ID   SP34_APIME              Reviewed;         405 AA.
AC   Q8MQS8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Venom serine protease 34;
DE            Short=SP34;
DE            EC=3.4.21.-;
DE   AltName: Allergen=Api m 7;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schmidt M., Winningham K.M., Hoffman D.R.;
RT   "The bee venom protease allergen contains a CUB domain.";
RL   J. Allergy Clin. Immunol. 109:S79-S79(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17073008; DOI=10.1038/nature05260;
RG   Honeybee genome sequencing consortium;
RT   "Insights into social insects from the genome of the honeybee Apis
RT   mellifera.";
RL   Nature 443:931-949(2006).
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; AY127579; AAN02286.1; -; mRNA.
DR   RefSeq; NP_001011584.1; NM_001011584.1.
DR   AlphaFoldDB; Q8MQS8; -.
DR   SMR; Q8MQS8; -.
DR   STRING; 7460.GB48510-PA; -.
DR   Allergome; 3093; Api m 7.0101.
DR   Allergome; 732; Api m 7.
DR   MEROPS; S01.492; -.
DR   PaxDb; Q8MQS8; -.
DR   EnsemblMetazoa; NM_001011584; NP_001011584; GeneID_406095.
DR   GeneID; 406095; -.
DR   KEGG; ame:406095; -.
DR   CTD; 406095; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 585700at2759; -.
DR   PhylomeDB; Q8MQS8; -.
DR   Proteomes; UP000005203; 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; cd00041; CUB; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF50494; SSF50494; 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;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..405
FT                   /note="Venom serine protease 34"
FT                   /id="PRO_5000088947"
FT   DOMAIN          42..147
FT                   /note="CUB"
FT   DOMAIN          161..397
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        95..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        188..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        323..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        345..375
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   405 AA;  45517 MW;  1D8C9211EEA37689 CRC64;
     MIFTNNIAAF QNVVLVKKVK IVLLIFYGSI MFSMTQVNKE ECDYYQNLNL GEIYYIYNPR
     YPLPYSGSKC TWTITSYHRI NLKCSLVEFS ENKNCNAGSL TVKKNFANKY CGNITLNIES
     TSNKMTVILT PPGRFFCEVR PIKRVKDSTN CNCGWKNPSR IVGGTNTGIN EFPMMAGIKR
     TYEPGMICGA TIISKRYVLT AAHCIIDENT TKLAIVVGEH DWSSKTETNA TVLHSINKVI
     IHPKYDIIEK DDWQINDIAL LKTEKDIKFG DKVGPACLPF QHFLDSFAGS DVTVLGWGHT
     SFNGMLSHIL QKTTLNMLTQ VECYKYYGNI MVNAMCAYAK GKDACQMDSG GPVLWQNPRT
     KRLVNIGIIS WGAECGKYPN GNTKVGSYID WIVSQTPDAE YCVIE