ID   SPI_SCHGR               Reviewed;          83 AA.
AC   P85064;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 3.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Greglin;
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   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   PHOSPHORYLATION AT SER-8; SER-11 AND SER-15.
RC   TISSUE=Ovary {ECO:0000269|PubMed:16839309};
RX   PubMed=16839309; DOI=10.1042/bj20060437;
RA   Brillard-Bourdet M., Hamdaoui A., Hajjar E., Boudier C., Reuter N.,
RA   Ehret-Sabatier L., Bieth J.G., Gauthier F.;
RT   "A novel locust (Schistocerca gregaria) serine protease inhibitor with a
RT   high affinity for neutrophil elastase.";
RL   Biochem. J. 400:467-476(2006).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP   SPECTROMETRY, DISULFIDE BONDS, PHOSPHORYLATION AT SER-8, AND X-RAY
RP   CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 21-78 IN COMPLEX WITH SUBTILISIN.
RC   TISSUE=Ovary {ECO:0000303|PubMed:23075397};
RX   PubMed=23075397; DOI=10.1111/febs.12033;
RA   Derache C., Epinette C., Roussel A., Gabant G., Cadene M., Korkmaz B.,
RA   Gauthier F., Kellenberger C.;
RT   "Crystal structure of greglin, a novel non-classical Kazal inhibitor, in
RT   complex with subtilisin.";
RL   FEBS J. 279:4466-4478(2012).
CC   -!- FUNCTION: Serine protease inhibitor (PubMed:16839309, PubMed:23075397).
CC       Inhibits porcine pancreatic elastase with a Ki of 58.3 nM, human
CC       neutrophil elastase with a Ki of 3.6 nM, cathepsin G with a Ki of 153.5
CC       nM, chymotrypsin with a Ki of 26.7 nM and subtilisin with a Ki of 0.68
CC       nM. Does not inhibit neutrophil protease 3 or pancreatic trypsin
CC       (PubMed:16839309). {ECO:0000269|PubMed:16839309,
CC       ECO:0000269|PubMed:23075397}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         No decrease in activity observed after incubating at pH 2.5, pH 7.4
CC         and at pH 11.0 for 1 hour to overnight (PubMed:16839309,
CC         PubMed:23075397). {ECO:0000269|PubMed:16839309,
CC         ECO:0000269|PubMed:23075397};
CC       Temperature dependence:
CC         Thermostable (PubMed:16839309, PubMed:23075397). No decrease in
CC         activity was observed after heating for 1 hour at up to 95 degrees
CC         Celsius (PubMed:16839309, PubMed:23075397).
CC         {ECO:0000269|PubMed:16839309, ECO:0000269|PubMed:23075397};
CC   -!- MASS SPECTROMETRY: Mass=9661.13; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23075397};
CC   -!- MASS SPECTROMETRY: Mass=9733.08; Method=Electrospray; Note=Mono-
CC       phosphorylated form.; Evidence={ECO:0000269|PubMed:23075397};
CC   -!- MASS SPECTROMETRY: Mass=9813.06; Method=Electrospray; Note=Di-
CC       phosphorylated form.; Evidence={ECO:0000269|PubMed:23075397};
CC   -!- MASS SPECTROMETRY: Mass=9893.04; Method=Electrospray; Note=Tri-
CC       phosphorylated form.; Evidence={ECO:0000269|PubMed:23075397};
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DR   PDB; 4GI3; X-ray; 1.75 A; C=1-83.
DR   PDBsum; 4GI3; -.
DR   AlphaFoldDB; P85064; -.
DR   SMR; P85064; -.
DR   IntAct; P85064; 1.
DR   MINT; P85064; -.
DR   MEROPS; I01.059; -.
DR   iPTMnet; P85064; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.30; -; 1.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..83
FT                   /note="Greglin"
FT                   /id="PRO_0000271408"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16839309,
FT                   ECO:0000269|PubMed:23075397"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16839309"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16839309"
FT   DISULFID        21..55
FT                   /evidence="ECO:0000269|PubMed:23075397"
FT   DISULFID        25..48
FT                   /evidence="ECO:0000269|PubMed:23075397"
FT   DISULFID        33..69
FT                   /evidence="ECO:0000269|PubMed:23075397"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000269|PubMed:23075397"
FT   CONFLICT        7
FT                   /note="A -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17..25
FT                   /note="TELPCPSIC -> LELPLPSIS (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="Q -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:4GI3"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:4GI3"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:4GI3"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:4GI3"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:4GI3"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:4GI3"
SQ   SEQUENCE   83 AA;  9195 MW;  CFEAA69ABDCC39EF CRC64;
     SEDDGSASPE SQEMSYTELP CPSICPLIYA PVCVEDSNQD FYLFVNECEV RKCGCEAGFV
     YTFVPREMCK ATTSLCPMQT KSS
//