ID   ACH2_BOMMO              Reviewed;         375 AA.
AC   P80034;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Antichymotrypsin-2;
DE   AltName: Full=Antichymotrypsin II;
DE            Short=ACHY-II;
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   PROTEIN SEQUENCE.
RC   STRAIN=Kinshu X Showa; TISSUE=Larval hemolymph;
RX   PubMed=1761030; DOI=10.1111/j.1432-1033.1991.tb16370.x;
RA   Sasaki T.;
RT   "Patchwork-structure serpins from silkworm (Bombyx mori) larval
RT   hemolymph.";
RL   Eur. J. Biochem. 202:255-261(1991).
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   -!- MISCELLANEOUS: The N-terminal section (1-336) is identical to the N-
CC       terminal section of the silk moth antitrypsin I (17-352).
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   PIR; S19546; S19546.
DR   AlphaFoldDB; P80034; -.
DR   SMR; P80034; -.
DR   HOGENOM; CLU_023330_2_0_1; -.
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; IPR015557; Serpin_B1.
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   PANTHER; PTHR11461:SF180; PTHR11461:SF180; 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.
FT   CHAIN           1..375
FT                   /note="Antichymotrypsin-2"
FT                   /id="PRO_0000094096"
FT   SITE            340..341
FT                   /note="Reactive bond"
SQ   SEQUENCE   375 AA;  41458 MW;  FDB01D3EADB9E1EF CRC64;
     AVTNLSNVLK NGNDNFTARM FTEVVKNNPG KSIVLSAFSV LPPLAQLALA SDGETHEELL
     KAIGFPDDDA IRTEFASKSR DLRSIKGVEL KMANKVYVHD GGKLDENFAV VSRDVFNSDV
     QNIDFSKNTV AAKSINDWVE ENTNNRIKDL VNPDSLSSAT AAVLVNAIYF KGAWSSKFDE
     RLTSDRDFYV SKDKTIKVPM MYKRGDYKYG ESAVLNAQLI EIPYKGDQSS LIVVLPKDKD
     GITQLQEALK DPKTLETAQQ SMYSTEVDLY LPKFKIETET NLKDVLSNMN VNKIFNNDAQ
     ITRLLKGESL SVSEAIQKAF IEINEEGAEA AAANAFAVVF MSAVVSQPLV FKANHPFVFF
     LKGDGVTLFN GVFHP