KCP2_PINMA
ID KCP2_PINMA Reviewed; 337 AA.
AC P86963;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=BPTI/Kunitz domain-containing protein 2;
DE AltName: Full=Nacre serine protease inhibitor 1;
DE Short=NSPI1;
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 41-50; 55-70 AND 89-95, SUBCELLULAR LOCATION, AND
RP 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 ---------------------------------------------------------------------------
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; GT278092; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT278284; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT278658; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT279792; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT280299; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT280446; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT280511; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT280778; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT280987; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT281039; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT281466; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT281498; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT281815; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT281974; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT282009; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT282247; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT283219; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT283302; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT283718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT284266; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT284471; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EZ420139; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EZ420140; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P86963; -.
DR SMR; P86963; -.
DR PRIDE; P86963; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..337
FT /note="BPTI/Kunitz domain-containing protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000413076"
FT DOMAIN 98..151
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 182..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 98..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 112..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 126..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT CONFLICT 219
FT /note="V -> G (in Ref. 1; EZ420140/GT282247)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> K (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> R (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="G -> C (in Ref. 1; GT282247)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="G -> R (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..244
FT /note="AGR -> PRK (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="Q -> H (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="G -> R (in Ref. 1; EZ420140)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> T (in Ref. 1; GT282247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 35956 MW; 36D0D2641C87FCD2 CRC64;
MLVFGFAFLS LLLIETEAQQ QNGMMGGGAA GPGINKMERG CYDTPPIQRR ARRQCGGGML
VPRFFYSNRL NRCIMRRACF FMRTGMRSMI ECNKECRCMQ PPSEGTGGGA LCEREVMRWM
FVGEMCVQRM FSGCGGNGNN FKTQGECMKF CKPREPEFMM GEMPSEMAAA MAFNNRGRNN
FGGSPGGWGG SPGGWEGSPG GWGGSPGGWG GGGNQGRRVN RGGGGGGGAR GGGGGGGGNG
GAGRMNGNNQ QGGNNQMGPT AATPPSPRPT MTTGPVTRPI PSVRRPKPKP KRWNNNNNNR
NNNLMIQGTT SGGWGGTTTP SYYNPYQSYI AHEYLFK
