAM222A in the brain, but other degenerative diseases such as Parkinson’s do not.[13][14] Interacting proteinsFAM222A has been found to interact with mainly transcription factors. These include mainly pre-B-cell leukemia transcription factors and Homeobox Meis proteins.[15] HomologsFAM222A has only one paralog in humans, FAM222B which is also not well characterized.[16] These two proteins only share about 20% identity. It has many orthologs in other organisms but is restricted to jawed vertebrates, as far back as bony and cartilaginous fish.[17] Overall the protein is well conserved with a lowest identity of around 50% but certain regions are very strictly conserved such as the beginning of pfam15258 as well as the last 60-70 amino acids on the C terminus.[6] The protein appears to be changing very slowly even in distantly related animals. It is changing at a rate just slightly higher than Cytochrome C, a highly conserved protein.] References
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