FASTKD3
| FASTKD3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | FASTKD3, FAST kinase domains 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 617530 MGI: 1916827 HomoloGene: 11457 GeneCards: FASTKD3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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FAST kinase domain-containing protein 3 (FASTKD3) is a protein that in humans is encoded by the FASTKD3 gene on chromosome 5.[5][6] This protein is part of the Fas-activated serine/threonine kinase domain (FASTKD) containing protein family, which is known for regulating the energy balance of mitochondria under stress.[7][8]
Structure
FASTKD3 shares structural characteristics of the FASTKD family, including an N-terminal mitochondrial targeting domain and three C-terminal domains: two FAST kinase-like domains (FAST_1 and FAST_2) and a RNA-binding domain (RAP).[7][8] The mitochondrial targeting domain directs FASTKD3 to be imported into the mitochondria. Though the functions of the C-terminal domains are unknown, RAP possibly binds RNA during trans-splicing.[7]
Function
As a member of the FASTKD family, FASTKD3 localizes to the mitochondria to modulate their energy balance, especially under conditions of stress. Though ubiquitously expressed in all tissues, FASTKD3 appears more abundantly in skeletal muscle, heart muscle, and other tissues enriched in mitochondria. FASTKD3 has been proposed to regulate energy production by serving as a scaffold protein that brings together RNA processing/translation and respiratory components.[7]
Clinical Significance
Currently, FASTKD3 has not been linked to any disease. (Dated: September 17, 2015)
Interactions
FASTKD3 has been shown to interact with:
- FASTKD2;
- Fatty acid beta oxidation pathway proteins (ACADVL, ECHS1, HADHA, HADHB, ACAA2);
- Amino acid catabolic pathways proteins (MCCC1, MCCC2, GLUD1, HIBADH, CPS1);
- Amino acid biosynthesis proteins (PYCR1, PYCR2, ALDH18A1, SHMT2, GLS);
- TCA cycle proteins (IDH3A, IDH2, SUCLG2, DLST);
- Respiratory chain proteins (NDUFS1, SDHA, ATP5A1, ETFA, ETFB);
- Mitochondrial RNA processing proteins (LRPPRC, DHX30, PNPT1); and
- Mitochondrial translation proteins (TUFM, GFM1, IARS2, MRPS22, TARS2, MRPS2, PTCD1, MTO1, MRPS31).[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000124279 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021532 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ UniProt: Q9NYY8
- ^ "Entrez Gene: FAST kinase domains 2".
- ^ a b c d e Simarro M, Gimenez-Cassina A, Kedersha N, Lazaro JB, Adelmant GO, Marto JA, Rhee K, Tisdale S, Danial N, Benarafa C, Orduña A, Anderson P (Oct 2010). "Fast kinase domain-containing protein 3 is a mitochondrial protein essential for cellular respiration". Biochemical and Biophysical Research Communications. 401 (3): 440–6. doi:10.1016/j.bbrc.2010.09.075. PMC 2963690. PMID 20869947.
- ^ a b Yeung KT, Das S, Zhang J, Lomniczi A, Ojeda SR, Xu CF, Neubert TA, Samuels HH (Jun 2011). "A novel transcription complex that selectively modulates apoptosis of breast cancer cells through regulation of FASTKD2". Molecular and Cellular Biology. 31 (11): 2287–98. doi:10.1128/MCB.01381-10. PMC 3133243. PMID 21444724.
Further reading
- Lai Y, Song M, Hakala K, Weintraub ST, Shiio Y (Nov 2011). "Proteomic dissection of the von Hippel-Lindau (VHL) interactome". Journal of Proteome Research. 10 (11): 5175–82. doi:10.1021/pr200642c. PMC 3208728. PMID 21942715.
- Simarro M, Gimenez-Cassina A, Kedersha N, Lazaro JB, Adelmant GO, Marto JA, Rhee K, Tisdale S, Danial N, Benarafa C, Orduña A, Anderson P (Oct 2010). "Fast kinase domain-containing protein 3 is a mitochondrial protein essential for cellular respiration". Biochemical and Biophysical Research Communications. 401 (3): 440–6. doi:10.1016/j.bbrc.2010.09.075. PMC 2963690. PMID 20869947.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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