ID   KCP3_PINMA              Reviewed;         157 AA.
AC   P86964;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=BPTI/Kunitz domain-containing protein 3;
DE   AltName: Full=Nacre serine protease inhibitor 2;
DE            Short=NSPI2;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 117-124, SUBCELLULAR LOCATION, AND TISSUE 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       {ECO:0000269|PubMed:23213212}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GT283012; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; GT278172; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT278177; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT278263; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT278547; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT280826; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281554; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281731; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283012; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283694; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT284261; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420214; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86964; -.
DR   SMR; P86964; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..157
FT                   /note="BPTI/Kunitz domain-containing protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413077"
FT   DOMAIN          42..95
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          97..151
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        42..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        70..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        97..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        107..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        126..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   157 AA;  17683 MW;  05534FD1AF683A4B CRC64;
     MIRLVTLAAL PVLVLCQFDP SKWFMGSNLG GLQGFGVLPA RCLNYLEAGY SRGNRLPSHR
     FFFNSTSGNC EQFVYYGRGG NRNNFRDVFK CMKSCGCKQQ RNGGVPCNPP SQPVVRYYYD
     TFTKLCNTFQ HTGCGGNSNH FKDWNDCFFT CGNGFET