ID   VDP_BOMMO               Reviewed;         264 AA.
AC   Q07943;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Vitellin-degrading protease;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Beta-VTN protease;
DE   Contains:
DE     RecName: Full=Alpha-VTN protease chain 1;
DE   Contains:
DE     RecName: Full=Alpha-VTN protease chain 2;
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 [GENOMIC DNA / MRNA].
RC   STRAIN=N4; TISSUE=Egg;
RX   PubMed=1764920; DOI=10.1016/0305-0491(91)90062-i;
RA   Ikeda M., Yaginuma T., Kobayashi M., Yamashita O.;
RT   "cDNA cloning, sequencing and temporal expression of the protease
RT   responsible for vitellin degradation in the silkworm, Bombyx mori.";
RL   Comp. Biochem. Physiol. 99B:405-411(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Shunrei X Shogetu; TISSUE=Egg;
RA   Ikeda M., Sasaki T., Yamashita O.;
RT   "Purification and characterization of proteases responsible for vitellin
RT   degradation of the silkworm, Bombyx mori.";
RL   Insect Biochem. 20:725-734(1990).
CC   -!- FUNCTION: Responsible for the degradation of vitellin in eggs at the
CC       head pigmentation stage.
CC   -!- DEVELOPMENTAL STAGE: Appears on egg day 7.5, becomes more active on day
CC       8-8.5 and disappears on day 9.5.
CC   -!- PTM: Cleavage after Arg-27 leads to beta-VTN protease and subsequent
CC       cleavage after Arg-89 leads to alpha-VTN.
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   EMBL; D16232; BAA03757.1; -; mRNA.
DR   EMBL; D16233; BAA03758.1; -; Genomic_DNA.
DR   PIR; S32794; S32794.
DR   RefSeq; NP_001037317.1; NM_001043852.1.
DR   AlphaFoldDB; Q07943; -.
DR   SMR; Q07943; -.
DR   STRING; 7091.BGIBMGA013836-TA; -.
DR   MEROPS; S01.113; -.
DR   GeneID; 692746; -.
DR   KEGG; bmor:692746; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..27
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028442"
FT   CHAIN           28..264
FT                   /note="Beta-VTN protease"
FT                   /id="PRO_0000028443"
FT   CHAIN           28..89
FT                   /note="Alpha-VTN protease chain 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028444"
FT   CHAIN           90..264
FT                   /note="Alpha-VTN protease chain 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028445"
FT   DOMAIN          28..253
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        178..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        41
FT                   /note="Y -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="T -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="Y -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   264 AA;  28521 MW;  6D536DD4184123AF CRC64;
     MTNSLLICFT ILGLAASSPT KPIGDIRIVG GEDIVITEAP YQVSVMFRGA HSCGGTLVAA
     DIVVTAAHCV MSFAPEDYRI RVGSSFHQRD GMLYDVGDLA WHPDFNFASM DNDIAILWLP
     KPVMFGDTVE AIEMVETNSE IPDGDITIVT GWGHMEEGGG NPSVLQRVIV PKINEAACAE
     AYSPIYAITP RMLCAGTPEG GKDACQGDSG GPLVHKKKLA GIVSWGLGCA RPEYPGVYTK
     VSALREWVDE NITNLRLKHI LRRF