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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Peroxidasin homolog

UniprotKB/SwissProt ID: Q92626 (Q92626)

Gene Name: PXDN

Organism: Homo sapiens (Human)

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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Secreted, extracellular space, extracellular matrix. Endoplasmic reticulum. Cell surface. Secreted, extracellular space, extracellular matrix, basement membrane. Secreted, extracellular space, extracellular matrix

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000483 Cys-rich_flank_reg_C
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR047018 Peroxidasin_Ig-like3
IPR034828 Peroxidasin_Ig-like4
IPR034824 Peroxidasin_peroxidase
IPR001007 VWF_dom

The S-nitrosylation sites of Q92626

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 49 RCLCFRTTVR C MHLLLEAVPA    37478858