PXDN
entrez
7837
canonical
uniprot
Q92626
canonical
ensembl
ENSG00000130508
resolver
ensp
ENSP00000252804
resolver
ensp
ENSP00000527564
resolver
genesymbol
PXDN
resolver
genesymbol_syn
KIAA0230
resolver
genesymbol_syn
MG50
resolver
genesymbol_syn
PRG2
resolver
genesymbol_syn
PXD01
resolver
genesymbol_syn
VPO
resolver
genesymbol_syn
VPO1
resolver
hgnc
HGNC:14966
resolver
uniprot
A8QM65
resolver
uniprot
D6W4Y0
resolver
uniprot
Q4KMG2
resolver
uniprot_entry
PXDN_HUMAN
resolver
uniprot_sec
A8QM65
resolver
uniprot_sec
D6W4Y0
resolver
uniprot_sec
Q4KMG2
resolver
activity_regulation
ACTIVITY REGULATION: The hypobromous acid formation is activated by increasing nitrite concentrations and inhibited by increasing urate concentrations. {ECO:0000269|PubMed:31953133}.
uniprot
proteins
amino_acid_sequence
MAKRSRGPGRRCLLALVLFCAWGTLAVVAQKPGAGCPSRCLCFRTTVRCMHLLLEAVPAVAPQTSILDLRFNRIREIQPGAFRRLRNLNTLLLNNNQIKRIPSGAFEDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLDPDSFQHLPKLERLFLHNNRITHLVPGTFNHLESMKRLRLDSNTLHCDCEILWLADLLKTYAESGNAQAAAICEYPRRIQGRSVATITPEELNCERPRITSEPQDADVTSGNTVYFTCRAEGNPKPEIIWLRNNNELSMKTDSRLNLLDDGTLMIQNTQETDQGIYQCMAKNVAGEVKTQEVTLRYFGSPARPTFVIQPQNTEVLVGESVTLECSATGHPPPRISWTRGDRTPLPVDPRVNITPSGGLYIQNVVQGDSGEYACSATNNIDSVHATAFIIVQALPQFTVTPQDRVVIEGQTVDFQCEAKGNPPPVIAWTKGGSQLSVDRRHLVLSSGTLRISGVALHDQGQYECQAVNIIGSQKVVAHLTVQPRVTPVFASIPSDTTVEVGANVQLPCSSQGEPEPAITWNKDGVQVTESGKFHISPEGFLTINDVGPADAGRYECVARNTIGSASVSMVLSVNVPDVSRNGDPFVATSIVEAIATVDRAINSTRTHLFDSRPRSPNDLLALFRYPRDPYTVEQARAGEIFERTLQLIQEHVQHGLMVDLNGTSYHYNDLVSPQYLNLIANLSGCTAHRRVNNCSDMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKSVYENGFNTPRGINPHRLYNGHALPMPRLVSTTLIGTETVTPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQHCSNVCSNDPPCFSVMIPPNDSRARSGARCMFFVRSSPVCGSGMTSLLMNSVYPREQINQLTSYIDASNVYGSTEHEARSIRDLASHRGLLRQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIATELLKLNPHWDGDTIYYETRKIVGAEIQHITYQHWLPKILGEVGMRTLGEYHGYDPGINAGIFNAFATAAFRFGHTLVNPLLYRLDENFQPIAQDHLPLHKAFFSPFRIVNEGGIDPLLRGLFGVAGKMRVPSQLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAHTFEDLKNEIKNPEIREKLKRLYGSTLNIDLFPALVVEDLVPGSRLGPTLMCLLSTQFKRLRDGDRLWYENPGVFSPAQLTQIKQTSLARILCDNADNITRVQSDVFRVAEFPHGYGSCDEIPRVDLRVWQDCCEDCRTRGQFNAFSYHFRGRRSLEFSYQEDKPTKKTRPRKIPSVGRQGEHLSNSTSAFSTRSDASGTNDFREFVLEMQKTITDLRTQIKKLESRLSTTECVDAGGESHANNTKWKKDACTICECKDGQVTCFVEACPPATCAVPVNIPGACCPVCLQKRAEEKP
uniprot
proteins
disease_involvement
DISEASE: Anterior segment dysgenesis 7 (ASGD7) [MIM:269400]: A form of anterior segment dysgenesis, a group of defects affecting anterior structures of the eye including cornea, iris, lens, trabecular meshwork, and Schlemm canal. Anterior segment dysgeneses result from abnormal migration or differentiation of the neural crest derived mesenchymal cells that give rise to components of the anterior chamber during eye development. Different anterior segment anomalies may exist alone or in combination, including iris hypoplasia, enlarged or reduced corneal diameter, corneal vascularization and opacity, posterior embryotoxon, corectopia, polycoria, abnormal iridocorneal angle, ectopia lentis, and anterior synechiae between the iris and posterior corneal surface. Clinical conditions falling within the phenotypic spectrum of anterior segment dysgeneses include aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters anomaly, and iridogoniodysgenesis. ASGD7 is an autosomal recessive disease. {ECO:0000269|PubMed:21907015}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:18929642, PubMed:19590037, PubMed:22842973, PubMed:25708780, PubMed:25713063, PubMed:27697841, PubMed:28154175, PubMed:34679700). 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 (PubMed:19590037, PubMed:32543734, PubMed:34679700). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (PubMed:32543734). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (PubMed:25713063). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1485' and leads to bromine enrichment of the basement membranes (PubMed:32571911). 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 (PubMed:28154175). Binds laminins (PubMed:32485152). May play a role in the organization of eyeball structure and lens development during eye development (By similarity). {ECO:0000250|UniProtKB:Q3UQ28, ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037, ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:25713063, ECO:0000269|PubMed:27697841, ECO:0000269|PubMed:28154175, ECO:0000269|PubMed:32485152, ECO:0000269|PubMed:32543734, ECO:0000269|PubMed:32571911, ECO:0000269|PubMed:34679700}.
