SPI_SCHGR
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 25-MAY-2022, entry version 33.
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 InterPro; IPR036058; Kazal_dom_sf.
DR SUPFAM; SSF100895; SSF100895; 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
