PXDN1_CAEEL
ID PXDN1_CAEEL Reviewed; 1285 AA.
AC Q1ENI8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Peroxidasin homolog pxn-1 {ECO:0000305};
DE EC=1.11.2.- {ECO:0000250|UniProtKB:Q92626};
DE Flags: Precursor;
GN Name=pxn-1 {ECO:0000312|WormBase:ZK994.3};
GN ORFNames=ZK994.3 {ECO:0000312|WormBase:ZK994.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-741 AND ASN-858, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [3]
RP FUNCTION.
RX PubMed=20876652; DOI=10.1242/dev.049189;
RA Gotenstein J.R., Swale R.E., Fukuda T., Wu Z., Giurumescu C.A.,
RA Goncharov A., Jin Y., Chisholm A.D.;
RT "The C. elegans peroxidasin PXN-2 is essential for embryonic morphogenesis
RT and inhibits adult axon regeneration.";
RL Development 137:3603-3613(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25475546; DOI=10.14348/molcells.2015.2202;
RA Lee J., Bandyopadhyay J., Lee J.I., Cho I., Park D., Cho J.H.;
RT "A role for peroxidasin PXN-1 in aspects of C. elegans development.";
RL Mol. Cells 38:51-57(2015).
RN [5]
RP FUNCTION.
RX PubMed=26194821; DOI=10.14348/molcells.2015.0124;
RA Cho I., Hwang G.J., Cho J.H.;
RT "pxn-1 and pxn-2 May Interact Negatively during Neuronal Development and
RT Aging in C. elegans.";
RL Mol. Cells 38:729-733(2015).
CC -!- FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen
CC peroxide and generates hypobromite as a reactive intermediate which
CC mediates the formation of sulfilimine cross-links between methionine
CC and hydroxylysine residues within an uncross-linked collagen IV NC1
CC hexamer (By similarity). Plays a role in the attachment of tissues and
CC in axonal guidance during early developmental stages (PubMed:25475546).
CC May functionally antagonize the peroxidasin pxn-2 to maintain neuronal
CC development (PubMed:20876652, PubMed:26194821).
CC {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:20876652,
CC ECO:0000269|PubMed:25475546, ECO:0000269|PubMed:26194821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29250; Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC Evidence={ECO:0000250|UniProtKB:Q92626};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC subunit. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:25475546}. Note=Localizes to the
CC extracellular space in between body wall muscle cells.
CC {ECO:0000269|PubMed:25475546}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral nerve cord, the dorsal
CC nerve cord, head neurons, GABAergic and cholinergic neurons, body wall
CC muscles, vulval muscles, uterine muscles, intestine, the hypodermis and
CC in coelomocytes. {ECO:0000269|PubMed:20876652,
CC ECO:0000269|PubMed:25475546}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis to adulthood.
CC {ECO:0000269|PubMed:25475546}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; BX284605; CCD71290.1; -; Genomic_DNA.
DR RefSeq; NP_505188.3; NM_072787.3.
DR AlphaFoldDB; Q1ENI8; -.
DR SMR; Q1ENI8; -.
DR BioGRID; 56017; 3.
DR STRING; 6239.ZK994.3; -.
DR PeroxiBase; 3359; CelPxd01.
DR iPTMnet; Q1ENI8; -.
DR EPD; Q1ENI8; -.
DR PaxDb; Q1ENI8; -.
DR PeptideAtlas; Q1ENI8; -.
DR EnsemblMetazoa; ZK994.3.1; ZK994.3.1; WBGene00004256.
DR GeneID; 191484; -.
DR KEGG; cel:CELE_ZK994.3; -.
DR UCSC; ZK994.3; c. elegans.
DR CTD; 191484; -.
DR WormBase; ZK994.3; CE40298; WBGene00004256; pxn-1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000168557; -.
DR HOGENOM; CLU_006087_0_0_1; -.
DR InParanoid; Q1ENI8; -.
DR OMA; FHRKYRA; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q1ENI8; -.
DR Reactome; R-CEL-209968; Thyroxine biosynthesis.
DR Reactome; R-CEL-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8941413; Events associated with phagocytolytic activity of PMN cells.
DR PRO; PR:Q1ENI8; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004256; Expressed in larva and 3 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:UniProtKB.
