ID   HYPA_HYPLI              Reviewed;         256 AA.
AC   P35587; Q25080;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hypodermin-A;
DE            Short=HA;
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].
RX   PubMed=7808473; DOI=10.1016/0166-6851(94)90150-3;
RA   Moire N., Bigot Y., Periquet G., Boulard C.;
RT   "Sequencing and gene expression of hypodermins A, B, C in larval stages of
RT   Hypoderma lineatum.";
RL   Mol. Biochem. Parasitol. 66:233-240(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-256.
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   [3]
RP   PROTEIN SEQUENCE OF 31-51.
RX   PubMed=7018579; DOI=10.1016/0005-2744(81)90291-6;
RA   Tong N.T., Imhoff J.M., Lecroisey A., Keil B.;
RT   "Hypodermin A, a trypsin-like neutral proteinase from the insect Hypoderma
RT   lineatum.";
RL   Biochim. Biophys. Acta 658:209-219(1981).
CC   -!- FUNCTION: Specificity, limited to carboxyl side of arginine residue in
CC       B-chain of insulin.
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; X74303; CAA52356.1; -; mRNA.
DR   EMBL; L24914; AAA29224.1; -; mRNA.
DR   PIR; A21590; A21590.
DR   AlphaFoldDB; P35587; -.
DR   SMR; P35587; -.
DR   MEROPS; S01.111; -.
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:7018579"
FT                   /id="PRO_0000027917"
FT   CHAIN           31..256
FT                   /note="Hypodermin-A"
FT                   /id="PRO_0000027918"
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        37
FT                   /note="S -> M (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="D -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="L -> W (in Ref. 2; AAA29224)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  27907 MW;  63D12D337F66AA61 CRC64;
     MLKFVILLCS IAYVFGAVVP LGMLSQSDGR IVGGVESKIE DFPWQISLQR DGRHYCGGSI
     YSKNVIITAA HCLRNVVAEE LRVRVGSSYW EHGGSLRNIS KFQIHESYVE PTKEYDVALL
     KLDSDLSFNS TIKAIELTNE IPPEYADAIV SGWGETLVPP PGIPDQLRSV DVKIIHREKC
     ASRNFGYGSN IKASMICAYA IGKDSCQGDS GGPLVVNNLL VGVVSWGIDC ARPSYPGVYV
     DVSHVRSLIV SNAESI