[1]	NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. STRAIN=A99; DOI=10.1242/jeb.01571; PubMed=15914659 [NCBI, ExPASy, EBI, Israel, Japan] Habetha M., Bosch T.C.G.; "Symbiotic Hydra express a plant-like peroxidase gene during oogenesis."; J. Exp. Biol. 208:2157-2165(2005).

Comments

FUNCTION: May play a role in the protection of oocyte incorporated cells from rapid apoptotic degradation.
CATALYTIC ACTIVITY: L-ascorbate + H₂O₂ = dehydroascorbate + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
DEVELOPMENTAL STAGE: Expressed exclusively during oogenesis.
MISCELLANEOUS: The gene for this protein may have been transferred horizontally following an endosymbiotic event early in evolution of the Hydra lineage as an RNA or cDNA intermediate.
SIMILARITY: Belongs to the peroxidase family.

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

AY608909; AAU07981.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q539E5.

Protein family/group databases

PeroxiBase

2285; HviNAnPrx01.

Family and domain databases

InterPro

IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`CHAIN`	`17 367`	`351`	`Putative ascorbate peroxidase.`	`PRO_0000023637`
`ACT_SITE`	`58 58`		`Proton acceptor (By similarity).`
`SITE`	`54 54`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`119 119`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`239 239`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`356 356`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`60 66`		`By similarity.`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 40790 Da [This is the MW of the unprocessed precursor]

CRC64: 91E0A494F416A10D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVPVIWLTVL IVLVDSLQII PTFHDFQRAK TDLLGLIESV KRGDDLPMIA GTVRLAFHDC 

        70         80         90        100        110        120 
IGKGKCDGCI DHSKPGNAGL KRVTDRLDAL YDASYKGKIS RADFYALASV TALTRSTANL 

       130        140        150        160        170        180 
SDKYNGLRKF KVGRKDCSTS PVESIDSSDI PRGSDGTSKT LQFFKSEFGM KTQEAVALLG 

       190        200        210        220        230        240 
AHTLGRCSLQ NSGFVGSWVD QRFSTAPPGE ENLSPTSILD NAYYRMIIDI VPWTQVNING 

       250        260        270        280        290        300 
TRIQWQEPSN SIPNDKLPES KRSPLLLNSD MAISWIIKPS DALGTVSCRP TSLKTPCRHS 

       310        320        330        340        350        360 
NAHTFAKIYA KNNALWVKDF TKAFNKMIEM NENKLRKAPI FNGYFDEMNS HDEPINESVD 


EISEDIF

Q539E5 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