SGP1_SCHGR
ID SGP1_SCHGR Reviewed; 92 AA.
AC O46162;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine protease inhibitor I/II;
DE Contains:
DE RecName: Full=Protease inhibitor SGPI-1;
DE AltName: Full=Schistocerca gregaria trypsin inhibitor;
DE Short=SGTI;
DE Contains:
DE RecName: Full=Protease inhibitor SGPI-2;
DE AltName: Full=Schistocerca gregaria chymotrypsin inhibitor;
DE Short=SGCI;
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 20-54 AND 57-91, 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).
RN [3] {ECO:0000312|PDB:1KGM, ECO:0000312|PDB:1KIO, ECO:0000312|PDB:1KJ0}
RP STRUCTURE BY NMR OF 20-54 AND 57-91, AND DISULFIDE BONDS.
RX PubMed=11997226; DOI=10.1016/s1096-4959(01)00530-9;
RA Simonet G., Claeys I., Vanden Broeck J.;
RT "Structural and functional properties of a novel serine protease inhibiting
RT peptide family in arthropods.";
RL Comp. Biochem. Physiol. 132B:247-255(2002).
CC -!- FUNCTION: [Protease inhibitor SGPI-1]: In vitro, is active against
CC alpha-chymotrypsin and trypsin. {ECO:0000269|PubMed:9475173}.
CC -!- FUNCTION: [Protease inhibitor SGPI-2]: In vitro, is active against
CC alpha-chymotrypsin and pancreatic elastase.
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; Y09605; CAA70818.1; -; mRNA.
DR PDB; 1KGM; NMR; -; A=57-91.
DR PDB; 1KIO; NMR; -; A=57-91.
DR PDB; 1KJ0; NMR; -; A=20-54.
DR PDB; 2F91; X-ray; 1.20 A; B=20-54.
DR PDB; 2XTT; X-ray; 0.93 A; A=20-54.
DR PDB; 3TVJ; X-ray; 1.28 A; I=57-91.
DR PDB; 4DJZ; X-ray; 3.20 A; H/I=57-87.
DR PDBsum; 1KGM; -.
DR PDBsum; 1KIO; -.
DR PDBsum; 1KJ0; -.
DR PDBsum; 2F91; -.
DR PDBsum; 2XTT; -.
DR PDBsum; 3TVJ; -.
DR PDBsum; 4DJZ; -.
DR AlphaFoldDB; O46162; -.
DR SMR; O46162; -.
DR MEROPS; I19.001; -.
DR MEROPS; I19.011; -.
DR EvolutionaryTrace; O46162; -.
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 InterPro; IPR016307; Prtase-inh_pacifastin.
DR Pfam; PF05375; Pacifastin_I; 2.
DR PIRSF; PIRSF001625; Prot_inhib_pacifastin; 1.
DR SUPFAM; SSF57283; SSF57283; 2.
DR PROSITE; PS51446; PACIFASTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:9475173"
FT PEPTIDE 20..54
FT /note="Protease inhibitor SGPI-1"
FT /evidence="ECO:0000269|PubMed:9475173"
FT /id="PRO_0000026710"
FT PEPTIDE 57..91
FT /note="Protease inhibitor SGPI-2"
FT /evidence="ECO:0000269|PubMed:9475173"
FT /id="PRO_0000026711"
FT DOMAIN 20..54
FT /note="Pacifastin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT DOMAIN 57..92
FT /note="Pacifastin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT SITE 48..49
FT /note="Reactive bond"
FT SITE 86..87
FT /note="Reactive bond"
FT DISULFID 23..38
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KJ0"
FT DISULFID 33..51
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KJ0"
FT DISULFID 36..46
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KJ0"
FT DISULFID 60..75
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KGM, ECO:0007744|PDB:1KIO"
FT DISULFID 70..89
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KGM, ECO:0007744|PDB:1KIO"
FT DISULFID 73..84
FT /evidence="ECO:0000269|PubMed:11997226,
FT ECO:0007744|PDB:1KGM, ECO:0007744|PDB:1KIO"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2XTT"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2XTT"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2XTT"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1KGM"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4DJZ"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3TVJ"
SQ SEQUENCE 92 AA; 9842 MW; 9E5A228C767C657C CRC64;
MKLALALCAA FLLVVLVQAE QECTPGQTKK QDCNTCNCTP TGVWACTRKG CPPHKREVTC
EPGTTFKDKC NTCRCGSDGK SAACTLKACP QK
