KCP2_PINMG
ID KCP2_PINMG Reviewed; 141 AA.
AC H2A0N1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=BPTI/Kunitz domain-containing protein 2;
DE AltName: Full=Prism serine protease inhibitor 2;
DE Short=PISP2;
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}
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC TISSUE=Mantle;
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 79-93, 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: Prismatic layer of shell (at protein level).
CC {ECO:0000269|PubMed:23213212}.
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DR EMBL; HE610398; CCE46172.1; -; mRNA.
DR AlphaFoldDB; H2A0N1; -.
DR SMR; H2A0N1; -.
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 PRINTS; PR00759; BASICPTASE.
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; Disulfide bond; Protease inhibitor; Repeat;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..141
FT /note="BPTI/Kunitz domain-containing protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417938"
FT DOMAIN 30..79
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 84..136
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 30..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 40..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 54..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 84..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 94..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 111..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 141 AA; 15454 MW; FFC9D44FC91A4531 CRC64;
MLASCHITSL SGILLLLCVQ CSAQILINPC GDVPGVRGPC SANLRRFTFA YGRCVPFYYG
GCLGTRNRFD SFVECERRCL GGPCNQTPGV VGRCYAAIPR YTYVPFPINS CVSFTYGGCE
GNDNNFEDVN VCFNLCVFRR G
