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- FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).
- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- MISCELLANEOUS: The active site is the redox-active Cys-12 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-?-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).
- MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation of Cys-12 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized (By similarity).
- SIMILARITY: Belongs to the ahpC/TSA family.
- SIMILARITY: Contains 1 thioredoxin domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 127 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 14168 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 1C05A9765EB69E84 [This is a checksum on the sequence] |
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10 20 30 40 50 60
LFFYPLDFTF VCPTEIIAFS DRAEEFHQLG CEVLGVSVDX QXTHLAWINT PRKEGGLGPL
70 80 90 100 110 120
KIPLLADVTR NLSLDYGVLK EDEGIAYRGL FIIDGKGVLR QITVNDLPVG RXVDEALRLV
QGXQYTD
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P52552 in FASTA format |
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