DR GO; GO:0048679; P:regulation of axon regeneration; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 1.10.640.10; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR InterPro; IPR034826; Peroxidasin_PXN-1_nema.
DR PANTHER; PTHR11475:SF74; PTHR11475:SF74; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Heme; Hydrogen peroxide; Immunoglobulin domain; Iron; Leucine-rich repeat;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1285
FT /note="Peroxidasin homolog pxn-1"
FT /id="PRO_0000319623"
FT DOMAIN 21..53
FT /note="LRRNT"
FT REPEAT 27..49
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 50..72
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 73..96
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 97..120
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 122..143
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 145..168
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 180..228
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT REPEAT 204..227
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 315..401
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 408..495
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REPEAT 998..1022
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 1049..1073
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 1168..1189
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 508..550
FT /evidence="ECO:0000255"
FT COMPBIAS 308..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 720
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 719
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 803
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 805
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 807
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 809
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 877
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 973
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 874
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 336..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 625..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 740..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 744..771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1076..1133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1174..1201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
SQ SEQUENCE 1285 AA; 146337 MW; B7110A400C54655D CRC64;
MNLYLLLLVI ATSSWQFVAG LECPVECTCD KKGLVVDCSS SGLTRIPKNI SRNVRSLVIR
NNRIHKLKRS DLEGFNQLET LVLTHNKIKI IEENVLDHLP ELKRLSLAHN ELVYIPPLCS
DSRPLASLNL KRNHIQFIDE QVLRYFPDLT QLDFSHNRIQ SLRTKLFDNL PALSHAHLHS
NPWHCDCRAS KVKALLQKVK WEKKVYCTNP VELRHQALDE VDDSALTCAR PAEESWTGEE
IKLTCAKNSS SKLVVWMYEN VEVDSSSLDG YEIHDTVITV PRKTNVNFMT CTYDFDHIPH
HRRLRQSQHQ GNGSPQFTYK PRDNSFREGS EVKVNCEVMG NPKPTINWYH NGKRFISSRK
RQLGLSNNVL RIYPFLEEDS GRYTCEAVNS VGKVRHAFSL DLISSVPPNI YEGPQSVSQN
LGGSVVFVCK ANGNPVPDYT WSFDGSTIGH IKGRFMVSDD GTELRISNIE KKDEGYYSCM
AGNPVGAMSA DAKLTVIGGE TRKAAAPQID EELLRAIAQK ARQNVENAVE KTRKQLTQDK
VTNTNDLKRL FRFSTPKQAV ELSKAREIYE ESVRLVREHV EKGLILNVDE LHPKNVSYES
VLHVTHVQAL MGLSGCHTGQ YKNPCTDTCF HHRYRSFDGQ CNNKNKPMTG VSLMPLRRLL
KPVYENGFNT PVGWEKGRLY NGYPLPNVRE VSRQLVATEN ITPHSKLSSM VMQWGQFVDH
DLTHTVTALS RHSYATGAFC NRTCENLDPC FNIPLSPNDP RVKSGSAKYP CIEFERSAAV
CGSGETSLVF NRVTYREQMN ALTSFLDASN VYGSNEVQAQ ELRDTYNNNG MLRFDITSEA
GKEYLPFEKD SNMDCRRNFS EENPIRCFLA GDLRANEQLA LAATHTIFIR EHNRIAKKLK
SMNGNWDGEI IYHETRKIVG AMMQHITYKH WMPIIFGGQA QMNKFVGTYQ GYDPDVDASV
TNAFATAAFR FGHTIINPSL FRLGNDFMPI KEGHIALHKA FFTPELVLTQ GGVDPLLRGL
FASPLKHPMP TQLLNMELIE KLFMKGHEVS LDLAVMNIQR SRDHGLPSYT EYRKFCNLPV
PVQWEDMKGY IKDDMIIQKL RGLYGVPQNI DLWVGGIVEE KLENGLFGPT FACIIGEQFR
KIRDGDRFWY EKDGVFTPEQ LREIKKITLA RLFCDNGDNI DRIQKDVFMY PGMDKENYGT
CQETEMMNLR AWSKCCDNVC PTMLDRILRS RHRGSRLHGC NQNGIWRPEG AKWIPQNEIC
TECVCQGSRV WCSTKEDCSD NRSPF
