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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8041738 [NCBI, ExPASy, EBI, Israel, Japan]
Chae H.Z.,
Robison K.,
Poole L.B.,
Church G.,
Storz G.,
Rhee S.G.;
"Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[3]
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PROTEIN SEQUENCE OF 93-135 AND 140-157, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G.,
Afjehi-Sadat L.,
Diao W.,
Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
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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.
- MISCELLANEOUS: The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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-51 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: 198 AA [This is the length of the unprocessed precursor] |
Molecular weight: 21784 Da [This is the MW of the unprocessed precursor] |
CRC64: FC6AD9B0E9C4447B [This is a checksum on the sequence] |
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10 20 30 40 50 60
MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD
70 80 90 100 110 120
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN
130 140 150 160 170 180
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
190
DTIKPNVDDS KEYFSKHN
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P35704 in FASTA format |
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