ID   SPI2_CRAVI              Reviewed;          85 AA.
AC   B9A8D7;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Serine protease inhibitor Cvsi-2 {ECO:0000303|PubMed:19464375};
DE   Flags: Precursor;
GN   Name=CVSI2 {ECO:0000312|EMBL:BAH20735.1};
OS   Crassostrea virginica (Eastern oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=6565;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAH20735.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-79, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND DISULFIDE
RP   BONDS.
RC   TISSUE=Digestive gland {ECO:0000269|PubMed:19464375}, and
RC   Hemolymph {ECO:0000269|PubMed:19464375};
RX   PubMed=19464375; DOI=10.1016/j.fsi.2009.05.006;
RA   Xue Q., Itoh N., Schey K.L., Cooper R.K., La Peyre J.F.;
RT   "Evidence indicating the existence of a novel family of serine protease
RT   inhibitors that may be involved in marine invertebrate immunity.";
RL   Fish Shellfish Immunol. 27:250-259(2009).
CC   -!- FUNCTION: Slow-binding inhibitor of serine proteases. The inhibitor
CC       rapidly binds to the protease forming a weak enzyme-inhibitor complex,
CC       and this is followed by a slow isomerization forming a tight-binding
CC       enzyme-inhibitor complex. Active against subtilisin A with a
CC       dissociation constant of 0.18 nM. Active against perkinsin. Not active
CC       against thermolysin, papain or pepsin. {ECO:0000269|PubMed:19464375}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19464375}.
CC   -!- TISSUE SPECIFICITY: Detected in hemolymph (at protein level). Within
CC       the digestive gland expression is limited to the basophil cells of the
CC       digestive diverticula. {ECO:0000269|PubMed:19464375}.
CC   -!- PTM: Contains 6 disulfide bonds. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7208; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19464375};
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DR   EMBL; AB468967; BAH20735.1; -; mRNA.
DR   AlphaFoldDB; B9A8D7; -.
DR   MEROPS; I84.001; -.
DR   Proteomes; UP000694844; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:19464375"
FT   CHAIN           19..85
FT                   /note="Serine protease inhibitor Cvsi-2"
FT                   /evidence="ECO:0000269|PubMed:19464375"
FT                   /id="PRO_0000390781"
SQ   SEQUENCE   85 AA;  9086 MW;  B48DC6DBF2BEFCF5 CRC64;
     MKVAVVVALL CFVCYTAAET CSADGDCKNT ICDASHDLEC HRGQCTCVNH ATACSSAADC
     SGSCTIFGRH GRWHCVDAKC RCFFV