ID   ACH1_BOMMO              Reviewed;         400 AA.
AC   Q03383;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Antichymotrypsin-1;
DE   AltName: Full=Antichymotrypsin I;
DE            Short=ACHY-I;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Kinshu X Showa; TISSUE=Larval fat body;
RX   PubMed=8508791; DOI=10.1111/j.1432-1033.1993.tb17911.x;
RA   Narumi H., Hishida T., Sasaki T., Feng D.-F., Doolittle R.F.;
RT   "Molecular cloning of silkworm (Bombyx mori) antichymotrypsin. A new member
RT   of the serpin superfamily of proteins from insects.";
RL   Eur. J. Biochem. 214:181-187(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-34.
RC   TISSUE=Hemolymph;
RX   PubMed=6430879; DOI=10.1093/oxfordjournals.jbchem.a134688;
RA   Sasaki T., Kobayashi K.;
RT   "Isolation of two novel proteinase inhibitors from hemolymph of silkworm
RT   larva, Bombyx mori. Comparison with human serum proteinase inhibitors.";
RL   J. Biochem. 95:1009-1017(1984).
CC   -!- FUNCTION: Inhibits chymotrypsin activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the serpin reactive site and the active site
CC       of the protease. The resulting inactive serpin-protease complex is
CC       highly stable (By similarity). {ECO:0000250}.
CC   -!- PTM: Does not seem to be glycosylated.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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   EMBL; D13895; BAA02995.1; -; mRNA.
DR   PIR; S33326; S33326.
DR   RefSeq; NP_001037530.1; NM_001044065.1.
DR   AlphaFoldDB; Q03383; -.
DR   SMR; Q03383; -.
DR   STRING; 7091.BGIBMGA001983-TA; -.
DR   MEROPS; I04.077; -.
DR   PRIDE; Q03383; -.
DR   GeneID; 693071; -.
DR   KEGG; bmor:693071; -.
DR   CTD; 693071; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_0_1_1; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:6430879"
FT   CHAIN           17..400
FT                   /note="Antichymotrypsin-1"
FT                   /id="PRO_0000032409"
FT   SITE            359..360
FT                   /note="Reactive bond"
FT   CONFLICT        22
FT                   /note="H -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="T -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  44572 MW;  3851D93AD6B56740 CRC64;
     MDKLLLLVTL VCGTQAFYMF GHEFSRTRLG DTIDKTSLKI LKESYNLADD KNVIASPLGV
     MLLLSLYESG AGAQSKEEIR EILGGGEAQE SSHTYGLLNQ RYAEFDPKFL TVAIKIYVSD
     QYKLADAFSR TANLFRSEVD NINFSAPKNA ADIINRWADE QTQGHIKTPV SEDKIDPATA
     VAMFNVIFFQ GHWHVPFNAS ETEEKDFHVD EKTIIKKPTM RLLQSLFYTE NEELGAKMIE
     LPYKEPGFRM VVVLPDKIDG LPAVLEKAAE KGLLEDVFNL SPAGRDIELE IPKFEIRSGL
     DLNTILPKVG VSKIFQEPAP AIVKNDQVVV SRAFQEAFVK VDEEGATAGA FTGLIAVPTS
     SLSRPPPSLL FKVDHPFLIL HEEDKILLLG HTHIKNCICF