https://www.genenames.org/data/genegroup/#!/group/65
THAP domeenin sisältävä transkriptiotekijä Zf
THAP4, (2q17. 3), Nitrobindiini (Ferrirautaa sisältävä proteiini)
Reaktiivisten typpilajien (NOS) pyydystys, sitoo
myös NO. Suojaa vapaata l-tyrosiinia- (Säädellyn tyrosiininitaation merkitys? Haittaako nitraatiosta vain vai onko hyötyä?
https://www.sciencedirect.com/science/article/abs/pii/S0003986108005031 )
https://www.sciencedirect.com/science/article/abs/pii/S0003986108005031 )
- Also known as PP238; CGI-36; Nb(III)
- Expression Ubiquitous expression in testis (RPKM 14.3), heart (RPKM 13.9) and 25 other tissues See more Orthologs mouse all
- Preferred Names THAP domain-containing protein 4
- Names epididymis secretory sperm binding protein
- nitrobindin
- Isoform2 https://www.ncbi.nlm.nih.gov/protein/NP_001157828.1
- Conserved Domains (1) summary
-
cd07828
Location:10 → 162 - nitrobindin; nitrobindin heme-binding domain. Nitrobindin is a heme-containing lipocalin that may reversibly bind nitric oxide (NO). This heme-binding domain forms a beta barrel structure, and in a small family of proteins from tetrapods, it is found C-terminal to a THAP zinc finger domain (a sequence-specific DNA binding domain). Members of this group are putatively related to fatty acid-binding proteins (FABPs).
- Conserved Domains (3) summary
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pfam05485
Location:4 → 86 - THAP; THAP domain
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pfam08768
Location:422 → 574 - DUF1794; Domain of unknown function (DUF1794)
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cl22422
Location:312 → 425 - SRP68-RBD; RNA-binding domain of signal recognition particle subunit 68. Signal recognition particles (SRPs) are ribonucleoprotein complexes that target particular nascent pre-secretory proteins to the endoplasmic reticulum. SRP68 is one of the two largest proteins found in SRPs (the other being SRP72), and it forms a heterodimer with SRP72. Heterodimer formation is essential for SRP function. This model characterizes the N-terminal RNA-binding domain SRP68-RBD, a tetratricopeptide-like module. Interactions between SRP68-RBD and SRP RNA (7SL RNA) are thought to facilitate a conformation of SRP RNA that is required for interactions with ribosomal RNA.
Related articles in PubMed
- Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification. De Simone G, et al. FEBS Open Bio, 2018 Dec. PMID 30524950, Free PMC Article *Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evidence of the heme-Fe(III)-based detoxification of peroxynitrite by the all-β-barrel C-terminal Nb-like domain of THAP4. Ferric human Nb (Nb(III)) catalyzes the conversion of peroxynitrite to NO−3 and impairs the nitration of free l-tyrosine. The rate of human Nb(III)-mediated scavenging of peroxynitrite is similar to those of all-α-helical horse heart and sperm whale myoglobin and human hemoglobin, generally taken as the prototypes of all-α-helical heme-proteins. The heme-Fe(III) reactivity of all-β-barrel human Nb(III) and all-α-helical prototypical heme-proteins possibly reflects the out-to-in-plane transition of the heme-Fe(III)-atom preceding peroxynitrite binding. Human Nb(III) not only catalyzes the detoxification of peroxynitrite but also binds NO, possibly representing a target of reactive nitrogen species.KEYWORDS: human nitrobindin; kinetics; peroxynitrite scavenging; protection of l‐tyrosine nitration
- Structure of the C-terminal heme-binding domain of THAP domain containing protein 4 from Homo sapiens. Bianchetti CM, et al. Proteins, 2011 Apr. PMID 21387410, Free PMC Article
- Voxelwise genome-wide association study (vGWAS). Stein JL, et al. Neuroimage, 2010 Nov 15. PMID 20171287, Free PMC Article
- The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase. Roussigne M, et al. Trends Biochem Sci, 2003 Feb. PMID 12575992Abstract We have identified a novel evolutionarily conserved protein motif - designated the THAP domain - that defines a new family of cellular factors. We have found that the THAP domain presents striking similarities with the site-specific DNA-binding domain (DBD) of Drosophila P element transposase, including a similar size, N-terminal location, and conservation of the residues that define the THAP motif, such as the C2CH signature (Cys-Xaa(2-4)-Cys-Xaa(35-50)-Cys-Xaa(2)-His). Our results suggest that the THAP domain is a novel example of a DBD that is shared between cellular proteins and transposases from mobile genomic parasites.
- Large-scale cDNA transfection screening for genes related to cancer development and progression. Wan D, et al. Proc Natl Acad Sci U S A, 2004 Nov 2. PMID 15498874, Free PMC Article
