ID   PWAPL_MYTGA             Reviewed;         141 AA.
AC   P86855;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Perlwapin-like protein {ECO:0000303|PubMed:21643827};
DE   Flags: Precursor;
OS   Mytilus galloprovincialis (Mediterranean mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=29158;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19203376; DOI=10.1186/1471-2164-10-72;
RA   Venier P., De Pitta C., Bernante F., Varotto L., De Nardi B., Bovo G.,
RA   Roch P., Novoa B., Figueras A., Pallavicini A., Lanfranchi G.;
RT   "MytiBase: a knowledgebase of mussel (M. galloprovincialis) transcribed
RT   sequences.";
RL   BMC Genomics 10:72-72(2009).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 45-51 AND 68-76, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell {ECO:0000269|PubMed:21643827};
RX   PubMed=21643827; DOI=10.1007/s00239-011-9451-6;
RA   Marie B., Le Roy N., Zanella-Cleon I., Becchi M., Marin F.;
RT   "Molecular evolution of mollusc shell proteins: insights from proteomic
RT   analysis of the edible mussel mytilus.";
RL   J. Mol. Evol. 72:531-546(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21643827}.
CC   -!- TISSUE SPECIFICITY: Component of the organic matrix of calcified shell
CC       layers like nacre and prisms. {ECO:0000269|PubMed:21643827}.
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DR   EMBL; FL494664; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86855; -.
DR   PRIDE; P86855; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..141
FT                   /note="Perlwapin-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000404084"
FT   DOMAIN          23..71
FT                   /note="WAP"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..60
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8"
FT   DISULFID        39..64
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8"
FT   DISULFID        47..59
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8"
FT   DISULFID        53..68
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8"
FT   DISULFID        81..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..104
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8"
SQ   SEQUENCE   141 AA;  16116 MW;  93F16B8F576AA6D8 CRC64;
     MNVYFILFLG VFAFIEVNCK SRKSKSLGTC PKLDVSTVCV VDYKFNCLFQ KQCPSGYRCC
     TYGCNRRCAA VTVNKKHLGS CRNSSGKKGK RCKKDKSCKR HEKCCNKRCR RVRKKIAPVR
     TLSKNSSNSF SFLMKLISIN R