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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
DOI=10.1021/bi00041a017; PubMed=7577926 [NCBI, ExPASy, EBI, Israel, Japan]
Iwahara S.,
Satoh H.,
Song D.-X.,
Webb J.,
Burlingame A.L.,
Nagae Y.,
Mueller-Eberhard U.;
"Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol.";
Biochemistry 34:13398-13406(1995).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and 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 17-35 AND 111-190, 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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[4]
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X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM.
DOI=10.1073/pnas.96.22.12333; PubMed=10535922 [NCBI, ExPASy, EBI, Israel, Japan]
Hirotsu S.,
Abe Y.,
Okada K.,
Nagahara N.,
Hori H.,
Nishino T.,
Hakoshima T.;
"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product.";
Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999).
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- FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not 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. May form heterodimers with AOP2.
- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity).
- PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity (By similarity).
- MISCELLANEOUS: The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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.
- MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation of Cys-52 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.
- 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: 199 AA [This is the length of the unprocessed precursor] |
Molecular weight: 22109 Da [This is the MW of the unprocessed precursor] |
CRC64: BDF2D4ABA8A776DA [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS
70 80 90 100 110 120
DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK
130 140 150 160 170 180
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG
190
SDTIKPDVNK SKEYFSKQK
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Q63716 in FASTA format |
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