ID   GEPRP_LOTGI             Reviewed;         419 AA.
AC   B3A0P5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Glycine, glutamate and proline-rich protein;
DE   Flags: Precursor;
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 26-48; 104-120; 245-257; 262-297 AND 304-409,
RP   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 organic matrix of
CC       calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 23 family. {ECO:0000255}.
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DR   EMBL; FC622269; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC626005; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3A0P5; -.
DR   SMR; B3A0P5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..419
FT                   /note="Glycine, glutamate and proline-rich protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415246"
FT   REGION          74..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  45187 MW;  E4A3E1772CAF2F4D CRC64;
     MKCLVALFLS LSLVACQYDD YDTERKNNNM LSSMNILDLL DSFGLNIKAR IAHVRRVAGR
     IRLTLDIGLG NGDVERESEE AEGEGTDGRG GGEGEREGWG GEREGGEGER EGGEGEREGR
     EGEREGKSSE SNESPEDFIG PPVDMCAGES RRGSPSIGCI AAECCQHSFY INSLCPGSSV
     CCFSMDVCDR LPVPVIPPFP TDPGTLPPPP PIPDSQTTVS PNQPSSYMCH GDFMKLMPKG
     ADQRTARQDN LAYAGVRASN KLVDNDLAEL NKRKDCYVQA GKNHCIHPAV IAAIASRETR
     GGKLLYSTNG YGDGGRAYGI MQCDGGASGL GDICKKYPWD SCEHINQLTD IILLNYVNQM
     KTKHPSWPAH YQLKGGVSAY NAGVGNVQTI AGMDAGTTND DYSNDVIARA QRLVNAHGW