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Protein

Peroxidase skpo-1

Gene

skpo-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in hypodermal immune response against some types of bacterial infection. Probably utilizes H2O2 produced by the NADPH oxidase bli-3. May play a role in cuticule biosynthesis.1 Publication1 Publication

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei222 – 2221Proton acceptorPROSITE-ProRule annotation
Sitei332 – 3321Transition state stabilizerPROSITE-ProRule annotation
Metal bindingi428 – 4281Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: UniProtKB

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • defense response to Gram-positive bacterium Source: UniProtKB
  • determination of adult lifespan Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • negative regulation of gene expression Source: UniProtKB
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei4139. CelPxd03.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase skpo-11 Publication (EC:1.11.1.7By similarity)
Alternative name(s):
ShKT and peroxidase domain-containing protein 1Imported
Gene namesi
Name:skpo-1Imported
ORF Names:F49E12.1Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiF49E12.1; CE03378; WBGene00009897; skpo-1.

Pathology & Biotechi

Disruption phenotypei

Knockouts show increased susceptibility to infection with E.faecalis but not with P.aeruginosa, increased levels of H2O2 upon infection and a slightly shorter life span. Fertile animals show a bagging phenotype due to embryos being retained in the body and an increase of clec-60 mRNA levels upon infection. 50% of knockouts also have a dumpy phenotype. RNAi-mediated knockdown of the protein also results in higher susceptibility to infection by E.faecalis but not in a decreased life span or morphological changes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 655636Peroxidase skpo-1Sequence analysisPRO_0000431239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 56PROSITE-ProRule annotation
Disulfide bondi29 ↔ 49PROSITE-ProRule annotation
Disulfide bondi38 ↔ 53PROSITE-ProRule annotation
Disulfide bondi133 ↔ 150PROSITE-ProRule annotation
Disulfide bondi520 ↔ 576PROSITE-ProRule annotation
Disulfide bondi617 ↔ 642PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ20616.
PaxDbiQ20616.
PRIDEiQ20616.

Expressioni

Tissue specificityi

Exclusively expressed in hypodermis.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6239.F49E12.1.

Structurei

3D structure databases

ProteinModelPortaliQ20616.
SMRiQ20616. Positions 142-655.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 5635ShKTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
Contains 1 ShKT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
InParanoidiQ20616.
OMAiKYRSMDG.
OrthoDBiEOG7D2FD6.
PhylomeDBiQ20616.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR003582. ShKT_dom.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00254. ShKT. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q20616-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLLFSILL IYLIQLVRSE ECTDKHIHCF FWSQEGECEV NPRWMKKHCQ
60 70 80 90 100
KACGTCSLTS PTPLTRQQDV PTARTFDDQQ DRQFLPSRPS SIPEGCNSVM
110 120 130 140 150
TVEAETRRIF SSGQLTARFR QQMCAEEQVA PDCSINQCFH KKYRSMDGTC
160 170 180 190 200
NNLQNPVKGA AFTAFTRLMP AAYDDGFNTL VSASRRNRPN PREVSVFLLS
210 220 230 240 250
SERSLPGHVN SLLMLFGQFV SHDITSNAAQ NFCGCQNSGP MCASIFAPPS
260 270 280 290 300
DRSRRCIPFT RSFPICGTGQ FGRVREQLNM NTAAIDASLI YGSEAITARS
310 320 330 340 350
LRFAAMLRTS MIGGRMFPPN TNPGSLTAGD GRAILFVGLA ALHTSFLRLH
360 370 380 390 400
NNVAARLQNM NRHWNADRIF QESRKIVGGI VQVITYQEFV PELIGDASKT
410 420 430 440 450
ILGAYNGYNP NVEIGVLNEF AAGAYRLHGM IQETYPLVNS QFQEVNRYRF
460 470 480 490 500
IDGVNNINHV LNNIDAIYRG MMTVPVRSPQ RLTTSVTERL FGGSVDMAAV
510 520 530 540 550
NIQRGRDHGL RSYNDYRRFC NLRPITSFND WPEVPDENVR QRIGQLYRTP
560 570 580 590 600
DDLDFYVGGI LEQPAAGSLL GATFACVIGK QFERLRDGDR FYYENPGVFT
610 620 630 640 650
SPQLAELKRT TLSWVLCQTG DNMVRVGRRA FDIENGSRAV PCSSITGLNL

EAWRE
Length:655
Mass (Da):73,496
Last modified:November 1, 1996 - v1
Checksum:iC8225BAFF8E2164E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z66520 Genomic DNA. Translation: CAA91388.1.
PIRiT22448.
RefSeqiNP_495768.1. NM_063367.5.
UniGeneiCel.5463.

Genome annotation databases

EnsemblMetazoaiF49E12.1; F49E12.1; WBGene00009897.
GeneIDi174340.
KEGGicel:CELE_F49E12.1.
UCSCiF49E12.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z66520 Genomic DNA. Translation: CAA91388.1.
PIRiT22448.
RefSeqiNP_495768.1. NM_063367.5.
UniGeneiCel.5463.

3D structure databases

ProteinModelPortaliQ20616.
SMRiQ20616. Positions 142-655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F49E12.1.

Protein family/group databases

PeroxiBasei4139. CelPxd03.

Proteomic databases

EPDiQ20616.
PaxDbiQ20616.
PRIDEiQ20616.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF49E12.1; F49E12.1; WBGene00009897.
GeneIDi174340.
KEGGicel:CELE_F49E12.1.
UCSCiF49E12.1. c. elegans.

Organism-specific databases

CTDi174340.
WormBaseiF49E12.1; CE03378; WBGene00009897; skpo-1.

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
InParanoidiQ20616.
OMAiKYRSMDG.
OrthoDBiEOG7D2FD6.
PhylomeDBiQ20616.

Miscellaneous databases

NextBioi883622.
PROiQ20616.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR003582. ShKT_dom.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00254. ShKT. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  2. "The SKPO-1 peroxidase functions in the hypodermis to protect Caenorhabditis elegans from bacterial infection."
    Tiller G.R., Garsin D.A.
    Genetics 197:515-526(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSKPO1_CAEEL
AccessioniPrimary (citable) accession number: Q20616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.