ID   SGP3_SCHGR              Reviewed;          63 AA.
AC   O46163;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Serine protease inhibitor 3;
DE   AltName: Full=Protease inhibitor SGPI-3;
DE   AltName: Full=Serine protease inhibitor III;
DE   Flags: Precursor;
OS   Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9652399; DOI=10.1046/j.1432-1327.1998.2540090.x;
RA   Vanden Broeck J., Chiou S.-J., Schoofs L., Hamdaoui A., Vandenbussche F.,
RA   Simonet G., Wataleb S., De Loof A.;
RT   "Cloning of two cDNAs encoding three small serine protease inhibiting
RT   peptides from the desert locust Schistocerca gregaria and analysis of
RT   tissue-dependent and stage-dependent expression.";
RL   Eur. J. Biochem. 254:90-95(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-63, FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary;
RX   PubMed=9475173; DOI=10.1016/s0014-5793(97)01585-8;
RA   Hamdaoui A., Wataleb S., Devreese B., Chiou S.-J., Vanden Broeck J.,
RA   Van Beeumen J., De Loof A., Schoofs L.;
RT   "Purification and characterization of a group of five novel peptide serine
RT   protease inhibitors from ovaries of the desert locust, Schistocerca
RT   gregaria.";
RL   FEBS Lett. 422:74-78(1998).
CC   -!- FUNCTION: In vitro, active against alpha-chymotrypsin.
CC       {ECO:0000269|PubMed:9475173}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in hemolymph, ovaries, testes and fat
CC       body of adults but are absent in the gut. Also present in larval
CC       hemolymph and fat body. {ECO:0000269|PubMed:9475173}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00776}.
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DR   EMBL; Y09606; CAA70819.1; -; mRNA.
DR   AlphaFoldDB; O46163; -.
DR   MEROPS; I19.012; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008037; Pacifastin_dom.
DR   InterPro; IPR036201; Pacifastin_dom_sf.
DR   Pfam; PF05375; Pacifastin_I; 1.
DR   SUPFAM; SSF57283; SSF57283; 1.
DR   PROSITE; PS51446; PACIFASTIN; 1.
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   PEPTIDE         24..63
FT                   /note="Serine protease inhibitor 3"
FT                   /id="PRO_0000026712"
FT   DOMAIN          24..55
FT                   /note="Pacifastin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   SITE            49..50
FT                   /note="Reactive bond"
FT   DISULFID        24..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        34..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        37..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
SQ   SEQUENCE   63 AA;  6533 MW;  EE46BACCD7441A6B CRC64;
     MAKLLAVFLV LLIAALVCEQ ALACTPGSRK YDGCNWCTCS SGGAWICTLK YCPPSSGGGL
     TFA