ID   SP4_POLDO               Reviewed;         277 AA.
AC   Q7Z269;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Venom serine protease;
DE            EC=3.4.21.-;
DE   AltName: Allergen=Pol d 4;
DE   Flags: Precursor;
OS   Polistes dominula (European paper wasp) (Vespa dominula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Polistini; Polistes.
OX   NCBI_TaxID=743375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fitch C.D., Hoffman D.R., Schmidt M.;
RT   "Cloning of a paper wasp venom serine protease allergen.";
RL   J. Allergy Clin. Immunol. 107:S221-S221(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15480337; DOI=10.1016/j.jaci.2004.07.043;
RA   Winningham K.M., Fitch C.D., Schmidt M., Hoffman D.R.;
RT   "Hymenoptera venom protease allergens.";
RL   J. Allergy Clin. Immunol. 114:928-933(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000250}.
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; AY285998; AAP37412.1; -; mRNA.
DR   RefSeq; NP_001310266.1; NM_001323337.1.
DR   AlphaFoldDB; Q7Z269; -.
DR   SMR; Q7Z269; -.
DR   Allergome; 3437; Pol d 4.0101.
DR   Allergome; 587; Pol d 4.
DR   MEROPS; S01.492; -.
DR   EnsemblMetazoa; XM_015328755.1; XP_015184241.1; LOC107070494.
DR   GeneID; 107070494; -.
DR   OrthoDB; 2877984at2759; -.
DR   Proteomes; UP000694924; Unplaced.
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; Trypsin-like serine proteases; 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   PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24250:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   2: Evidence at transcript level;
KW   Allergen; Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..277
FT                   /note="Venom serine protease"
FT                   /id="PRO_5000090673"
FT   DOMAIN          34..269
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        220
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        192..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        216..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   277 AA;  30804 MW;  9B316A8824C5CDA6 CRC64;
     MNCGKIILLF ITIIGVAKSR EENCKCGWDN PSRIVNGVET EINEFPMVAR LIYPSPGMYC
     GGTIITPQHI VTAAHCLQKY KRTNYTGIHV VVGEHDYTTD TETNVTKRYT IAEVTIHPNY
     NSHNNDIAIV KTNERFEYSM KVGPVCLPFN YMTRNLTNET VTALGWGKLR YNGQNSKVLR
     KVDLHVITRE QCETHYGAAI ANANLLCTFD VGRDACQNDS GGPILWRSPT TDNLILVGVV
     NFGRTCADDA PGGNARVTSF MEFIHNATIG ETYCKAD
//