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