Q9VZZ4 · PXDN_DROME
- ProteinPeroxidasin
- GenePxn
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1527 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV NC1 hexamer (PubMed:22842973).
Plays a role in extracellular matrix consolidation, phagocytosis and defense (PubMed:8062820).
Plays a role in extracellular matrix consolidation, phagocytosis and defense (PubMed:8062820).
Catalytic activity
- (5R)-5-hydroxy-L-lysyl-[collagen] + H2O2 + L-methionyl-[collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-[collagen] + H+ + 2 H2OThis reaction proceeds in the forward direction.
- bromide + H2O2 = H2O + hypobromiteThis reaction proceeds in the forward direction.
- (5R)-5-hydroxy-L-lysyl-[collagen] + hypobromite + L-methionyl-[collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H+ + H2OThis reaction proceeds in the forward direction.
- H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H+ + 2 H2OThis reaction proceeds in the forward direction.
- hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H+ + H2OThis reaction proceeds in the forward direction.
- bromide + H+ + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + 2 H2OThis reaction proceeds in the forward direction.
- H+ + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + H2OThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 862 | heme b (UniProtKB | ChEBI); covalent | ||||
Sequence: D | ||||||
Active site | 863 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 864 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 941 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 943 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 945 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 947 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 1012 | Transition state stabilizer | ||||
Sequence: R | ||||||
Binding site | 1015 | heme b (UniProtKB | ChEBI); covalent | ||||
Sequence: E | ||||||
Binding site | 1109 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on peroxide as acceptor | |
Molecular Function | peroxidase activity | |
Biological Process | basement membrane assembly | |
Biological Process | collagen fibril organization | |
Biological Process | extracellular matrix organization | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | phagocytosis | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxidasin
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VZZ4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MRFMLLMLQLLGLLLLLAGGVQS | ||||||
Chain | PRO_0000319624 | 24-1527 | Peroxidasin | |||
