[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26. STRAIN=ATCC 32195; PubMed=2760051 [NCBI, ExPASy, EBI, Israel, Japan] Garrard L.J., Goodman J.M.; "Two genes encode the major membrane-associated protein of methanol-induced peroxisomes from Candida boidinii."; J. Biol. Chem. 264:13929-13937(1989).
[2]	CROSS-REACTIVITY WITH ASP F 3. PubMed=9412580 [NCBI, ExPASy, EBI, Israel, Japan] Hemmann S., Blaser K., Crameri R.; "Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes."; Am. J. Respir. Crit. Care Med. 156:1956-1962(1997).

Comments

FUNCTION: Its function is very likely to be related to the metabolism of methanol.
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein.
INDUCTION: By methanol.
ALLERGEN: Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Asp f 3 of Aspergillus fumigatus.
SIMILARITY: Belongs to the peroxiredoxin 2 family.
SIMILARITY: Contains 1 thioredoxin domain.

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

J04984; AAA34357.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32646; A32646.

3D structure databases

HSSP

P44758; 1NM3. [HSSP ENTRY / PDB]

ModBase

P14292.

Ontologies

GO:0005778;	Cellular component: peroxisomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
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:0015945;	Biological process: methanol metabolic process (inferred from electronic annotation from UniProtKB-KW).
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

P14292.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allergen; Direct protein sequencing; Membrane; Methanol utilization; Oxidoreductase; Peroxidase; Peroxisome; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 167`	`166`	`Putative peroxiredoxin-A.`	`PRO_0000056604`
`DOMAIN`	`4 167`	`164`	`Thioredoxin.`
`MOTIF`	`165 167`	`3`	`Microbody targeting signal.`

Sequence information

Length: 167 AA [This is the length of the unprocessed precursor]

Molecular weight: 18004 Da [This is the MW of the unprocessed precursor]

CRC64: BB6474B84834D0D5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPIKRGDRF PTTDDVYYIP PEGGEPGPLE LSKFVKTKKF VVVSVPGAFT PPCTEQHLPG 

        70         80         90        100        110        120 
YIKNLPRILS KGVDFVLVIS QNDPFVLKGW KKELGAADAK KLVFVSDPNL KLTKKLGSTI 

       130        140        150        160 
DLSAIGLGTR SGRLALIVNR SGIVEYAAIE NGGEVDVSTA QKIIAKL

P14292 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools