ID   HYPB_HYPLI              Reviewed;         256 AA.
AC   P35588;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hypodermin-B;
DE            Short=HB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Hypoderma lineatum (Early cattle grub) (Common cattle grub).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Oestridae; Hypodermatinae; Hypoderma.
OX   NCBI_TaxID=7389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kuhn I., Files J.G., Pruett J.H., Temeyer K.B.;
RT   "Cloning, expression and immunogenicity of hypodermins A and B of Hypoderma
RT   lineatum.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 31-46.
RX   PubMed=6307690; DOI=10.1111/j.1432-1033.1983.tb07560.x;
RA   Lecroisey A., Tong N.T., Keil B.;
RT   "Hypodermin B, a trypsin-related enzyme from the insect Hypoderma lineatum.
RT   Comparison with hypodermin A and Hypoderma collagenase, two serine
RT   proteinases from the same source.";
RL   Eur. J. Biochem. 134:261-267(1983).
CC   -!- FUNCTION: Protease that shows preferential cleavage after Arg and Lys
CC       residues.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Larval-specific.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; L24915; AAA29225.1; -; mRNA.
DR   PIR; A20190; A20190.
DR   AlphaFoldDB; P35588; -.
DR   SMR; P35588; -.
DR   MEROPS; S01.090; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..30
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:6307690"
FT                   /id="PRO_0000027919"
FT   CHAIN           31..256
FT                   /note="Hypodermin-B"
FT                   /id="PRO_0000027920"
FT   DOMAIN          31..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        71
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            204
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        206..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        45
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  27711 MW;  3258EE71D3BF3A07 CRC64;
     MLKFVILVCS VACVFGAVVP GGMLPQLDGR IVGGFEADIE DFPWQVSIQR GGYHFCGGSI
     YSPEIIVTAA HCLEKIDASQ LRVRVGGSYW DEEGSLLTVS NFKIHEKYDA MIMWYDVALL
     KLSSKLTYGA TVKNIELAKE TPPDNADAVV SGWGTIYENY PYMPVQLRSV DVKIVSREVC
     RSDEYGYGNA IGPTMICAYA VGKDACQGDS GGPLVVGEAL VGVVSWGEGC AYPGFPGVYT
     DVSVVRSWIT ENAKSF