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Protein

Peroxidasin

Gene

pxdn

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei815Heme (covalent; via 2 links)By similarity1
Active sitei816Proton acceptorPROSITE-ProRule annotation1
Metal bindingi817CalciumPROSITE-ProRule annotation1
Metal bindingi896CalciumPROSITE-ProRule annotation1
Metal bindingi898Calcium; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi900CalciumPROSITE-ProRule annotation1
Metal bindingi902CalciumPROSITE-ProRule annotation1
Sitei966Transition state stabilizerPROSITE-ProRule annotation1
Binding sitei969Heme (covalent; via 2 links)By similarity1
Metal bindingi1063Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei4051. XtPxd.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidasin (EC:1.11.1.7)
Gene namesi
Name:pxdn
Synonyms:pxn
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-923300. pxdn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000031962126 – 1457PeroxidasinAdd BLAST1432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi257 ↔ 307By similarity
Disulfide bondi353 ↔ 402By similarity
Disulfide bondi444 ↔ 492By similarity
Disulfide bondi536 ↔ 584By similarity
Glycosylationi630N-linked (GlcNAc...)Sequence analysis1
Glycosylationi689N-linked (GlcNAc...)Sequence analysis1
Glycosylationi709N-linked (GlcNAc...)Sequence analysis1
Glycosylationi721N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi722 ↔ 738By similarity
Disulfide bondi836 ↔ 846By similarity
Disulfide bondi840 ↔ 864By similarity
Disulfide bondi948 ↔ 959By similarity
Disulfide bondi1166 ↔ 1223By similarity
Glycosylationi1167N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1264 ↔ 1290By similarity
Glycosylationi1269N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1347N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1434N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiA4IGL7.

Expressioni

Developmental stagei

Maternal expression is localized to the animal hemisphere where it persists through early cleavage stages. Initial zygotic expression is detected in the developing neural tube and becomes localized to the hindbrain and midbrain. Expressed in the primordium of the pronephric kidney and expression persists in the pronephric tubules and duct throughout development.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA4IGL7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 52LRRNTAdd BLAST27
Repeati53 – 74LRR 1Add BLAST22
Repeati77 – 98LRR 2Add BLAST22
Repeati101 – 122LRR 3Add BLAST22
Repeati125 – 146LRR 4Add BLAST22
Repeati149 – 170LRR 5Add BLAST22
Domaini182 – 235LRRCTAdd BLAST54
Domaini236 – 324Ig-like C2-type 1Add BLAST89
Domaini332 – 418Ig-like C2-type 2Add BLAST87
Domaini423 – 510Ig-like C2-type 3Add BLAST88
Domaini515 – 600Ig-like C2-type 4Add BLAST86
Domaini1392 – 1450VWFCPROSITE-ProRule annotationAdd BLAST59

