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Database: UniProt/SWISS-PROT
Entry: VDP_BOMMO
LinkDB: VDP_BOMMO
Original site: VDP_BOMMO 
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   10-OCT-2018, entry version 87.
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;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Bombycoidea; Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=N4; TISSUE=Egg;
RX   PubMed=1764920;
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
RT   vitellin degradation of the silkworm, Bombyx mori.";
RL   Insect Biochem. 20:725-734(1990).
CC   -!- FUNCTION: Responsible for the degradation of vitellin in eggs at
CC       the head pigmentation stage.
CC   -!- DEVELOPMENTAL STAGE: Appears on egg day 7.5, becomes more active
CC       on day 8-8.5 and disappears on day 9.5.
CC   -!- PTM: Cleavage after Arg-27 leads to beta-VTN protease and
CC       subsequent cleavage after Arg-89 leads to alpha-VTN.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Bmo.117; -.
DR   ProteinModelPortal; Q07943; -.
DR   SMR; Q07943; -.
DR   STRING; 7091.BGIBMGA013836-TA; -.
DR   MEROPS; S01.113; -.
DR   PRIDE; Q07943; -.
DR   GeneID; 692746; -.
DR   KEGG; bmor:692746; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG1819; LUCA.
DR   eggNOG; COG5640; LUCA.
DR   KO; K01312; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     15       {ECO:0000255}.
FT   PROPEP       16     27       Activation peptide. {ECO:0000255}.
FT                                /FTId=PRO_0000028442.
FT   CHAIN        28    264       Beta-VTN protease.
FT                                /FTId=PRO_0000028443.
FT   CHAIN        28     89       Alpha-VTN protease chain 1.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000028444.
FT   CHAIN        90    264       Alpha-VTN protease chain 2.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000028445.
FT   DOMAIN       28    253       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     68     68       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    113    113       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    209    209       Charge relay system. {ECO:0000250}.
FT   BINDING     203    203       Substrate. {ECO:0000250}.
FT   CARBOHYD    251    251       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     53     69       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    178    194       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    205    229       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   CONFLICT     41     41       Y -> T (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     56     56       T -> S (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     94     94       Y -> T (in Ref. 2; AA sequence).
FT                                {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
//
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