HPX2_CAEEL
ID HPX2_CAEEL Reviewed; 718 AA.
AC P90820;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Heme peroxidase 2 {ECO:0000303|PubMed:30695063, ECO:0000312|WormBase:F09F3.5};
DE EC=1.11.1.7 {ECO:0000250|UniProtKB:Q23490};
DE Contains:
DE RecName: Full=Heme peroxidase 2 light chain {ECO:0000255};
DE Contains:
DE RecName: Full=Heme peroxidase 2 heavy chain {ECO:0000255};
DE Flags: Precursor;
GN Name=hpx-2 {ECO:0000303|PubMed:30695063, ECO:0000312|WormBase:F09F3.5};
GN ORFNames=F09F3.5 {ECO:0000312|WormBase:F09F3.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24621828; DOI=10.1534/genetics.113.160606;
RA Tiller G.R., Garsin D.A.;
RT "The SKPO-1 peroxidase functions in the hypodermis to protect
RT Caenorhabditis elegans from bacterial infection.";
RL Genetics 197:515-526(2014).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 133-ARG--ARG-718; 210-LEU--ARG-718 AND ARG-373.
RX PubMed=30695063; DOI=10.1371/journal.pgen.1007944;
RA Liu Y., Kaval K.G., van Hoof A., Garsin D.A.;
RT "Heme peroxidase HPX-2 protects Caenorhabditis elegans from pathogens.";
RL PLoS Genet. 15:E1007944-E1007944(2019).
CC -!- FUNCTION: Peroxidase which is involved in maintaining the cuticle
CC integrity in the hypodermis and pharynx (PubMed:30695063). It thus
CC plays a role in conferring resistance against Gram-positive bacteria
CC such as E.faecalis, S.aureus and C.diphtheriae, and yeast such as
CC C.albicans (PubMed:24621828, PubMed:30695063).
CC {ECO:0000269|PubMed:24621828, ECO:0000269|PubMed:30695063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000250|UniProtKB:Q23490};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q23490};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis and gland cells of the
CC pharynx (PubMed:30695063). Specifically, there is low and transient
CC expression from the distal bulb of the pharynx to the anterior of the
CC buccal cavity (PubMed:30695063). Whole body expression levels increase
CC upon entry into the dauer phase (PubMed:30695063).
CC {ECO:0000269|PubMed:30695063}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC survival in response to infection by E.faecalis.
CC {ECO:0000269|PubMed:24621828, ECO:0000269|PubMed:30695063}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; BX284605; CAB02910.1; -; Genomic_DNA.
DR PIR; T20673; T20673.
DR RefSeq; NP_506432.1; NM_074031.3.
DR AlphaFoldDB; P90820; -.
DR SMR; P90820; -.
DR DIP; DIP-24859N; -.
DR STRING; 6239.F09F3.5; -.
DR PeroxiBase; 4147; CelPxt05.
DR EPD; P90820; -.
DR PaxDb; P90820; -.
DR EnsemblMetazoa; F09F3.5.1; F09F3.5.1; WBGene00008627.
DR GeneID; 179880; -.
DR KEGG; cel:CELE_F09F3.5; -.
DR UCSC; F09F3.5; c. elegans.
DR CTD; 179880; -.
DR WormBase; F09F3.5; CE20661; WBGene00008627; hpx-2.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_5_0_1; -.
DR InParanoid; P90820; -.
DR OMA; NGQENFG; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P90820; -.
DR PRO; PR:P90820; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..146
FT /evidence="ECO:0000255"
FT /id="PRO_0000447484"
FT CHAIN 147..259
FT /note="Heme peroxidase 2 light chain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT /id="PRO_0000447485"
FT CHAIN 260..718
FT /note="Heme peroxidase 2 heavy chain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT /id="PRO_0000447486"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 477
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 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:30695063"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 149..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 262..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 358..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 682..705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MUTAGEN 133..718
FT /note="Missing: In gk252521; reduced survival in response
FT to infection by E.faecalis, C.albicans, S.aureus and
FT C.diphtheriae. Slightly reduced survival in response to
FT infection by E.coli. Loss of cuticle integrity."
FT /evidence="ECO:0000269|PubMed:30695063"
FT MUTAGEN 210..718
FT /note="Missing: In dg047; reduced survival in response to
FT infection by E.faecalis, C.albicans, S.aureus and
FT C.diphtheriae. Slightly reduced survival in response to
FT infection by E.coli. Loss of cuticle integrity."
FT /evidence="ECO:0000269|PubMed:30695063"
FT MUTAGEN 373
FT /note="R->A: In syb482; reduced survival in response to
FT infection by E.faecalis."
FT /evidence="ECO:0000269|PubMed:30695063"
SQ SEQUENCE 718 AA; 81183 MW; 7729071EF145B09A CRC64;
MNLKPTILLF TILFLKCATF EVNEETERIV EDAVMRALDS RASENSESEQ TSQHIIVSQQ
ANSDSKSAQF TGEVLEEATR ILVREFGLEI LPAANEVIER WRNEEEELLQ SSETTTTTEH
PDPTRSKRSA IFRSKRQANR RCSSPPINCN NRFHTSIRSI TGLCNNRQNS DLGNSVSPLR
RILGAASYAD GLGRIRTRSV NGGELPSARL ISNRIHDDRN NQVFSPSINH LHMIIGQFIA
HDVVFMPSSV ARDGGALDCS ACNSPQRVSP NCAPITIPRN DPYFNTPCMR LTRALNGQEN
FGVRSQIGQN SHFLDLSPVY GSADCEAETV RSFQEGKMLT FDDLGYTLPP QNANDSNCQS
SAPFHCFTCG DFRNSLHPAL IPVHTILIKE HNRLAEQVRV ARPRFNDEQI FQLVRKIMIG
MWQHIVYNEY IPKYLPRRTI RNFALRPLRN GVHRGYSTSV DPSISAEFAG AAFRFGHSQS
RFDFPRLTEN GRPAGNYDLG NDIFYADQMY LTRIGGWEPV MNGMVRMPAM KSDRYFSFGI
RNQMFEIRGR NGSGVDLVSI NIQRGRDMGL FPYIQYRQLV GLPTVTSFNE LNTTFSQENI
QALRNVYSDP ADIDLYVGIM LEEPLSGGQL GPTASFMIGE QFRALKRGDR FFYESIAEGT
DNFTQEEISE LRNKTSLAKI ICTNMDFAAR INTDIFDHRS RQVACTSLPQ LDIDRFLR
