ID   A1AT_BOMMO              Reviewed;         392 AA.
AC   P22922;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Antitrypsin;
DE            Short=AT;
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 PROTEIN SEQUENCE OF 17-47.
RC   TISSUE=Larval fat body;
RX   PubMed=2277028; DOI=10.1093/oxfordjournals.jbchem.a123208;
RA   Takagi H., Narumi H., Nakamura K., Sasaki T.;
RT   "Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin
RT   deduced from its cDNA nucleotide sequence: confirmation of its homology
RT   with serpins.";
RL   J. Biochem. 108:372-378(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 352-376.
RX   PubMed=1368515; DOI=10.1271/bbb1961.54.131;
RA   Sasaki T., Kohara A., Takagi H., Shimidzu T.;
RT   "Limited proteolysis of silkworm antitrypsin by several proteinases.";
RL   Agric. Biol. Chem. 54:131-137(1990).
CC   -!- FUNCTION: May play a role in the prophenoloxydase activating system in
CC       the silkworm hemolymph.
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   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; D00738; BAA00639.1; -; mRNA.
DR   PIR; JX0130; JX0130.
DR   RefSeq; NP_001037305.1; NM_001043840.1.
DR   AlphaFoldDB; P22922; -.
DR   SMR; P22922; -.
DR   STRING; 7091.BGIBMGA009953-TA; -.
DR   MEROPS; I04.031; -.
DR   PRIDE; P22922; -.
DR   GeneID; 692739; -.
DR   KEGG; bmor:692739; -.
DR   CTD; 692739; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_2_0_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; 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; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:2277028"
FT   CHAIN           17..392
FT                   /note="Antitrypsin"
FT                   /id="PRO_0000032408"
FT   SITE            359..360
FT                   /note="Reactive bond"
SQ   SEQUENCE   392 AA;  43499 MW;  2A40C345D94B1095 CRC64;
     MKTIICLFTI AIAAMAAVTN LSNVLKNGND NFTARMFTEV VKNNPGKSIV LSAFSVLPPL
     AQLALASDGE THEELLKAIG FPDDDAIRTE FASKSRDLRS IKGVELKMAN KVYVHDGGKL
     DENFAVVSRD VFNSDVQNID FSKNTVAAKS INDWVEENTN NRIKDLVNPD SLSSATAAVL
     VNAIYFKGAW SSKFDERLTS DRDFYVSKDK TIKVPMMYKR GDYKYGESAV LNAQLIEIPY
     KGDQSSLIVV LPKDKDGITQ LQEALKDPKT LETAQQSMYS TEVDLYLPKF KIETETNLKD
     VLSNMNVNKI FNNDAQITRL LKGESLSVSE AIQKAFIEIN EEGAEAAAAN AFTMTRSSKV
     YVRPPIVFNA NKPFYYALQV DGVIMFNGIF IN