ACH1_LONAC
ID ACH1_LONAC Reviewed; 213 AA.
AC P23604;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Achelase-1;
DE EC=3.4.21.-;
DE AltName: Full=Achelase I;
OS Lonomia achelous (Giant silkworm moth) (Saturnid moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Hemileucinae; Lonomia.
OX NCBI_TaxID=7125;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph;
RX PubMed=1911844; DOI=10.1016/0167-4838(91)90128-m;
RA Amarant T., Burkhart W., Levine H. III, Arocha-Pinango C.L., Parikh I.;
RT "Isolation and complete amino acid sequence of two fibrinolytic proteinases
RT from the toxic Saturnid caterpillar Lonomia achelous.";
RL Biochim. Biophys. Acta 1079:214-221(1991).
CC -!- FUNCTION: Fibrinolytic activity; shows preferential cleavage of Arg-Gly
CC bonds in all three fibrinogen chains. Contact with the caterpillars
CC causes severe bleeding, due the anticoagulant effect of the protein.
CC {ECO:0000269|PubMed:1911844}.
CC -!- ACTIVITY REGULATION: Sensitive to serine proteinase inhibitors and
CC thiol proteinase inhibitors. {ECO:0000269|PubMed:1911844}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:1911844}.
CC -!- TISSUE SPECIFICITY: Hemolymph and saliva of the larval form
CC (caterpillar). {ECO:0000269|PubMed:1911844}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR PIR; S17537; S17537.
DR AlphaFoldDB; P23604; -.
DR SMR; P23604; -.
DR MEROPS; S01.420; -.
DR PRIDE; P23604; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
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 Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW Hemostasis; Hydrolase; Protease; Secreted; Serine protease.
FT CHAIN 1..213
FT /note="Achelase-1"
FT /id="PRO_0000088743"
FT DOMAIN 1..213
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 26..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 213 AA; 22472 MW; 21DD6769C9466542 CRC64;
IVGGSVTTIG QYPSMASLLF NNRQVCGGVI INNRSVLTAA HCPFGDAVSS WRFRVGSTNA
NSGGTVFTLS TIINHPSYNR WTLDNDISIM RAASNIGTSA SVQPAGIAGS NYNLGDNQVV
WATGWGATSA GGSLARFPGV NARHVQIWTV NQNTCASRYA AIGRTVTANM LCSGWLDVGG
RDQCQGDSGG PLYHNRIVVA VVSRYTSWIQ SNA
