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Protein

Chorion peroxidase

Gene

Pxt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Required for ovarian follicle maturation. Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization.1 Publication

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei320 – 3201Proton acceptorPROSITE-ProRule annotationBy similarity
Sitei464 – 4641Transition state stabilizerPROSITE-ProRule annotationBy similarity
Metal bindingi568 – 5681Iron (heme axial ligand)PROSITE-ProRule annotationBy similarity

GO - Molecular functioni

GO - Biological processi

  • chorion-containing eggshell formation Source: FlyBase
  • eggshell chorion assembly Source: UniProtKB
  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • hydrogen peroxide metabolic process Source: UniProtKB
  • ovarian follicle cell development Source: UniProtKB
  • prostaglandin biosynthetic process Source: FlyBase
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei3552. DmPxt01-A.
3553. DmPxt01-B.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorion peroxidase (EC:1.11.1.7)
Alternative name(s):
Peroxinectin-related protein
Short name:
Dpxt
Gene namesi
Name:Pxt
ORF Names:CG7660
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0261987. Pxt.

Subcellular locationi

  • Secreted 1 Publication

  • Note: In the chorion layer of the mature eggs.

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Females are sterile, and maturing follicles show defects in actin filament formation, nurse cell membrane stability and border cell migration.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 223202By similarityPRO_0000232898Add
BLAST
Chaini224 – 809586Chorion peroxidasePRO_0000407856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence analysis
Modified residuei224 – 2241N-acetylcysteine; in Chorion peroxidase light chainBy similarity
Disulfide bondi230 ↔ 244PROSITE-ProRule annotationBy similarity
Disulfide bondi448 ↔ 457PROSITE-ProRule annotationBy similarity
Disulfide bondi765 ↔ 794PROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9VEG6.
PRIDEiQ9VEG6.

Expressioni

Tissue specificityi

Expressed at low levels in the germarium and early follicles. Expression becomes progressively stronger during vitellogenesis, and is highly expressed in germ cells and somatic cells. A subset of follicle cells, termed border cells (BC), exhibit a high level of expression.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiFBgn0261987.
GenevisibleiQ9VEG6. DM.

Interactioni

Subunit structurei

Heterodimer.By similarityCurated

Protein-protein interaction databases

BioGridi67163. 11 interactions.
IntActiQ9VEG6. 1 interaction.
MINTiMINT-1547498.
STRINGi7227.FBpp0082932.

Structurei

3D structure databases

ProteinModelPortaliQ9VEG6.
SMRiQ9VEG6. Positions 227-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
InParanoidiQ9VEG6.
OMAiCPAHVRM.
OrthoDBiEOG091G04XU.
PhylomeDBiQ9VEG6.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029590. Pxt.
[Graphical view]
PANTHERiPTHR11475:SF57. PTHR11475:SF57. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VEG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRILFILLL LIVTQLSELQ AAAFSVRQNR FDEVPDLQTP APLATSTESS
60 70 80 90 100
KKPEKATSGL LKKCLPCSDG IRCVPQIQCP AHVRMESHEK PQICDLPAGK
110 120 130 140 150
FGYCCETGQN HTAPKPETSP KERRSGFPTI LSPAVLDEAR RNFEHLMHGV
160 170 180 190 200
AQIPVRRGFP DFAHGLVFHS TAKDDLHNFA ISNSAIEQVM TTQLFGKKEQ
210 220 230 240 250
VPVEDFITNN VPIKFTETPL AHHCQPPPVC GNIRSVYRSM DGTCNNPEPQ
260 270 280 290 300
RSLWGAAGQP MERMLPPAYE DGIWTPRAHS SDGTPLLGAR KISRTLLSDV
310 320 330 340 350
DRPHPKYNLM VMQFGQVLAH DISQTSSIRL EDGSLVQCCS PEGKVALSPQ
360 370 380 390 400
QSHFACMPIH VEPDDEFFSA FGVRCLNFVR LSLVPSPDCQ LSYGKQLTKV
410 420 430 440 450
THFVDASPVY GSSDEASRSL RAFRGGRLRM MNDFGRDLLP LTNDKKACPS
460 470 480 490 500
EEAGKSCFHS GDGRTNQIIS LITLQILLAR EHNRVAGALH ELNPSASDET
510 520 530 540 550
LFQEARRIVI AEMQHITYNE FLPIIIGPQQ MKRFRLVPLH QGYSHDYNVN
560 570 580 590 600
VNPAITNEFS GAAYRMGHSS VDGKFQIRQE HGRIDEVVNI PDVMFNPSRM
610 620 630 640 650
RKREFYDDML RTLYSQPMQQ VDSSISQGLS RFLFRGDNPF GLDLAAINIQ
660 670 680 690 700
RGRDQGLRSY NDYLELMGAP KLHSFEQFPI EIAQKLSRVY RTPDDIDLWV
710 720 730 740 750
GGLLEKAVEG GVVGVTFAEI IADQFARFKQ GDRYYYEYDN GINPGAFNPL
760 770 780 790 800
QLQEIRKVTL ARLLCDNSDR LTLQAVPLAA FVRADHPGNQ MIGCDDPNLP