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
Contains 5 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG108312.
InParanoidiA4IGL7.
KOiK19511.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF13855. LRR_8. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
SSF48726. SSF48726. 4 hits.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS51450. LRR. 5 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A4IGL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAGSWLYL TAGLLVVALP QLSHSCPSRC LCFRTTVRCM HLMLESVPAV
60 70 80 90 100
PPHTTILDLR FNRIKDIQTG AFKHLKNLNT LLLNNNQIKR IPSEAFKDLE
110 120 130 140 150
NLKYLYLYKN EIQSIDRQAF KGLASLEQLY LHFNQIETLE PESFNYLPKL
160 170 180 190 200
ERLFLHNNRI THLVPGTFSQ LESMKRLRLD SNALHCDCEI LWLADLLKIY
210 220 230 240 250
SESGNAQAAA TCEYPRRLQG RSVSTITPSE LNCERPRITS EPQDVDVTFG
260 270 280 290 300
NTVYFTCRAE GNPKPEIIWL RNNNELSMKD DSRLNLLNDG TLMIQNTKET
310 320 330 340 350
DQGIYQCMAK NVAGEVKTHE VTLRYYGTPA TPTFVIQPQN TEVLVGESVT
360 370 380 390 400
LECSATGQPH PRVTWTRGDR TPLPSDPRIN ITPSGGLYIQ NVNQDDAGEY
410 420 430 440 450
TCFATNSVET IHSTAYIIVQ AVPQFTVVPQ DRNVFEGHTV DFHCEAQGNP
460 470 480 490 500
KPVIAWTKGG NQLSVDRRHQ VLSSGTLRIL RVALHDQGQY ECQAVNIVGS
510 520 530 540 550
KSTAAQLIVQ TRVTPVFATV PNDMTVEVGT DVQIPCSSQG DPLPIITWNK
560 570 580 590 600
DGIQVTESGK FHISPHGYLA IRDAGLADQG RYECVARNPI GYSSVSMVLS
610 620 630 640 650
VLVPEVSRTG DPFVATSIIE AIATVDRAIN STRTHLFDSR PRSPGDLLAL
660 670 680 690 700
FRYPRDPYTV EQARAAEIFE RTLQLIQDHV QSGLMVDLNG TSYHYNDLVS
710 720 730 740 750
PQYLNMIANL SGCATHRRIN NCSNMCFHQK YRTHDGTCNN LQHPMWGASL
760 770 780 790 800
TAFERLLKSV YENGFNLPRG ISGRIYNGFP LPLPRLVSTT LIGTHTITPD
810 820 830 840 850
EQFTHMLMQW GQFLDHDLDS TVVALSQARF SDGQDCSVVC TNDAPCFPIM
860 870 880 890 900
VPPNDPRVRN NARCMSMVRS SPVCGSGMTS LLMNSVYPRE QMNQLTSYID
910 920 930 940 950
ASNVYGSSDH ESNEIRDSAS HRGLLKQGIV QRSGKPLLPF ATGPPTECMR
960 970 980 990 1000
DENESPIPCF LAGDHRANEQ LGLTSMHTLW FREHNRIATE LLRLNPHWDG
1010 1020 1030 1040 1050
DTIYHETRKI VGAQMQHITY SHWLPKIFGD VGMKMLGEYK SYDPNVNAGI
1060 1070 1080 1090 1100
LNEFATAAFR FGHTLINPIL YRLDEKFEPI PQGHVPLHRA FFSPFRIVNE
1110 1120 1130 1140 1150
GGIDPLLRGL IGVAAKMRVT SQLLNTELTE KLFSMAHAVA LDLAALNVQR
1160 1170 1180 1190 1200
GRDHGIPPYH DFRVFCNLST VQTFDDLRNE IKNPDVREKL KRLYGSPLNI
1210 1220 1230 1240 1250
DLFPALMVED LIPGSRLGPT LMCLLTTQFR NIRDGDRFWY ENPGVFTAAQ
1260 1270 1280 1290 1300
LTQIKQTSLA RVLCDNGDNI TKVQHDLFRV AEFPHGYVSC KNIAKMDLRV
1310 1320 1330 1340 1350
WQDCCEDCRT RGQFSTFSNH FRGKRSTEHS YKEDNKEPSS LLNQSVNTTC
1360 1370 1380 1390 1400
NTEQPKNLPH VNDFKEFVLD MQKTITGLRK QIKKLESRLS NTDCTDETGE
1410 1420 1430 1440 1450
SHSTKEKWNK DACTKCECYN GHITCFVKSC PPVNCSRPQR IEGVCCPVCT

DDKIQST
Length:1,457
Mass (Da):163,914
Last modified:May 1, 2007 - v1
Checksum:i902697AA1C02311A
GO

Sequence cautioni

The sequence DAA05635 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC135155 mRNA. Translation: AAI35156.1.
BK005589 Genomic DNA. Translation: DAA05635.1. Different initiation.
RefSeqiNP_001076815.1. NM_001083346.1.
UniGeneiStr.25013.

Genome annotation databases

GeneIDi493201.
KEGGixtr:493201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC135155 mRNA. Translation: AAI35156.1.
BK005589 Genomic DNA. Translation: DAA05635.1. Different initiation.
RefSeqiNP_001076815.1. NM_001083346.1.
UniGeneiStr.25013.

3D structure databases

ProteinModelPortaliA4IGL7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei4051. XtPxd.

Proteomic databases

PRIDEiA4IGL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi493201.
KEGGixtr:493201.

Organism-specific databases

CTDi7837.
XenbaseiXB-GENE-923300. pxdn.

Phylogenomic databases

HOVERGENiHBG108312.
InParanoidiA4IGL7.
KOiK19511.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF13855. LRR_8. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
SSF48726. SSF48726. 4 hits.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS51450. LRR. 5 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPXDN_XENTR
AccessioniPrimary (citable) accession number: A4IGL7
Secondary accession number(s): Q5HZ61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: November 2, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.