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Q9VZZ4 (PXDN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length1527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in extracellular matrix consolidation, phagocytosis and defense. Ref.1

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per subunit By similarity.

Subunit structure

Homotrimer; disulfide-linked. Ref.1

Subcellular location

Secreted Potential.

Tissue specificity

Expressed in hemocytes. Also expressed in the fat body and gastric caeca. Ref.1

Developmental stage

Expressed throughout embryonic and larval development. Expressed in hemocytes as they migrate in the early embryo and later in embryogenesis, become localized to basement membranes. Ref.1

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Contains 4 Ig-like C2-type (immunoglobulin-like) domains.

Contains 5 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Contains 1 VWFC domain.

Sequence caution

The sequence AAA61568.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9VZZ4-1)

Also known as: C; D; E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9VZZ4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     456-457: EL → GE
     458-1527: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 15271504Peroxidasin
PRO_0000319624

Regions

Domain24 – 5229LRRNT
Repeat53 – 7422LRR 1
Repeat77 – 9822LRR 2
Repeat101 – 12222LRR 3
Repeat125 – 14622LRR 4
Repeat149 – 17022LRR 5
Domain182 – 23554LRRCT
Domain236 – 32287Ig-like C2-type 1
Domain365 – 45389Ig-like C2-type 2
Domain458 – 54588Ig-like C2-type 3
Domain553 – 64391Ig-like C2-type 4
Domain1463 – 152462VWFC
Coiled coil1403 – 144139 Potential

Sites

Active site8631Proton acceptor By similarity
Metal binding8641Calcium By similarity
Metal binding9411Calcium By similarity
Metal binding9431Calcium; via carbonyl oxygen By similarity
Metal binding9451Calcium By similarity
Metal binding9471Calcium By similarity
Metal binding11091Iron (heme axial ligand) By similarity
Binding site8621Heme (covalent; via 2 links) By similarity
Binding site10151Heme (covalent; via 2 links) By similarity
Site10121Transition state stabilizer By similarity

Amino acid modifications

Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6731N-linked (GlcNAc...) Potential
Glycosylation6821N-linked (GlcNAc...) Potential
Glycosylation7311N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation9621N-linked (GlcNAc...) Ref.5
Glycosylation11201N-linked (GlcNAc...) Potential
Glycosylation12131N-linked (GlcNAc...) Potential
Disulfide bond257 ↔ 307 By similarity
Disulfide bond388 ↔ 437 By similarity
Disulfide bond479 ↔ 529 By similarity
Disulfide bond574 ↔ 627 By similarity
Disulfide bond768 ↔ 784 By similarity
Disulfide bond882 ↔ 892 By similarity
Disulfide bond886 ↔ 909 By similarity
Disulfide bond994 ↔ 1005 By similarity
Disulfide bond1212 ↔ 1269 By similarity
Disulfide bond1310 ↔ 1336 By similarity

Natural variations

Alternative sequence456 – 4572EL → GE in isoform B.
VSP_032693
Alternative sequence458 – 15271070Missing in isoform B.
VSP_032694

Experimental info

Sequence conflict1281A → G in AAA61568. Ref.1
Sequence conflict1831A → AID in AAA61568. Ref.1
Sequence conflict2631P → H in AAA61568. Ref.1
Sequence conflict2821A → T in AAA61568. Ref.1
Sequence conflict2941I → H in AAA61568. Ref.1
Sequence conflict3511M → T in AAA61568. Ref.1
Sequence conflict361 – 3622LP → SPSH in AAA61568. Ref.1
Sequence conflict3801G → S in AAA61568. Ref.1
Sequence conflict6921G → D in AAA61568. Ref.1
Sequence conflict959 – 9602EL → LA in AAA61568. Ref.1
Sequence conflict10831G → S in AAA61568. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C) (D) (E) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 71174FEBEA7C9152

FASTA1,527170,514
        10         20         30         40         50         60 
MRFMLLMLQL LGLLLLLAGG VQSVYCPAGC TCLERTVRCI RAKLSAVPKL PQDTQTLDLR 

        70         80         90        100        110        120 
FNHIEELPAN AFSGLAQLTT LFLNDNELAY LQDGALNGLT ALRFVYLNNN RLSRLPATIF 

       130        140        150        160        170        180 
QRMPRLEAIF LENNDIWQLP AGLFDNLPRL NRLIMYNNKL TQLPVDGFNR LNNLKRLRLD 

       190        200        210        220        230        240 
GNAIDCNCGV YSLWRRWHLD VQRQLVSISL TCAAPQMLQN QGFSSLGEHH FKCAKPQFLV 

       250        260        270        280        290        300 
APQDAQVAAG EQVELSCEVT GLPRPQITWM HNTQELGLEE QAQAEILPSG SLLIRSADTS 

       310        320        330        340        350        360 
DMGIYQCIAR NEMGALRSQP VRLVVNGGNH PLDSPIDARS NQVWADAGTP MHGATPLPSP 

       370        380        390        400        410        420 
LPSPPHFTHQ PHDQIVALHG SGHVLLDCAA SGWPQPDIQW FVNGRQLLQS TPSLQLQANG 

       430        440        450        460        470        480 
SLILLQPNQL SAGTYRCEAR NSLGSVQATA RIELKELPEI LTAPQSQTIK LGKAFVLECD 

       490        500        510        520        530        540 
ADGNPLPTID WQLNGVPLPG NTPDLQLENE NTELVVGAAR QEHAGVYRCT AHNENGETSV 

       550        560        570        580        590        600 
EATIKVERSQ SPPQLAIEPS NLVAITGTTI ELPCQADQPE DGLQISWRHD GRLIDPNVQL 