uniprot
proteins
mass_dalton
165275
uniprot
proteins
mutagenesis
MUTAGEN 736; /note="C->S: Loss of protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315. Does not affect peroxidase activity; when associated with S-1315. Retains the ability to support the collagen IV cross-links; when associated with S-1315. Slightly reduces proteolysis; when associated with S-1315."; /evidence="ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:34679700"; MUTAGEN 823; /note="Q->A: Loss of bromide oxidation. Loss of tubulogenesis. Does not induce angiogenesis."; /evidence="ECO:0000269|PubMed:29982533"; MUTAGEN 823; /note="Q->W: Loss of peroxidase activity. Does not affect oligomerization. Loss of peroxidase activity; when associated with E-826. Does not support the formation of collagen IV cross-links; when associated with E-826. Reduces the proteolytic processing; when associated with E-826. Loss of collagen IV cross-link; when associated with E-826."; /evidence="ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:34679700"; MUTAGEN 826; /note="D->E: Loss of peroxidase activity. Does not affect oligomerization. Loss of peroxidase activity; when associated with E-823. Does not support the formation of collagen IV cross-links; when associated with W-823. Reduces the proteolytic processing; when associated with W-823. Loss of collagen IV cross-link; when associated with W-823."; /evidence="ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:34679700"; MUTAGEN 1315; /note="C->S: Loss of protein homooligomerization. Loss of protein homooligomerization; when associated with S-1316 and S-1319. Loss of protein homooligomerization; when associated with S-736. Does not affect peroxidase activity; when associated with S-736. Affects cell surface location; when associated with S-736. Slightly reduces proteolysis; when associated with S-736."; /evidence="ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:34679700"; MUTAGEN 1316; /note="C->S: Does not affect protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315 and S-1319."; /evidence="ECO:0000269|PubMed:25708780"; MUTAGEN 1319; /note="C->S: Does not affect protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315 and S-1316."; /evidence="ECO:0000269|PubMed:25708780"; MUTAGEN 1335..1336; /note="RR->AA: Loss of proteolytic cleavage. Decreases the formation of sulfilimine cross-links in collagen IV. Reduces the proteolytic processing. Affects collagen IV cross-linking."; /evidence="ECO:0000269|PubMed:27697841, ECO:0000269|PubMed:34679700"; MUTAGEN 1354..1355; /note="RK->AA: Does not affect the proteolytic processing."; /evidence="ECO:0000269|PubMed:34679700
uniprot
proteins
post_translational_modification
PTM: Glycosylated (PubMed:25713063). Four sites are completely N-glycosylated (Asn-640, Asn-731, Asn-865 and Asn-1425), whereas the others are found partially glycosylated (PubMed:25713063). {ECO:0000269|PubMed:25713063}.; PTM: Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (PubMed:27697841, 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 (PubMed:27697841, PubMed:31295557). The processing enhances both peroxidase activity and sulfilimine cross-links formation (PubMed:27697841, PubMed:34679700). {ECO:0000269|PubMed:27697841, ECO:0000269|PubMed:31295557, ECO:0000269|PubMed:34679700}.
uniprot
proteins
protein_family
Peroxidase family
uniprot
proteins
protein_family
XPO subfamily
uniprot
proteins
pubmed
10441517
uniprot
proteins
pubmed
11103812
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18929642
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19590037
uniprot
proteins
pubmed
21907015
uniprot
proteins
pubmed
22842973
uniprot
proteins
pubmed
24253521
uniprot
proteins
pubmed
25708780
uniprot
proteins
pubmed
25713063
uniprot
proteins
pubmed
26178375
uniprot
proteins
pubmed
27697841
uniprot
proteins
pubmed
28154175
uniprot
proteins
pubmed
29982533
uniprot
proteins
pubmed
31295557
uniprot
proteins
pubmed
31953133
uniprot
proteins
pubmed
32485152
uniprot
proteins
pubmed
32543734
uniprot
proteins
pubmed
32571911
uniprot
proteins
pubmed
34679700
uniprot
proteins
pubmed
9039502
uniprot
proteins
sequence_length
1479
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037, ECO:0000269|PubMed:26178375, ECO:0000269|Ref.9}. Endoplasmic reticulum {ECO:0000269|PubMed:19590037, ECO:0000269|PubMed:25708780}. Cell surface {ECO:0000269|PubMed:25708780}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q3UQ28}. Note=Enriched in the peritubular space of fibrotic kidneys. Adheres on the cell surface in 'hot spots' (PubMed:25708780). Only the proteolytically processed PXDN integrates into the extracellular matrix (PubMed:34679700). {ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:34679700}.; SUBCELLULAR LOCATION: [PXDN active fragment]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:34679700}.
uniprot
proteins