ID   PLSP2_LOTGI             Reviewed;         884 AA.
AC   B3A0P3;
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 2;
DE   Flags: Fragments;
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 37-50; 62-81; 285-308; 346-394; 400-410; 452-465 AND
RP   474-482, SUBCELLULAR LOCATION, AND TISSUE 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; FC623427; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC627615; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC628592; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC631694; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3A0P3; -.
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; -; 2.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted.
FT   CHAIN           1..884
FT                   /note="Peroxidase-like protein 2"
FT                   /id="PRO_0000415263"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        280..281
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   884 AA;  92943 MW;  B896EA9E960CBD82 CRC64;
     TTSCTDAKGK QYRTADGTCN NVNKPTVGSS MDKFKRDVKP QYDDKKGDPR TKGRCLYKTE
     KGCYRPDLPS ARAISVVVHS KQTSVDDDSS KSSAVSPKMP SMGNLQSLGN LLSLGSVPVP
     APAPAPEPVS APSVDIAPAQ PVAGPSITDL LGLMSIIQKP KSKPKPKPKP KPQPKPQPES
     KPILSQGAIG DILGLLGTLV ASPEKETPVS SQPDDSISGL MGKVDEPRIR TPKKSPRKKA
     RQSIFRRRDD RKDDRKGLRG TKGRRDDSDD NDDSDDDDDD IEVRISNVFA TAAIKFVAAL
     SPDYIDIRGR KIRLRDTYNN PEMVFDELPE LIEEMLQQPT EERNRFISKE LTDHFLEDGS
     RSFDEVASII QRGRDHGVPP YNWFRQFCGL PIVRSFNSRV FGDAGPYLRK VYKSVDDIDI
     YTGAMSEPNL PGSLLGETFS CIFARQFRDL KFGDSFFYLS DDPLRGFSKE QRRELDTITL
     SKAMCFVFGL EAVQMNPLRV PSAQNPLSDC EQIPSFFSFL EDPSEGPRSN LLSRVSQSES
     VASLSGIMPR FFDAESAGPS MKDNGYEGVG NVLPPAFTTN GVSKTVVGAS PRGSERFRDV
     EVEDPEGGFG MPLPGVPIPS MSSNTDAVSQ GDPLNELTQM GGTVDGEVEV EEPEIPGPQE
     GKASGSLPRA FTDGRQMPLG SSPGSLGGVQ GSATQPDALD PTILPGVPLD LQPKAQDPTK
     LPGVPEYLQP KPKSSGLSTQ GAVGGEMGKG EIELEDQLGS HGVAGGAVEV GEAEGAAGGI
     DGSVGSGGMG GSVGVGGSGG MGGSVGVGGM GGSVGVGGSG GMGGSVGVGG MGGSVGVGGS
     VGSGGSGGSR GAGGSGDDGD DCCQDDSKCS DDEKQKYCKN SDTK