ID   PLSP3_LOTGI             Reviewed;         294 AA.
AC   B3A0Q8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Peroxidase-like protein 3;
DE   Flags: Fragment;
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|Ref.1};
RA   Richardson P., Lucas S., Rokhsar D., Wang M., Lindquist E.A.;
RT   "DOE Joint Genome Institute Lottia gigantea EST project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 11-18 AND 249-265, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23145877; DOI=10.1111/febs.12062;
RA   Marie B., Jackson D.J., Ramos-Silva P., Zanella-Cleon I., Guichard N.,
RA   Marin F.;
RT   "The shell-forming proteome of Lottia gigantea reveals both deep
RT   conservations and lineage-specific novelties.";
RL   FEBS J. 280:214-232(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23145877}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC       organic matrix of calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298}.
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DR   EMBL; FC622773; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC631979; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3A0Q8; -.
DR   SMR; B3A0Q8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
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   Direct protein sequencing; Glycoprotein; Secreted.
FT   CHAIN           1..294
FT                   /note="Peroxidase-like protein 3"
FT                   /id="PRO_0000415264"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  33212 MW;  D7D70E3837451C33 CRC64;
     ADKIFEETKK IINAFIQRIT YVEFLPEILN AETLKNNELN EGIYGYEEFT DPRISNVFST
     AAFQFIHSLT PSSIEFDGTE TPLMDLFNNQ NFLFLDTEKV AVYMMSSAGE PMDRFFSKQL
     TDHYFQSGNI SFDLVAQIIQ RGRDHGLPSY NTFRRHCGLP RLPHFYAMEA ANVLKAVYHN
     IDDVDVFVGG MVEIPLPGSL LGPTFSCLIA RQFRDTKFGD SHWYESADPK KGFNEGQLKS
     IKAMSAAKIL CDGFGLSLIP ENPFRVTSPS NPMVVCADLP GLDFQPWFLL GNQI