       610        620        630        640        650        660 
AEKYQISGAG SLFVKNVTIP DGGRYECQLK NQFGRASASA LVTIRNNVDL APGDRYVRIA 

       670        680        690        700        710        720 
FAEAAKEIDL AINNTLDMLF SNRSDKAPPN YGELLRVFRF PTGEARQLAR AAEIYERTLV 

       730        740        750        760        770        780 
NIRKHVQEGD NLTMKSEEYE FRDLLSREHL HLVAELSGCM EHREMPNCTD MCFHSRYRSI 

       790        800        810        820        830        840 
DGTCNNLQHP TWGASLTAFR RLAPPIYENG FSMPVGWTKG MLYSGHAKPS ARLVSTSLVA 

       850        860        870        880        890        900 
TKEITPDARI THMVMQWGQF LDHDLDHAIP SVSSESWDGI DCKKSCEMAP PCYPIEVPPN 

       910        920        930        940        950        960 
DPRVRNRRCI DVVRSSAICG SGMTSLFFDS VQHREQINQL TSYIDASQVY GYSTAFAQEL 

       970        980        990       1000       1010       1020 
RNLTSQEGLL RVGVHFPRQK DMLPFAAPQD GMDCRRNLDE NTMSCFVSGD IRVNEQVGLL 

      1030       1040       1050       1060       1070       1080 
AMHTIWMREH NRIASKLKQI NSHWDGDTLY QEARKIVGAQ MQHITFKQWL PLIIGESGME 

      1090       1100       1110       1120       1130       1140 
MMGEYQGYNP QLNPSIANEF ATAALRFGHT IINPILHRLN ETFQPIPQGH LLLHKAFFAP 

      1150       1160       1170       1180       1190       1200 
WRLAYEGGVD PLMRGFLAVP AKLKTPDQNL NTELTEKLFQ TAHAVALDLA AINIQRGRDH 

      1210       1220       1230       1240       1250       1260 
GMPGYNVYRK LCNLTVAQDF EDLAGEISSA EIRQKMKELY GHPDNVDVWL GGILEDQVEG 

      1270       1280       1290       1300       1310       1320 
GKVGPLFQCL LVEQFRRLRD GDRLYYENPG VFSPEQLTQI KQANFGRVLC DVGDNFDQVT 

      1330       1340       1350       1360       1370       1380 
ENVFILAKHQ GGYKKCEDII GINLYLWQEC GRCNSPPAIF DSYIPQTYTK RSNRQKRDLG 

      1390       1400       1410       1420       1430       1440 
KENDEVATAE SYDSPLESLY DVNEERVSGL EELIGSFQKE LKKLHKKLRK LEDSCNSADS 

      1450       1460       1470       1480       1490       1500 
EPVAQVVQLA AAPPQLVSKP KRSHCVDDKG TTRLNNEVWS PDVCTKCNCF HGQVNCLRER 

      1510       1520 
CGEVSCPPGV DPLTPPEACC PHCPMVK 

« Hide

Isoform B [UniParc].

Checksum: 243FB8041A16D483
Show »

FASTA45750,558

References

« Hide 'large scale' references
[1]"Peroxidasin: a novel enzyme-matrix protein of Drosophila development."
Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F., Parker C.G., Fessler J.H.
EMBO J. 13:3438-3447(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Salivary gland.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1527 (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[5]"Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-962, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Oregon-R.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11052 mRNA. Translation: AAA61568.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF47668.1.
AE014296 Genomic DNA. Translation: AAN11518.1.
AE014296 Genomic DNA. Translation: AAS64946.1.
AE014296 Genomic DNA. Translation: AAS64947.1.
AE014296 Genomic DNA. Translation: AAS64948.1.
AY051536 mRNA. Translation: AAK92960.1.
AY052120 mRNA. Translation: AAK93544.1.
RefSeqNP_523891.2. NM_079167.4. [Q9VZZ4-1]
NP_728759.1. NM_167957.2. [Q9VZZ4-2]
NP_995975.1. NM_206253.2. [Q9VZZ4-1]
NP_995976.1. NM_206254.2. [Q9VZZ4-1]
NP_995977.1. NM_206255.2. [Q9VZZ4-1]
UniGeneDm.8030.

3D structure databases

ProteinModelPortalQ9VZZ4.
SMRQ9VZZ4. Positions 24-709, 774-1349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63831. 4 interactions.
IntActQ9VZZ4. 2 interactions.
MINTMINT-1680107.

Protein family/group databases

PeroxiBase3369. DmPxd-A.
3370. DmPxd.

Proteomic databases

PaxDbQ9VZZ4.
PRIDEQ9VZZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072951; FBpp0072828; FBgn0011828. [Q9VZZ4-1]
FBtr0072952; FBpp0089205; FBgn0011828. [Q9VZZ4-1]
FBtr0072953; FBpp0089215; FBgn0011828. [Q9VZZ4-1]
FBtr0072954; FBpp0089216; FBgn0011828. [Q9VZZ4-1]
GeneID38326.
KEGGdme:Dmel_CG12002.

Organism-specific databases

CTD5829.
FlyBaseFBgn0011828. Pxn.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00550000074325.
InParanoidQ9VZZ4.
OMARVRNGRC.
OrthoDBEOG7D2FD6.
PhylomeDBQ9VZZ4.

Gene expression databases

BgeeQ9VZZ4.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
InterProIPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR001007. VWF_C.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF13855. LRR_8. 2 hits.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 3 hits.
SM00369. LRR_TYP. 3 hits.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS50835. IG_LIKE. 4 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPXN. drosophila.
GenomeRNAi38326.
NextBio808033.
PROQ9VZZ4.

Entry information

Entry namePXDN_DROME
AccessionPrimary (citable) accession number: Q9VZZ4
Secondary accession number(s): Q23991, Q960D1, Q961K8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase