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Sentrin-specific protease 1 is an enzyme that in humans is encoded by the SENP1gene.
General
There are six known SUMO proteases in humans that have been designated SENP1-3 and SENP5-7 (sentrin/SUMO-specific protease). The six proteases possess a conserved C-terminal domain which are variable in size, and with a distinct N-terminal domain between them. The C-terminal domain shows catalytic activity and the N-terminal domain regulates cell localization and substrate specificity.
Features
SENP1 (Sentrin-specific protease 1) is a human protease of 643 amino acids with a molecular weight of 73 kDa, EC number in humans 3.4.22.B70. It adopts a conformation that identifies it as a member of the superfamily of cysteine proteases, which contain a catalytic triad with three characterized amino acids: a cysteine at position 603, a histidine at position 533 and aspartic acid at position 550.
The primary nucleophile is cysteine located at the N-terminal alpha helix of the protein core. The other two amino acids, aspartate and histidine, are located in the end of a beta sheet.
SENP1 The catalytic site consists of three amino acids: Cys 602, His 533 and Asp 550.
Location
Both SENP1 are located in the nucleus and cytosol depending on the cell type, although it has been seen to be exported out from the nucleus to the cytosol through a sequence of nuclear export (NES) that is located at the C-terminus. The mammalian SENP1 is localized mainly in the nucleus.
Function
SENP1 catalyzes maturation of SUMO protein (small ubiquitin-related modifier). SENP1 causes hydrolysis of a peptide bond of SUMO in the conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminus, which can then be conjugated to other proteins (sumoylation).
In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze the maturation of any of these three.
This conjugation of SUMO toward other proteins is similar to ubiquitination, however these modifications can lead to different outcomes depending on the type of protein being modified.
Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y (2005). "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1". FEBS Letters. 579 (27): 6272–6278. doi:10.1016/j.febslet.2005.10.010. PMID16253240. S2CID13388952.
Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS (Jan 2008). "Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family". The Biochemical Journal. 409 (2): 461–9. doi:10.1042/BJ20070940. PMID17916063. S2CID12234952.
Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y (Nov 2005). "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1". FEBS Letters. 579 (27): 6272–8. doi:10.1016/j.febslet.2005.10.010. PMID16253240. S2CID13388952.
