Pxdn
entrez
69675
canonical
uniprot
Q3UQ28
canonical
ensembl
ENSMUSG00000020674
resolver
ensp
ENSMUSP00000113703
resolver
ensp
ENSMUSP00000319850
resolver
enst
ENSMUST00000122328
resolver
genesymbol
Pxdn
resolver
genesymbol_syn
Kiaa0230
resolver
uniprot
A4FU83
resolver
uniprot
E9QNQ9
resolver
uniprot_entry
PXDN_MOUSE
resolver
uniprot_sec
A4FU83
resolver
uniprot_sec
E9QNQ9
resolver
activity_regulation
ACTIVITY REGULATION: Thiocyanate inhibits the formation of 3-bromotyrosine. {ECO:0000269|PubMed:32675287}.
uniprot
proteins
amino_acid_sequence
MAVRPTRRCLLALLLCFAWWAMAVVASKQGAGCPSRCLCFRTTVRCMHLLLEAVPAVAPQTSILDLRFNRIREIQPGAFRRLRSLNTLLLNNNQIKKIPNGAFEDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLDPESFQHLPKLERLFLHNNRITHLVPGTFSQLESMKRLRLDSNALHCDCEILWLADLLKTYAQSGNAQAAATCEYPRRIQGRSVATITPEELNCERPRITSEPQDADVTSGNTVYFTCRAEGNPKPEIIWLRNNNELSMKTDSRLNLLDDGTLMIQNTQEADEGVYQCMAKNVAGEAKTQEVTLRYLGSPARPTFVIQPQNTEVLVGESVTLECSATGHPLPQITWTRGDRTPLPIDPRVNITPSGGLYIQNVAQSDSGEYTCFASNSVDSIHATAFIIVQALPQFTVTPQSRVVIEGQTVDFQCAAKGHPQPVIAWTKGGSQLSVDRRHLVLSSGTLRISGVALHDQGQYECQAVNIIGSQKVVAHLTVQPRVTPVFASIPSDMTVEVGTNVQLPCSSQGEPEPAITWNKDGVQVTESGKFHISPEGFLTINDVGTADAGRYECVARNTIGYASVSMVLSVNVPDVSRNGDPYVATSIVEAIATVDRAINSTRTHLFDSRPRSPNDLLALFRYPRDPYTVGQARAGEIFERTLQLIQEHVQHGLMVDLNGTSYHYNDLVSPQYLSLIANLSGCTAHRRVNNCSDMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKAVYENGFNTPRGINSQRQYNGHVLPMPRLVSTTLIGTEVITPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQHCSSVCSNDPPCFSVMIPPNDPRVRSGARCMFFVRSSPVCGSGMTSLLMNSVYPREQINQLTSYIDASNVYGSTDHEARSIRDLASHRGLLRQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEVGMKMLGEYRGYDPSVNAGIFNAFATAAFRFGHTLINPLLYRLDENFEPIPQGHVPLHKAFFSPFRIVNEGGIDPLLRGLFGVAGKMRIPSQLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEIKSPVIREKLQRLYGSTLNIDLFPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPGVFSPAQLTQLKQTSLARILCDNSDNITRVQQDVFRVAEFPHGYSSCEDIPRVDLRVWQDCCEDCRTRGQFNAFSYHFRGRRSLEFSYEDDKPTKRARWRKALSVKHGKHLSNATSATHEHLEGPATNDLKEFVLEMQKIITDLRKQINSLESRLSTTECVDDSGESHGGNTKWKKDPCTVCECKNGQITCFVEACQPAACPQPVKVEGACCPVCLKNTAEEKP
uniprot
proteins
ec_number
1.11.2.-
uniprot
proteins
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/COL4A1 NC1 hexamer (PubMed:22842973, PubMed:25708780, PubMed:28424209, PubMed:29626421, PubMed:31817535). In turns, directly contributes to the collagen IV network-dependent fibronectin/FN and laminin assembly, which is required for full extracellular matrix (ECM)-mediated signaling (By similarity). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (By similarity). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (By similarity). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1480' and leads to bromine enrichment of the basement membranes (PubMed:32571911, PubMed:32675287). In vitro, can also catalyze the two-electron oxidation of thiocyanate and iodide and these two substrates could effectively compete with bromide and thus inhibit the formation of sulfilimine bonds (By similarity). Binds laminins (By similarity). May play a role in the organization of eyeball structure and lens development during eye development (PubMed:24895407, PubMed:31817535). {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:24895407, ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:28424209, ECO:0000269|PubMed:29626421, ECO:0000269|PubMed:31817535, ECO:0000269|PubMed:32571911, ECO:0000269|PubMed:32675287}.
uniprot
proteins
mass_dalton
165103
uniprot
proteins
mutagenesis
MUTAGEN 1272..1475; /note="Missing: Kinky tail mutant mice show kinky tail and white spot at the belly; additionally, homozygous mutants show microphthalmia and anterior segment dysgenesis including corneal opacity, severe iris bombe (forward-bowing iris) and very shallow or absent anterior chamber."; /evidence="ECO:0000269|PubMed:24895407
uniprot
proteins
post_translational_modification
PTM: Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (PubMed:34679700). The proteolytic cleavage occurs after intracellular homotrimerization and releases into the extracellular matrix a large, catalytically active fragment and a smaller fragment consisting primarily of the C-terminal VWFC domain. The processing enhances both peroxidase activity and sulfilimine cross-links formation (By similarity). {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:34679700}.
uniprot
proteins
protein_family
Peroxidase family
uniprot
proteins
protein_family
XPO subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18848646
uniprot
proteins
pubmed
18929642
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19590037
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21907015
uniprot
proteins
pubmed
22842973
uniprot
proteins
pubmed
24895407
uniprot
proteins
pubmed
25708780
uniprot
proteins
pubmed
28424209
uniprot
proteins
pubmed
29626421
uniprot
proteins
pubmed
31817535
uniprot
proteins
pubmed
32571911
uniprot
proteins
pubmed
32675287
uniprot
proteins
pubmed
34679700
uniprot
proteins
sequence_length
1475
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19590037}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92626}. Cell surface {ECO:0000250|UniProtKB:Q92626}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:22842973}. Note=Adheres on the cell surface in 'hot spots'. {ECO:0000250|UniProtKB:Q92626}.; SUBCELLULAR LOCATION: [PXDN active fragment]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}.
uniprot
proteins