ID   KCP_HALAI               Reviewed;         126 AA.
AC   P86733;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=BPTI/Kunitz domain-containing protein {ECO:0000303|PubMed:21050442};
DE   Flags: Fragment;
OS   Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=109174;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 25-35; 42-61; 75-90 AND 112-117, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Shell {ECO:0000269|PubMed:21050442};
RX   PubMed=21050442; DOI=10.1186/1477-5956-8-54;
RA   Marie B., Marie A., Jackson D.J., Dubost L., Degnan B.M., Milet C.,
RA   Marin F.;
RT   "Proteomic analysis of the organic matrix of the abalone Haliotis asinina
RT   calcified shell.";
RL   Proteome Sci. 8:54-54(2010).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250|UniProtKB:P84875}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21050442}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-soluble and acid-insoluble
CC       organic matrix of calcified shell layers (at protein level).
CC       {ECO:0000269|PubMed:21050442}.
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DR   EMBL; GT274423; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT276627; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ421228; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86733; -.
DR   SMR; P86733; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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.
FT   CHAIN           <1..126
FT                   /note="BPTI/Kunitz domain-containing protein"
FT                   /id="PRO_0000399444"
FT   DOMAIN          14..64
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          70..120
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        14..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        23..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        39..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        70..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        79..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        95..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   CONFLICT        122
FT                   /note="K -> R (in Ref. 1; GT274423)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   126 AA;  14526 MW;  DF7A1A3B1683EB01 CRC64;
     LFVGLTSAKY HDVCQLPRDP GPCRAYIPLY YFNSRTCLCE KFVYGGCQGN ANRFDTVEDC
     RRRCGGGDLC SLPRDSGPCE AAIPRWWYNK RTNRCQRFTY GGCEGNANNF KTLDECRFQC
     RKRSTY