ID   PLCL_MYTGA              Reviewed;         156 AA.
AC   P86854;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Perlucin-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=17010391; DOI=10.1016/j.mrfmmm.2006.08.007;
RA   Venier P., De Pitta C., Pallavicini A., Marsano F., Varotto L.,
RA   Romualdi C., Dondero F., Viarengo A., Lanfranchi G.;
RT   "Development of mussel mRNA profiling: Can gene expression trends reveal
RT   coastal water pollution?";
RL   Mutat. Res. 602:121-134(2006).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 57-67 AND 89-99, 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; AJ624413; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86854; -.
DR   SMR; P86854; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033989; CD209-like_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lectin; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..156
FT                   /note="Perlucin-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000404080"
FT   DOMAIN          37..156
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        30..41
FT                   /evidence="ECO:0000250|UniProtKB:Q07108,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        58..156
FT                   /evidence="ECO:0000250|UniProtKB:Q07108,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        131..147
FT                   /evidence="ECO:0000250|UniProtKB:Q07108,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   156 AA;  17781 MW;  3F46A4BD10862CF6 CRC64;
     MGKLTVVGIL TLFIFYIVAA SGKCTAPVNC PAGWKKYKTN CYFFSPDGKN WHDAAKQCQT
     MGGYLVKITD SEENSWVVDM ITKSVKHKYG YWMGMADLKN EGDWRWVNDS SAVSYSNWHR
     GQPNNANNED CGHFWSAVNY EWNDIVCNTD QMGYIC