PXDN1_CAEBR
ID PXDN1_CAEBR Reviewed; 1288 AA.
AC A8WQH2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Peroxidasin homolog {ECO:0000305};
DE EC=1.11.2.- {ECO:0000250|UniProtKB:Q92626};
DE Flags: Precursor;
GN Name=pxn-1 {ECO:0000312|WormBase:CBG01526};
GN ORFNames=CBG01526 {ECO:0000312|WormBase:CBG01526};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity).
CC May functionally antagonize the peroxidasin pxn-2 to maintain neuronal
CC development (By similarity). {ECO:0000250|UniProtKB:Q1ENI8,
CC ECO:0000250|UniProtKB:Q92626}.
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:0000250|UniProtKB:Q1ENI8}. Note=Localizes to the
CC extracellular space in between body wall muscle cells.
CC {ECO:0000250|UniProtKB:Q1ENI8}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; HE601420; CAP22730.3; -; Genomic_DNA.
DR RefSeq; XP_002635355.1; XM_002635309.1.
DR STRING; 6238.CBG01526; -.
DR PRIDE; A8WQH2; -.
DR GeneID; 8577351; -.
DR KEGG; cbr:CBG_01526; -.
DR CTD; 8577351; -.
DR WormBase; CBG01526; CBP43088; WBGene00024751; Cbr-pxn-1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_0_0_1; -.
DR InParanoid; A8WQH2; -.
DR OMA; FHRKYRA; -.
DR OrthoDB; 276568at2759; -.
DR Proteomes; UP000008549; Chromosome V.
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: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 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; PS51450; LRR; 5.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 3: Inferred from homology;
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1288
FT /note="Peroxidasin homolog"
FT /id="PRO_0000319622"
FT DOMAIN 17..51
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 314..400
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REPEAT 356..381
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 387..412
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT DOMAIN 407..494
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 ACT_SITE 719
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 718
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 802
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 804
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 806
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 808
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 876
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 972
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 873
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 335..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 428..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 624..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 739..749
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 743..770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1075..1132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 1173..1200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
SQ SEQUENCE 1288 AA; 146519 MW; 86E1176F4632B3A4 CRC64;
MNLLLYLLLL VPWVLGSEDG CPAKCTCDKK GFTVDCSNAG LTRIPKGISS NVRSLVLRNN
RIHTLIKSDL EGFPLLESLV LTHNKIKVVE ENILDHLPEL KRLSLSHNLL VYIPPLASES
RPLASLNLKR NHIQFIDERW LLQYFPELVQ IDLSHNRIQS LRTKLFENLP SLTHAHLHAN
PWNCDCRVTK VKALLRKVEW ERKAYCTNPV ELRHQAIDEV EESLLKCAKP EEESWTGDEF
KLVCTKNASS SRPVVWLYEN AEVDSSSLDG YEIHDSVITV PRKTNVNQMT CTYDYEHVPH
HRRLRQSHHS NGAPQFTYKP RDNSYREGSE VKVNCEVMGT PKPSITWYHN GVRFASSRKK
QLGLSNNVLR IYPFLEEDSG RYTCEAVNSL GKVSHTFSLD LISSIPPNIY EGPQSVSQNI
GGEVVFVCKA KGNPTPDYTW SFDGSTIGHI KGRFMVSDDG TELXISNIEK KDEGYYSCMA
GNPVGAMSAD AKLTVIGGET RKSSTPQIDE ELLRAIAQKA RQNVESAVEK TRKQLNQDKI
TNTNDLKRLF RFSTPKQAVE LSKAREIYEE SVRLVREHVE KGLILNVDEL HPNNVSYESV
LHVTHVQALM GLSGCHTGQF KNPCTDTCFH NKYRSFDGQC NNKNKPMNGV SLMPLRRLLK
PVYENGFNTP VGWEKGKLYN GYPMPNVREV SRQLVATETI TPHRKLSSMV MQWGQFVDHD
LTHTVTALSR HSYATGAFCN RTCDNLDPCF NIPLSPSDPR VISESAKYPC IEFERSAAVC
GSGETSLVFN RVTYREQMNA LTSFLDASNV YGSNEVQAQE LRDTYNNNGQ LRYDITSAAG
KEYLPFEKDS NMDCRRNFSE ENPIRCFLAG DLRANEQLAL AATHTIFVRE HNRIAKKLKK
MNGNWDGEVI YHETRKIIGA MMQHITFKHW LPVVFGGQEQ MDKFVGKYQG YDPAIDSSVT
NAFATAAFRF GHTIINPTLF RLGNDFMSIK QGHIALHKAF FTPELVLTEG GIDPLLRGLF
ASPLKHPMPT QLLNMELIEK LFMKGHEVSL DLAVMNIQRS RDHGLPSYTE YRQFCNLPVP
ARWEDMKGYI KDDMIIQKLR GLYGVPQNID LWVGGIVEEK LENGLFGPTF ACIIGEQFRK
MRDGDRFWYE KDGVFTPEQM KEIKKVTLAR LLCDNGDEID RIQKDVFMYP GKEKENYGRC
EDTEMMDLKA WSKCCDDVCP TMLDRILRSR HRGSRLHGCN QNGLWRPEGA KWIPPNEYCT
EEAVFGAPPK KTVLTTEVHS SQRNSVLY