Sequence: VYCPAGCTCLERTVRCIRAKLSAVPKLPQDTQTLDLRFNHIEELPANAFSGLAQLTTLFLNDNELAYLQDGALNGLTALRFVYLNNNRLSRLPATIFQRMPRLEAIFLENNDIWQLPAGLFDNLPRLNRLIMYNNKLTQLPVDGFNRLNNLKRLRLDGNAIDCNCGVYSLWRRWHLDVQRQLVSISLTCAAPQMLQNQGFSSLGEHHFKCAKPQFLVAPQDAQVAAGEQVELSCEVTGLPRPQITWMHNTQELGLEEQAQAEILPSGSLLIRSADTSDMGIYQCIARNEMGALRSQPVRLVVNGGNHPLDSPIDARSNQVWADAGTPMHGATPLPSPLPSPPHFTHQPHDQIVALHGSGHVLLDCAASGWPQPDIQWFVNGRQLLQSTPSLQLQANGSLILLQPNQLSAGTYRCEARNSLGSVQATARIELKELPEILTAPQSQTIKLGKAFVLECDADGNPLPTIDWQLNGVPLPGNTPDLQLENENTELVVGAARQEHAGVYRCTAHNENGETSVEATIKVERSQSPPQLAIEPSNLVAITGTTIELPCQADQPEDGLQISWRHDGRLIDPNVQLAEKYQISGAGSLFVKNVTIPDGGRYECQLKNQFGRASASALVTIRNNVDLAPGDRYVRIAFAEAAKEIDLAINNTLDMLFSNRSDKAPPNYGELLRVFRFPTGEARQLARAAEIYERTLVNIRKHVQEGDNLTMKSEEYEFRDLLSREHLHLVAELSGCMEHREMPNCTDMCFHSRYRSIDGTCNNLQHPTWGASLTAFRRLAPPIYENGFSMPVGWTKGMLYSGHAKPSARLVSTSLVATKEITPDARITHMVMQWGQFLDHDLDHAIPSVSSESWDGIDCKKSCEMAPPCYPIEVPPNDPRVRNRRCIDVVRSSAICGSGMTSLFFDSVQHREQINQLTSYIDASQVYGYSTAFAQELRNLTSQEGLLRVGVHFPRQKDMLPFAAPQDGMDCRRNLDENTMSCFVSGDIRVNEQVGLLAMHTIWMREHNRIASKLKQINSHWDGDTLYQEARKIVGAQMQHITFKQWLPLIIGESGMEMMGEYQGYNPQLNPSIANEFATAALRFGHTIINPILHRLNETFQPIPQGHLLLHKAFFAPWRLAYEGGVDPLMRGFLAVPAKLKTPDQNLNTELTEKLFQTAHAVALDLAAINIQRGRDHGMPGYNVYRKLCNLTVAQDFEDLAGEISSAEIRQKMKELYGHPDNVDVWLGGILEDQVEGGKVGPLFQCLLVEQFRRLRDGDRLYYENPGVFSPEQLTQIKQANFGRVLCDVGDNFDQVTENVFILAKHQGGYKKCEDIIGINLYLWQECGRCNSPPAIFDSYIPQTYTKRSNRQKRDLGKENDEVATAESYDSPLESLYDVNEERVSGLEELIGSFQKELKKLHKKLRKLEDSCNSADSEPVAQVVQLAAAPPQLVSKPKRSHCVDDKGTTRLNNEVWSPDVCTKCNCFHGQVNCLRERCGEVSCPPGVDPLTPPEACCPHCPMVK | ||||||
Disulfide bond | 257↔307 | |||||
Sequence: CEVTGLPRPQITWMHNTQELGLEEQAQAEILPSGSLLIRSADTSDMGIYQC | ||||||
Disulfide bond | 388↔437 | |||||
Sequence: CAASGWPQPDIQWFVNGRQLLQSTPSLQLQANGSLILLQPNQLSAGTYRC | ||||||
Glycosylation | 419 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 479↔529 | |||||
Sequence: CDADGNPLPTIDWQLNGVPLPGNTPDLQLENENTELVVGAARQEHAGVYRC | ||||||
Disulfide bond | 574↔627 | |||||
Sequence: CQADQPEDGLQISWRHDGRLIDPNVQLAEKYQISGAGSLFVKNVTIPDGGRYEC | ||||||
Glycosylation | 616 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 673 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 682 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 731 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 767 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 768↔784 | |||||
Sequence: CTDMCFHSRYRSIDGTC | ||||||
Disulfide bond | 772 | Interchain (with C-1350); in homotrimer | ||||
Sequence: C | ||||||
Disulfide bond | 882↔892 | |||||
Sequence: CKKSCEMAPPC | ||||||
Disulfide bond | 886↔909 | |||||
Sequence: CEMAPPCYPIEVPPNDPRVRNRRC | ||||||
Glycosylation | 962 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 994↔1005 | |||||
Sequence: CRRNLDENTMSC | ||||||
Glycosylation | 1120 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1212↔1269 | |||||
Sequence: CNLTVAQDFEDLAGEISSAEIRQKMKELYGHPDNVDVWLGGILEDQVEGGKVGPLFQC | ||||||
Glycosylation | 1213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1310↔1336 | |||||
Sequence: CDVGDNFDQVTENVFILAKHQGGYKKC | ||||||
Disulfide bond | 1350 | Interchain (with C-772); in homotrimer | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in hemocytes. Also expressed in the fat body and gastric caeca.
