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Protein

Peroxidase mlt-7

Gene

mlt-7

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

Functioni

Plays an essential role in cuticle biogenesis. Required in combination with bli-3 for correct formation of cross-links in cuticle collagens.1 Publication

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei271 – 2711Proton acceptorPROSITE-ProRule annotation
Metal bindingi272 – 2721CalciumPROSITE-ProRule annotation
Metal bindingi335 – 3351CalciumPROSITE-ProRule annotation
Metal bindingi337 – 3371Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi339 – 3391CalciumPROSITE-ProRule annotation
Metal bindingi341 – 3411CalciumPROSITE-ProRule annotation
Sitei396 – 3961Transition state stabilizerPROSITE-ProRule annotation
Metal bindingi493 – 4931Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cuticle development involved in collagen and cuticulin-based cuticle molting cycle Source: WormBase
  • nematode larval development Source: WormBase
  • peptide cross-linking Source: WormBase
  • post-embryonic body morphogenesis Source: WormBase
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Oxidoreductase, Peroxidase

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei4141. CelPxd05.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase mlt-71 Publication (EC:1.11.1.7)
Alternative name(s):
Molting defective protein 71 Publication
Short name:
MoLT-71 Publication
Cleaved into the following 2 chains:
Gene namesi
Name:mlt-7Imported
ORF Names:ZK430.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiZK430.8; CE05084; WBGene00022743; mlt-7.

Pathology & Biotechi

Disruption phenotypei

Gross morphological abnormalities causing larval arrest with associated molt defects and low levels of embryonic lethality. Cuticle function and integrity are also impaired.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 178154Sequence analysisPRO_0000391682Add
BLAST
Chaini179 – 281103Peroxidase mlt-7 light chainSequence analysisPRO_0000391683Add
BLAST
Chaini282 – 724443Peroxidase mlt-7 heavy chainSequence analysisPRO_0000391684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi7 – 71N-linked (GlcNAc...)Sequence analysis
Disulfide bondi181 ↔ 198Sequence analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi284 ↔ 294Sequence analysis
Glycosylationi509 – 5091N-linked (GlcNAc...)1 Publication
Disulfide bondi588 ↔ 645Sequence analysis
Glycosylationi617 – 6171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi686 ↔ 710Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ23490.
PaxDbiQ23490.
PRIDEiQ23490.

Expressioni

Tissue specificityi

Expressed in the hypodermal cells, specifically the head and seam/body.1 Publication

Developmental stagei

Expressed in all adult and larval stages. Expression is cyclical and coincides with each of the larval molts, peaking at 12, 18, 24, and 30h post-hatching.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6239.ZK430.8.

Structurei

3D structure databases

ProteinModelPortaliQ23490.
SMRiQ23490. Positions 191-722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 7635ShKTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
InParanoidiQ23490.
OMAiLACGTCT.
OrthoDBiEOG7RFTN1.
PhylomeDBiQ23490.

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.

Q23490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRLHRNLSL LFLICILNEY RIESQTLSPP ITDRFKCLTN GCCDHHEWCR
60 70 80 90 100
FWASIGECNA NKDWMTENCQ LACGTCTAPA APLLPVTTTA SSFNGGGFVQ
110 120 130 140 150
TTTQSSGPTT TITIPPSSLT SVTSCERVKD SIAQASELMS ISRLINPVED
160 170 180 190 200
NFGRNMLSID DITRSVPTGC VPQLSDVGVD CRKSLCYHLM YRTLDGTCNN
210 220 230 240 250
LEKPMQGAAF RRFNRHFPAQ YDDGKGEPIS SLNQSRPSAR EANRVMLSSA
260 270 280 290 300
QSVVHDKFNN MMMQWGQFMS HDMSKTTLQP SANCKTCDPV PSKCMPIPIG
310 320 330 340 350
EKDPNLGFKS KQCLKVSRSA PICRVEPREQ LNENTAYIDG SMIYGSSLKD
360 370 380 390 400
LHKFRDGRTG FLRVTRFNNQ NVLPFDQSKC ANKDKCTASF TAGDIRANLF
410 420 430 440 450
IGLSSLHIMF AREHNRIAQK LTELNPTWSG DRVFQEARKI VGAQIQNVLY
460 470 480 490 500
KEYLPKLLGV SFDKVIGPYK GYDTNVDATI ANEFTTSAFR FGHGMIEEFY
510 520 530 540 550
KRVDLSGNNI THGGFFFGDG VFKSGKILFE GGVDPIIRGF MTTAVKRPHR
560 570 580 590 600
MTPAITEKMF GSTDLGSLNI QRGRDHGIPS YNKMRQFCGL KSANTFDDFA
610 620 630 640 650
DMILDRNLRA GLARNYNTTN DVDFYVGSML EDPVIGGLVG TTLSCAIGEQ
660 670 680 690 700
FKRARDGDRF YFENPGIFTR SQMEEIKKSS LSRIICDNAD NFELVSQDAF
710 720
LLPGSNLTPC SKIPKMDLSK WRAL
Length:724
Mass (Da):80,829
Last modified:November 1, 1996 - v1
Checksum:i54986FA3545753AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080155 Genomic DNA. Translation: CCD61675.1.
PIRiT27858.
RefSeqiNP_494777.1. NM_062376.4.
UniGeneiCel.8878.

Genome annotation databases

EnsemblMetazoaiZK430.8; ZK430.8; WBGene00022743.
GeneIDi173775.
KEGGicel:CELE_ZK430.8.
UCSCiZK430.8. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080155 Genomic DNA. Translation: CCD61675.1.
PIRiT27858.
RefSeqiNP_494777.1. NM_062376.4.
UniGeneiCel.8878.

3D structure databases

ProteinModelPortaliQ23490.
SMRiQ23490. Positions 191-722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.ZK430.8.

Protein family/group databases

PeroxiBasei4141. CelPxd05.

Proteomic databases

EPDiQ23490.
PaxDbiQ23490.
PRIDEiQ23490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK430.8; ZK430.8; WBGene00022743.
GeneIDi173775.
KEGGicel:CELE_ZK430.8.
UCSCiZK430.8. c. elegans.

Organism-specific databases

CTDi173775.
WormBaseiZK430.8; CE05084; WBGene00022743; mlt-7.

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
InParanoidiQ23490.
OMAiLACGTCT.
OrthoDBiEOG7RFTN1.
PhylomeDBiQ23490.

Miscellaneous databases

PROiQ23490.

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 N2.
  2. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans."
    Thein M.C., Winter A.D., Stepek G., McCormack G., Stapleton G., Johnstone I.L., Page A.P.
    J. Biol. Chem. 284:17549-17563(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMLT7_CAEEL
AccessioniPrimary (citable) accession number: Q23490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 118 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.