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UniProtKB/Swiss-Prot entry Q9GLW7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX5_CERAE
Primary accession number Q9GLW7
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2002
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Peroxiredoxin-5, mitochondrial [Precursor]
Synonyms EC 1.11.1.15
Prx-V
Thioredoxin reductase
Gene name
Name: PRDX5
From
Cercopithecus aethiops (Green monkey) (Grivet) [TaxID: 9534] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Knoops B., Cherif H.;
"Cloning and characterization of COS-7 AOEB166/PRDX5.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF110736; AAG13453.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P30044; 1HD2. [HSSP ENTRY / PDB]
SMR Q9GLW7; 55-215.
ModBase Q9GLW7.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF08534; Redoxin; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9GLW7.
Phylogenomic databases
HOVERGEN Q9GLW7; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; Antioxidant; Cytoplasm; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    53  53     Mitochondrion (Potential). 
CHAIN   54   215  162     Peroxiredoxin-5, mitochondrial. PRO_0000023790
DOMAIN   57   215  159     Thioredoxin. 
MOTIF   213   215  3     Microbody targeting signal (By similarity). 
ACT_SITE   101   101        Cysteine sulfenic acid (-SOH) intermediate (Potential). 
DISULFID   101   205        Redox-active (By similarity). 
VAR_SEQ   1    53        Missing (in isoform Cytoplasmic+peroxisomal). VSP_018828
Sequence information
Length: 215 AA [This is the length of the unprocessed precursor] Molecular weight: 22237 Da [This is the MW of the unprocessed precursor] CRC64: 7C9E45C1B9517B78 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLAGVCVLR RSAGYILGGA ARQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG 

        70         80         90        100        110        120 
DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG 

       130        140        150        160        170        180 
VQVLACLSVN DAFVTGEWGR AHKAEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK 

       190        200        210 
RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL 

Q9GLW7 in FASTA format

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