ID SKPO1_CAEEL Reviewed; 655 AA.
AC Q20616;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Peroxidase skpo-1 {ECO:0000303|PubMed:9851916};
DE EC=1.11.1.7 {ECO:0000250|UniProtKB:Q23490};
DE AltName: Full=ShKT and peroxidase domain-containing protein 1 {ECO:0000312|WormBase:F49E12.1};
DE Flags: Precursor;
GN Name=skpo-1 {ECO:0000312|WormBase:F49E12.1};
GN ORFNames=F49E12.1 {ECO:0000312|WormBase:F49E12.1};
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, TISSUE SPECIFICITY, 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).
CC -!- FUNCTION: Involved in hypodermal immune response against some types of
CC bacterial infection. Probably utilizes H(2)O(2) produced by the NADPH
CC oxidase bli-3. May play a role in cuticule biosynthesis.
CC {ECO:0000269|PubMed:24621828, ECO:0000303|PubMed:24621828}.
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:0000255|PROSITE-ProRule:PRU00298};
CC -!- TISSUE SPECIFICITY: Exclusively expressed in hypodermis.
CC {ECO:0000269|PubMed:24621828}.
CC -!- DISRUPTION PHENOTYPE: Knockouts show increased susceptibility to
CC infection with E.faecalis but not with P.aeruginosa, increased levels
CC of H(2)O(2) upon infection and a slightly shorter life span. Fertile
CC animals show a bagging phenotype due to embryos being retained in the
CC body and an increase of clec-60 mRNA levels upon infection. 50% of
CC knockouts also have a dumpy phenotype. RNAi-mediated knockdown of the
CC protein also results in higher susceptibility to infection by
CC E.faecalis but not in a decreased life span or morphological changes.
CC {ECO:0000269|PubMed:24621828}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; Z66520; CAA91388.1; -; Genomic_DNA.
DR PIR; T22448; T22448.
DR RefSeq; NP_495768.1; NM_063367.5.
DR AlphaFoldDB; Q20616; -.
DR SMR; Q20616; -.
DR BioGRID; 39669; 3.
DR STRING; 6239.F49E12.1.1; -.
DR PeroxiBase; 4139; CelPxd03.
DR EPD; Q20616; -.
DR PaxDb; 6239-F49E12-1; -.
DR PeptideAtlas; Q20616; -.
DR EnsemblMetazoa; F49E12.1.1; F49E12.1.1; WBGene00009897.
DR GeneID; 174340; -.
DR KEGG; cel:CELE_F49E12.1; -.
DR UCSC; F49E12.1; c. elegans.
DR AGR; WB:WBGene00009897; -.
DR WormBase; F49E12.1; CE03378; WBGene00009897; skpo-1.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_4_0_1; -.
DR InParanoid; Q20616; -.
DR OMA; NRYRFID; -.
DR OrthoDB; 1021077at2759; -.
DR PhylomeDB; Q20616; -.
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:Q20616; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009897; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.10.1940; -; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR11475:SF4; LD42267P; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00254; ShKT; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Heme; Immunity; Innate immunity; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..655
FT /note="Peroxidase skpo-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431239"
FT DOMAIN 22..56
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 428
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 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 22..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 29..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 38..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 133..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 520..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 617..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
SQ SEQUENCE 655 AA; 73496 MW; C8225BAFF8E2164E CRC64;
MKSLLFSILL IYLIQLVRSE ECTDKHIHCF FWSQEGECEV NPRWMKKHCQ KACGTCSLTS
PTPLTRQQDV PTARTFDDQQ DRQFLPSRPS SIPEGCNSVM TVEAETRRIF SSGQLTARFR
QQMCAEEQVA PDCSINQCFH KKYRSMDGTC NNLQNPVKGA AFTAFTRLMP AAYDDGFNTL
VSASRRNRPN PREVSVFLLS SERSLPGHVN SLLMLFGQFV SHDITSNAAQ NFCGCQNSGP
MCASIFAPPS DRSRRCIPFT RSFPICGTGQ FGRVREQLNM NTAAIDASLI YGSEAITARS
LRFAAMLRTS MIGGRMFPPN TNPGSLTAGD GRAILFVGLA ALHTSFLRLH NNVAARLQNM
NRHWNADRIF QESRKIVGGI VQVITYQEFV PELIGDASKT ILGAYNGYNP NVEIGVLNEF
AAGAYRLHGM IQETYPLVNS QFQEVNRYRF IDGVNNINHV LNNIDAIYRG MMTVPVRSPQ
RLTTSVTERL FGGSVDMAAV NIQRGRDHGL RSYNDYRRFC NLRPITSFND WPEVPDENVR
QRIGQLYRTP DDLDFYVGGI LEQPAAGSLL GATFACVIGK QFERLRDGDR FYYENPGVFT
SPQLAELKRT TLSWVLCQTG DNMVRVGRRA FDIENGSRAV PCSSITGLNL EAWRE
//
