ACPH1_APIME
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 25-MAY-2022, entry version 78.
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; Apidae;
OC 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.GB41338-PA; -.
DR Allergome; 2778; Api m A1-A2-A3.
DR Allergome; 3090; Api m 3.0101.
DR Allergome; 47; Api m 3.
DR PaxDb; Q5BLY5; -.
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; 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; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR029630; Api_m_3.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF183; PTHR11567:SF183; 1.
DR Pfam; PF00328; His_Phos_2; 2.
DR SUPFAM; SSF53254; SSF53254; 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
