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 27-MAR-2024, entry version 32.
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 GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083:SF377; BPTI_KUNITZ INHIBITOR DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; BPTI-like; 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
//
