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VCP_APIME
ID   VCP_APIME               Reviewed;         467 AA.
AC   C9WMM5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Venom serine carboxypeptidase;
DE            EC=3.4.16.5 {ECO:0000255|PROSITE-ProRule:PRU10074};
DE   AltName: Allergen=Api m 9;
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].
RC   TISSUE=Venom duct;
RA   Blank S., Seismann H., Braren I., Bockisch B., Bredehorst R., Ollert M.,
RA   Grunwald T., Spillner E.;
RT   "Identification, recombinant expression and characterization of high
RT   molecular weight hymenoptera venom allergens.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074,
CC         ECO:0000255|PROSITE-ProRule:PRU10075};
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 S10 family. {ECO:0000305}.
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DR   EMBL; FJ765738; ACN71203.1; -; mRNA.
DR   RefSeq; NP_001152775.1; NM_001159303.1.
DR   AlphaFoldDB; C9WMM5; -.
DR   SMR; C9WMM5; -.
DR   Allergome; 6189; Api m 9.
DR   Allergome; 6190; Api m 9.0101.
DR   ESTHER; apime-vcp; Carboxypeptidase_S10.
DR   MEROPS; S10.003; -.
DR   PaxDb; C9WMM5; -.
DR   EnsemblMetazoa; NM_001159303; NP_001152775; LOC410451.
DR   GeneID; 410451; -.
DR   KEGG; ame:410451; -.
DR   PhylomeDB; C9WMM5; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Allergen; Carboxypeptidase; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..467
FT                   /note="Venom serine carboxypeptidase"
FT                   /id="PRO_5000525219"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   467 AA;  53702 MW;  3482EB0FAF6BB466 CRC64;
     MKKLVLLQFL FFISFARGFT NVYPKPKYCP LLHEEDAGIP LFLTPLIENG KIDEARNKAV
     IQHKEVEAIS SYAGFLTVNK KYNSNMFFWF FPALHDPKTA PVVLWLQGGP GATSMYGLFL
     ENGPFIVTKN KTLKMREYSW NKCHNLLYID NPVGTGFSFT EDERGYATNE THVGRDVHTA
     LVQFFELFPE LQTNDFYVTG ESYGGKYVPA VSHAIKDYNI KAKIKINLKG LAIGNGLTDP
     VNQLDYGDYL YQLGLLDANG RNLFQKYEEQ GKNLIKQEKW LEAFDLFDEL LDGDITQQPS
     LYKNLTGFDY YFNYLHEKDP SNDSDYMVEW LQRADVRKAI HVGNRTFIPE SKKVEKYMKA
     DVMQSLAVLI ADLTQHYRVL IYNGQLDIIV AYPLTENYLQ KLKWPGAEKY KTAQRKVWFV
     GNELAGYSKT VDSLTEVLVR NAGHMVPLDQ PKWALDLITR FTHNKGF
 
 
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