ID   PLSP_PINMG              Reviewed;         793 AA.
AC   H2A0M7;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Peroxidase-like protein;
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 431-447 AND 633-648, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle edge
CC       and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298}.
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DR   EMBL; HE610394; CCE46168.1; -; mRNA.
DR   PRIDE; H2A0M7; -.
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; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..793
FT                   /note="Peroxidase-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000418021"
SQ   SEQUENCE   793 AA;  88310 MW;  DD91EEE3CD70A1E4 CRC64;
     MNLFICHVFL LLLHGYLIIC QDIPPDTIIS AVNTAQQEVT QREASSFSQQ QARASVAAFA
     GAPQPAAVLA ASRPARTGLD RFNRRNDPQR NTELSIGGQV TQRATLALRS SDPASAAAPA
     ARTLTPLDAR APAAGFSASS TMTFRNAAAQ SCTDSRPVTV CDPQQRYRET DGQCNNLVFP
     SFPSGAFKLG AAFTAQGRFL FPAYDDGVSS PRIRSVIPGF LLPNARLVSR NVHSGTAFDS
     DRHTPFLTHF GQFIDHDIVS TPETEPKFTM PNSHCCLEPN LEECFNINFE PDPLLQGSCI
     RFNRADTAPS YFCNPGPRLQ QNQRSSFVDG TMVYGWDVEQ ENRLREPGTG RLISEGDDQL
     KLEPVADPLN PPCFPVDNRC FEAGDHRSLE TVPLTVMHIM FLRRHNLIVQ ELQNLPLPWT
     PELLFQEAKR IVVAELQHIT YNEFLPRVLG PQFMTIFRLW PAPLFSDTYS PLVDPRTTSG
     FSVAAYRFGH SLVRNVHDQI GPGGLPVNNL LLQDHFDRLQ THLNVFPGGN TEGFARWMKL
     SQKSRADRTL VDGLQNNLFP CEDPDCPMGG GVTKSFDLAA LNIQRGRDHG LPPYTAWRYW
     CTGRRAFVFT PNAVGLSDHS PFEANILSNT YRHVDDIDLF TGGMTEMRRP GALLGPTLSC
     IIGLQFSNYK RGDRFFYERP DPVMAFTPGQ LQAIKETSLA KILCSTMRSF SNVQIBAMDR
     VSPSNPIVNC DELRSQDIIA KIPFLWNQLP NRAIQSAAAR ASNISGRTGL RVSTRFEDPA
     MLRLIGRRRL YKH