ID   KCP1_PINMA              Reviewed;         138 AA.
AC   P86959;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=BPTI/Kunitz domain-containing protein 1;
DE   AltName: Full=Prism serine protease inhibitor 1;
DE            Short=PSPI1;
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 67-76 AND 88-95, 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: Prismatic layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle edge
CC       and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GT282225; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT282425; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420477; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86959; -.
DR   SMR; P86959; -.
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; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR004094; Antistasin-like.
DR   InterPro; IPR011061; Hirudin/antistatin.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF02822; Antistasin; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57262; SSF57262; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..138
FT                   /note="BPTI/Kunitz domain-containing protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413075"
FT   DOMAIN          72..122
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        72..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        81..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        97..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   138 AA;  16200 MW;  CD8B844C5EAD942D CRC64;
     MYTLYILSLL CAFVTFSECK YPPGPIYPHR PIYPIQPVYP DHCPGVCYIA CPNGNIHDRN
     GCPICRCRPD ECTLPRKIGP CRASIPRYYF NFVTKRCELF FWGGCQPNKN NFETIYDCQG
     YCGYAERRYP YPYVKRTY