SVNLEAWRA
Length:809
Mass (Da):90,539
Last modified:May 5, 2009 - v3
Checksum:iD46C1EC4879DD926
GO

Sequence cautioni

The sequence AAF78217 differs from that shown. Reason: Frameshift at positions 220, 233, 238, 244, 331, 336, 381, 384, 644 and 688. Curated
The sequence AAF78217 differs from that shown. Reason: Erroneous termination at position 810. Translated as stop.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871L → F in AAF78217 (PubMed:12459925).Curated
Sequence conflicti358 – 3581P → R in AAF78217 (PubMed:12459925).Curated
Sequence conflicti428 – 4292LR → FG in AAF78217 (PubMed:12459925).Curated
Sequence conflicti443 – 46018NDKKA…SCFHS → KSLLSNVFLIIKILNNILTL RCYSLLLLPLLLMRFFFLLH L in AAF78217 (PubMed:12459925).CuratedAdd
BLAST
Sequence conflicti557 – 5637NEFSGAA → KPNS in AAF78217 (PubMed:12459925).Curated
Sequence conflicti602 – 6032KR → G in AAF78217 (PubMed:12459925).Curated
Sequence conflicti606 – 6061Y → F in AAF78217 (PubMed:12459925).Curated
Sequence conflicti645 – 6451A → AAINIR in AAF78217 (PubMed:12459925).Curated
Sequence conflicti655 – 6551Q → H in AAF78217 (PubMed:12459925).Curated
Sequence conflicti658 – 6581R → P in AAF78217 (PubMed:12459925).Curated
Sequence conflicti695 – 6951D → H in AAF78217 (PubMed:12459925).Curated
Sequence conflicti707 – 7071A → P in AAF78217 (PubMed:12459925).Curated
Sequence conflicti717 – 7171F → I in AAF78217 (PubMed:12459925).Curated
Sequence conflicti736 – 7361Y → YY in AAF78217 (PubMed:12459925).Curated
Sequence conflicti756 – 7583RKV → GIL in AAF78217 (PubMed:12459925).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238306 mRNA. Translation: AAF78217.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAN13751.2.
AY119616 mRNA. Translation: AAM50270.1.
RefSeqiNP_650648.3. NM_142391.5.
UniGeneiDm.19352.

Genome annotation databases

EnsemblMetazoaiFBtr0083508; FBpp0082932; FBgn0261987.
GeneIDi42131.
KEGGidme:Dmel_CG7660.
UCSCiCG7660-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238306 mRNA. Translation: AAF78217.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAN13751.2.
AY119616 mRNA. Translation: AAM50270.1.
RefSeqiNP_650648.3. NM_142391.5.
UniGeneiDm.19352.

3D structure databases

ProteinModelPortaliQ9VEG6.
SMRiQ9VEG6. Positions 227-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67163. 11 interactions.
IntActiQ9VEG6. 1 interaction.
MINTiMINT-1547498.
STRINGi7227.FBpp0082932.

Protein family/group databases

PeroxiBasei3552. DmPxt01-A.
3553. DmPxt01-B.

Proteomic databases

PaxDbiQ9VEG6.
PRIDEiQ9VEG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083508; FBpp0082932; FBgn0261987.
GeneIDi42131.
KEGGidme:Dmel_CG7660.
UCSCiCG7660-RB. d. melanogaster.

Organism-specific databases

CTDi42131.
FlyBaseiFBgn0261987. Pxt.

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
InParanoidiQ9VEG6.
OMAiCPAHVRM.
OrthoDBiEOG091G04XU.
PhylomeDBiQ9VEG6.

Miscellaneous databases

GenomeRNAii42131.
PROiQ9VEG6.

Gene expression databases

BgeeiFBgn0261987.
GenevisibleiQ9VEG6. DM.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029590. Pxt.
[Graphical view]
PANTHERiPTHR11475:SF57. PTHR11475:SF57. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPERC_DROME
AccessioniPrimary (citable) accession number: Q9VEG6
Secondary accession number(s): Q8IN93, Q8MRH7, Q9NBX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: May 5, 2009
Last modified: September 7, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.