ID   ACPH1_APIME             Reviewed;         388 AA.
AC   Q5BLY5; B6E2X9; Q4TUB9;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Venom acid phosphatase Acph-1;
DE            EC=3.1.3.2;
DE   AltName: Allergen=Api m 3;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-53; 62-72; 75-130;
RP   134-154 AND 312-381, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RC   TISSUE=Venom, and Venom gland;
RA   Hoffman D.R., Weimer E.T., Sakell R.H., Schmidt M.;
RT   "Sequence and characterization of honeybee venom acid phosphatase.";
RL   J. Allergy Clin. Immunol. 115:S107-S107(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Zhang Q., Liu Z., Wu Y.;
RT   "Molecular cloning of honeybee venom allergen acid phosphatase.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-388, AND ALLERGEN.
RC   TISSUE=Venom gland;
RX   PubMed=16630944; DOI=10.1016/j.jaci.2005.12.1331;
RA   Grunwald T., Bockisch B., Spillner E., Ring J., Bredehorst R., Ollert M.W.;
RT   "Molecular cloning and expression in insect cells of honeybee venom
RT   allergen acid phosphatase (Api m 3).";
RL   J. Allergy Clin. Immunol. 117:848-854(2006).
RN   [5]
RP   REVIEW.
RX   PubMed=16645223; DOI=10.1385/criai:30:2:109;
RA   Hoffman D.R.;
RT   "Hymenoptera venom allergens.";
RL   Clin. Rev. Allergy Immunol. 30:109-128(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:16630944, ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AY939855; AAX33235.1; -; mRNA.
DR   EMBL; FJ200211; ACI25605.1; -; mRNA.
DR   EMBL; DQ058012; AAY57281.1; -; mRNA.
DR   RefSeq; NP_001013377.2; NM_001013359.2.
DR   AlphaFoldDB; Q5BLY5; -.
DR   SMR; Q5BLY5; -.
DR   STRING; 7460.Q5BLY5; -.
DR   Allergome; 2778; Api m A1-A2-A3.
DR   Allergome; 3090; Api m 3.0101.
DR   Allergome; 47; Api m 3.
DR   PaxDb; 7460-GB41338-PA; -.
DR   GeneID; 411830; -.
DR   KEGG; ame:411830; -.
DR   CTD; 48445; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   InParanoid; Q5BLY5; -.
DR   BRENDA; 3.1.3.2; 387.
DR   Proteomes; UP000005203; Linkage group LG5.
DR   Proteomes; UP001105180; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..388
FT                   /note="Venom acid phosphatase Acph-1"
FT                   /id="PRO_5000095341"
FT   ACT_SITE        26
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        145..355
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..334
FT                   /evidence="ECO:0000250"
FT   CONFLICT        152
FT                   /note="L -> F (in Ref. 2; ACI25605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="S -> A (in Ref. 2; ACI25605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="R -> G (in Ref. 2; ACI25605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="V -> A (in Ref. 2; ACI25605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   388 AA;  45389 MW;  DD3327ECC2B03C6B CRC64;
     MSVIAILAMV VGVQAELKQI NVIFRHGDRI PDEKNEMYPK DPYLYYDFYP LERGELTNSG
     KMREYQLGQF LRERYGDFLG DIYTEESVSA LSSFYDRTKM SLQLVLAALY PPNKLQQWNE
     DLNWQPIATK YLRRYEDNIF LPEDCLLFTI ELDRVLESPR GKYEFSKYDK LKKKLEEWTG
     KNITTPWDYY YIYHTLVAEQ SYGLTLPSWT NNIFPRGELF DATVFTYNIT NSTPLLKKLY
     GGPLLRIFTK HMLDVVSGTQ KKKRKIYLFS GHESNIASVL HALQLYYPHV PEYSSSIIME
     LHNIEGTHYV KIVYYLGIPS EARELQLPGC EVLCPLYKYL QLIENVIPSN EELICDKRFV
     DESANNLSIE ELDFVKLNLI RIAGTENK
//