ID   KCP5_PINMG              Reviewed;         182 AA.
AC   H2A0P0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=BPTI/Kunitz domain-containing protein 5;
DE   AltName: Full=Nacre serine protease inhibitor 5;
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, ECO:0000312|EMBL:CCE46181.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000312|EMBL:CCE46181.1};
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 46-53 AND 107-117, 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: Nacreous layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle
CC       pallium and lower level in the mantle edge.
CC       {ECO:0000269|PubMed:23213212}.
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DR   EMBL; HE610407; CCE46181.1; -; mRNA.
DR   AlphaFoldDB; H2A0P0; -.
DR   SMR; H2A0P0; -.
DR   PRIDE; H2A0P0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd00109; KU; 2.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..182
FT                   /note="BPTI/Kunitz domain-containing protein 5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417941"
FT   DOMAIN          29..81
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          83..141
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   182 AA;  20824 MW;  7EB101520DE7F764 CRC64;
     MIRLYIQCLI LWIIILPLLA AREGFGGRCL KPKDKGNRSC GRSQKYYYFN AEKGRCYRFT
     YYGCKGNSNR FKKKSDCVSS CACQAVLDHG SHCKSKAKRK EGSKVRYYFD SESGLCRKFW
     YVGCGGNHNK FTSKTSCKKV CVKDAPKRSK SSKPTSKTFS KNAQYSMNSL LRMLKNLSKK
     VM