CTR1_SOLIN
ID CTR1_SOLIN Reviewed; 222 AA.
AC Q7SIG2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Chymotrypsin-1;
DE EC=3.4.21.1;
DE AltName: Full=Chymotrypsin I;
DE AltName: Full=Soli C1;
OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Solenopsis.
OX NCBI_TaxID=13686;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-22, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Larva {ECO:0000269|PubMed:9603955};
RX PubMed=9603955; DOI=10.1074/jbc.273.23.14430;
RA Whitworth S.T., Blum M.S., Travis J.;
RT "Proteolytic enzymes from larvae of the fire ant, Solenopsis invicta.
RT Isolation and characterization of four serine endopeptidases.";
RL J. Biol. Chem. 273:14430-14434(1998).
RN [2] {ECO:0000305, ECO:0000312|PDB:1EQ9}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP DISULFIDE BONDS.
RC TISSUE=Larva {ECO:0000269|PubMed:10801356};
RX PubMed=10801356; DOI=10.1006/jmbi.2000.3699;
RA Botos I., Meyer E., Nguyen M., Swanson S.M., Koomen J.M., Russell D.H.,
RA Meyer E.F.;
RT "The structure of an insect chymotrypsin.";
RL J. Mol. Biol. 298:895-901(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC ECO:0000255|PROSITE-ProRule:PRU10079, ECO:0000269|PubMed:9603955};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DEVELOPMENTAL STAGE: Expressed in fourth instar larvae.
CC {ECO:0000269|PubMed:9603955}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1EQ9; X-ray; 1.70 A; A/B=1-222.
DR PDBsum; 1EQ9; -.
DR AlphaFoldDB; Q7SIG2; -.
DR SMR; Q7SIG2; -.
DR BRENDA; 3.4.21.1; 6959.
DR EvolutionaryTrace; Q7SIG2; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Secreted; Serine protease.
FT CHAIN 1..222
FT /note="Chymotrypsin-1"
FT /id="PRO_0000248259"
FT DOMAIN 1..221
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10801356"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10801356"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10801356"
FT DISULFID 26..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:10801356"
FT DISULFID 151..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:10801356"
FT DISULFID 174..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:10801356"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1EQ9"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1EQ9"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1EQ9"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1EQ9"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1EQ9"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1EQ9"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1EQ9"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1EQ9"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1EQ9"
SQ SEQUENCE 222 AA; 24012 MW; 862770BF2A44E652 CRC64;
IVGGKDAPVG KYPYQVSLRL SGSHRCGASI LDNNNVLTAA HCVDGLSNLN RLKVHVGTNY
LSESGDVYDV EDAVVNKNYD DFLLRNDVAL VHLTNPIKFN DLVQPIKLST NDEDLESNPC
TLTGWGSTRL GGNTPNALQE IELIVHPQKQ CERDQWRVID SHICTLTKRG EGACHGDSGG
PLVANGAQIG IVSFGSPCAL GEPDVYTRVS SFVSWINANL KK