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.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, repeat, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-53 | LRRNT | ||||
Sequence: VYCPAGCTCLERTVRCIRAKLSAVPKLPQD | ||||||
Repeat | 51-74 | LRR 1 | ||||
Sequence: PQDTQTLDLRFNHIEELPANAFSG | ||||||
Repeat | 75-98 | LRR 2 | ||||
Sequence: LAQLTTLFLNDNELAYLQDGALNG | ||||||
Repeat | 99-122 | LRR 3 | ||||
Sequence: LTALRFVYLNNNRLSRLPATIFQR | ||||||
Repeat | 124-146 | LRR 4 | ||||
Sequence: PRLEAIFLENNDIWQLPAGLFDN | ||||||
Repeat | 147-170 | LRR 5 | ||||
Sequence: LPRLNRLIMYNNKLTQLPVDGFNR | ||||||
Repeat | 172-196 | LRR 6 | ||||
Sequence: NNLKRLRLDGNAIDCNCGVYSLWRR | ||||||
Domain | 236-322 | Ig-like C2-type 1 | ||||
Sequence: PQFLVAPQDAQVAAGEQVELSCEVTGLPRPQITWMHNTQELGLEEQAQAEILPSGSLLIRSADTSDMGIYQCIARNEMGALRSQPVR | ||||||
Domain | 365-453 | Ig-like C2-type 2 | ||||
Sequence: PHFTHQPHDQIVALHGSGHVLLDCAASGWPQPDIQWFVNGRQLLQSTPSLQLQANGSLILLQPNQLSAGTYRCEARNSLGSVQATARIE | ||||||
Domain | 458-545 | Ig-like C2-type 3 | ||||
Sequence: PEILTAPQSQTIKLGKAFVLECDADGNPLPTIDWQLNGVPLPGNTPDLQLENENTELVVGAARQEHAGVYRCTAHNENGETSVEATIK | ||||||
Domain | 553-643 | Ig-like C2-type 4 | ||||
Sequence: PQLAIEPSNLVAITGTTIELPCQADQPEDGLQISWRHDGRLIDPNVQLAEKYQISGAGSLFVKNVTIPDGGRYECQLKNQFGRASASALVT | ||||||
Coiled coil | 1403-1441 | |||||
Sequence: NEERVSGLEELIGSFQKELKKLHKKLRKLEDSCNSADSE | ||||||
Domain | 1463-1524 | VWFC | ||||
Sequence: SHCVDDKGTTRLNNEVWSPDVCTKCNCFHGQVNCLRERCGEVSCPPGVDPLTPPEACCPHCP |
Sequence similarities
Belongs to the peroxidase family. XPO subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9VZZ4-1
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.
- NameA
- SynonymsC, D, E
- Length1,527
- Mass (Da)170,514
- Last updated2000-05-01 v1
- Checksum71174FEBEA7C9152
Q9VZZ4-2
- NameB
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 128 | in Ref. 1; AAA61568 | ||||
Sequence: A → G | ||||||
Sequence conflict | 183 | in Ref. 1; AAA61568 | ||||
Sequence: A → AID | ||||||
Sequence conflict | 263 | in Ref. 1; AAA61568 | ||||
Sequence: P → H | ||||||
Sequence conflict | 282 | in Ref. 1; AAA61568 | ||||
Sequence: A → T | ||||||
Sequence conflict | 294 | in Ref. 1; AAA61568 | ||||
Sequence: I → H | ||||||
Sequence conflict | 351 | in Ref. 1; AAA61568 | ||||
Sequence: M → T | ||||||
Sequence conflict | 361-362 | in Ref. 1; AAA61568 | ||||
Sequence: LP → SPSH | ||||||
Sequence conflict | 380 | in Ref. 1; AAA61568 | ||||
Sequence: G → S | ||||||
Alternative sequence | VSP_032693 | 456-457 | in isoform B | |||
Sequence: EL → GE | ||||||
Alternative sequence | VSP_032694 | 458-1527 | in isoform B | |||
Sequence: Missing | ||||||
Sequence conflict | 692 | in Ref. 1; AAA61568 | ||||
Sequence: G → D | ||||||
Sequence conflict | 959-960 | in Ref. 1; AAA61568 | ||||
Sequence: EL → LA | ||||||
Sequence conflict | 1083 | in Ref. 1; AAA61568 | ||||
Sequence: G → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U11052 EMBL· GenBank· DDBJ | AAA61568.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AE014296 EMBL· GenBank· DDBJ | AAF47668.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAN11518.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAS64946.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAS64947.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAS64948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051536 EMBL· GenBank· DDBJ | AAK92960.1 EMBL· GenBank· DDBJ | mRNA | ||
AY052120 EMBL· GenBank· DDBJ | AAK93544.1 EMBL· GenBank· DDBJ | mRNA |