MLT7_CAEEL
ID MLT7_CAEEL Reviewed; 724 AA.
AC Q23490;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peroxidase mlt-7 {ECO:0000303|PubMed:19406744};
DE EC=1.11.1.7;
DE AltName: Full=Molting defective protein 7 {ECO:0000303|PubMed:19406744};
DE Short=MoLT-7 {ECO:0000303|PubMed:19406744};
DE Contains:
DE RecName: Full=Peroxidase mlt-7 light chain;
DE Contains:
DE RecName: Full=Peroxidase mlt-7 heavy chain;
DE Flags: Precursor;
GN Name=mlt-7 {ECO:0000312|WormBase:ZK430.8}; ORFNames=ZK430.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19406744; DOI=10.1074/jbc.m900831200;
RA Thein M.C., Winter A.D., Stepek G., McCormack G., Stapleton G.,
RA Johnstone I.L., Page A.P.;
RT "Combined extracellular matrix cross-linking activity of the peroxidase
RT MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability
RT in Caenorhabditis elegans.";
RL J. Biol. Chem. 284:17549-17563(2009).
CC -!- FUNCTION: Plays an essential role in cuticle biogenesis. Required in
CC combination with bli-3 for correct formation of cross-links in cuticle
CC collagens. {ECO:0000269|PubMed:19406744}.
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:0000269|PubMed:19406744};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000305|PubMed:19406744};
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermal cells, specifically the
CC head and seam/body. {ECO:0000269|PubMed:19406744}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all adult and larval stages.
CC Expression is cyclical and coincides with each of the larval molts,
CC peaking at 12, 18, 24, and 30 hours post-hatching.
CC {ECO:0000269|PubMed:19406744}.
CC -!- DISRUPTION PHENOTYPE: Gross morphological abnormalities causing larval
CC arrest with associated molt defects and low levels of embryonic
CC lethality. Cuticle function and integrity are also impaired.
CC {ECO:0000269|PubMed:19406744}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; FO080155; CCD61675.1; -; Genomic_DNA.
DR PIR; T27858; T27858.
DR RefSeq; NP_494777.1; NM_062376.4.
DR AlphaFoldDB; Q23490; -.
DR SMR; Q23490; -.
DR BioGRID; 39131; 13.
DR STRING; 6239.ZK430.8; -.
DR PeroxiBase; 4141; CelPxd05.
DR iPTMnet; Q23490; -.
DR EPD; Q23490; -.
DR PaxDb; Q23490; -.
DR PeptideAtlas; Q23490; -.
DR PRIDE; Q23490; -.
DR EnsemblMetazoa; ZK430.8.1; ZK430.8.1; WBGene00022743.
DR GeneID; 173775; -.
DR KEGG; cel:CELE_ZK430.8; -.
DR UCSC; ZK430.8; c. elegans.
DR CTD; 173775; -.
DR WormBase; ZK430.8; CE05084; WBGene00022743; mlt-7.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_4_0_1; -.
DR InParanoid; Q23490; -.
DR OMA; ICDNGDH; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q23490; -.
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:Q23490; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00022743; Expressed in larva and 3 other tissues.
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; IDA:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018149; P:peptide cross-linking; IMP:WormBase.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
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 InterPro; IPR003582; ShKT_dom.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00254; ShKT; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Calcium; Developmental protein; Disulfide bond; Glycoprotein; Heme; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..178
FT /evidence="ECO:0000255"
FT /id="PRO_0000391682"
FT CHAIN 179..281
FT /note="Peroxidase mlt-7 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000391683"
FT CHAIN 282..724
FT /note="Peroxidase mlt-7 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000391684"
FT DOMAIN 42..76
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 493
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 396
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..198
FT /evidence="ECO:0000255"
FT DISULFID 284..294
FT /evidence="ECO:0000255"
FT DISULFID 588..645
FT /evidence="ECO:0000255"
FT DISULFID 686..710
FT /evidence="ECO:0000255"
SQ SEQUENCE 724 AA; 80829 MW; 54986FA3545753AA CRC64;
MRRLHRNLSL LFLICILNEY RIESQTLSPP ITDRFKCLTN GCCDHHEWCR FWASIGECNA
NKDWMTENCQ LACGTCTAPA APLLPVTTTA SSFNGGGFVQ TTTQSSGPTT TITIPPSSLT
SVTSCERVKD SIAQASELMS ISRLINPVED NFGRNMLSID DITRSVPTGC VPQLSDVGVD
CRKSLCYHLM YRTLDGTCNN LEKPMQGAAF RRFNRHFPAQ YDDGKGEPIS SLNQSRPSAR
EANRVMLSSA QSVVHDKFNN MMMQWGQFMS HDMSKTTLQP SANCKTCDPV PSKCMPIPIG
EKDPNLGFKS KQCLKVSRSA PICRVEPREQ LNENTAYIDG SMIYGSSLKD LHKFRDGRTG
FLRVTRFNNQ NVLPFDQSKC ANKDKCTASF TAGDIRANLF IGLSSLHIMF AREHNRIAQK
LTELNPTWSG DRVFQEARKI VGAQIQNVLY KEYLPKLLGV SFDKVIGPYK GYDTNVDATI
ANEFTTSAFR FGHGMIEEFY KRVDLSGNNI THGGFFFGDG VFKSGKILFE GGVDPIIRGF
MTTAVKRPHR MTPAITEKMF GSTDLGSLNI QRGRDHGIPS YNKMRQFCGL KSANTFDDFA
DMILDRNLRA GLARNYNTTN DVDFYVGSML EDPVIGGLVG TTLSCAIGEQ FKRARDGDRF
YFENPGIFTR SQMEEIKKSS LSRIICDNAD NFELVSQDAF LLPGSNLTPC SKIPKMDLSK
WRAL
