PA1_SOLIN
ID PA1_SOLIN Reviewed; 346 AA.
AC Q68KK0; E9IC36; Q9TXF4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Phospholipase A1 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000305|PubMed:15753912};
DE AltName: Full=Allergen Sol i I;
DE AltName: Full=Venom allergen 1;
DE AltName: Full=Venom allergen I;
DE AltName: Allergen=Sol i 1 {ECO:0000303|PubMed:15753912, ECO:0000303|Ref.1};
DE Flags: Precursor;
OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Solenopsis.
OX NCBI_TaxID=13686;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Schmidt M., Sakell R.H., Hoffman D.R.;
RT "The sequence of Sol i 1, the cross-reactive allergen of imported fire ant
RT venom.";
RL J. Allergy Clin. Immunol. 113:S73-S73(2004).
RN [2]
RP PROTEIN SEQUENCE OF 61-94; 109-125; 130-153; 154-178; 245-270 AND 322-346,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8588684; DOI=10.1111/j.1398-9995.1995.tb01196.x;
RA Hoffman D.R.;
RT "Fire ant venom allergy.";
RL Allergy 50:535-544(1995).
RN [3]
RP PROTEIN SEQUENCE OF 38-94; 109-125; 135-138; 141-150; 155-178; 191-205;
RP 244-266 AND 316-346, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP ALLERGEN.
RC TISSUE=Venom;
RX PubMed=15753912; DOI=10.1016/j.jaci.2004.11.020;
RA Hoffman D.R., Sakell R.H., Schmidt M.;
RT "Sol i 1, the phospholipase allergen of imported fire ant venom.";
RL J. Allergy Clin. Immunol. 115:611-616(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 145-281.
RX PubMed=21282665; DOI=10.1073/pnas.1009690108;
RA Wurm Y., Wang J., Riba-Grognuz O., Corona M., Nygaard S., Hunt B.G.,
RA Ingram K.K., Falquet L., Nipitwattanaphon M., Gotzek D., Dijkstra M.B.,
RA Oettler J., Comtesse F., Shih C.J., Wu W.J., Yang C.C., Thomas J.,
RA Beaudoing E., Pradervand S., Flegel V., Cook E.D., Fabbretti R.,
RA Stockinger H., Long L., Farmerie W.G., Oakey J., Boomsma J.J., Pamilo P.,
RA Yi S.V., Heinze J., Goodisman M.A., Farinelli L., Harshman K., Hulo N.,
RA Cerutti L., Xenarios I., Shoemaker D., Keller L.;
RT "The genome of the fire ant Solenopsis invicta.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5679-5684(2011).
RN [5]
RP ISOLATION, AND ALLERGEN.
RX PubMed=3192865; DOI=10.1016/0091-6749(88)90084-x;
RA Hoffman D.R., Dove D.E., Jacobson R.S.;
RT "Allergens in Hymenoptera venom. XX. Isolation of four allergens from
RT imported fire ant (Solenopsis invicta) venom.";
RL J. Allergy Clin. Immunol. 82:818-827(1988).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 activity. Shows hemolytic activity (Probable).
CC {ECO:0000305|PubMed:15753912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000305|PubMed:15753912};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15753912,
CC ECO:0000269|PubMed:8588684}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15753912, ECO:0000305|PubMed:8588684}.
CC -!- PTM: Contains six disulfide bonds. {ECO:0000250}.
CC -!- PTM: N-glycosylated; contains mannose. {ECO:0000269|PubMed:15753912}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:3192865). It
CC exhibits some cross-reactivity with IgE antibodies from patients
CC sensitized to other Hymenoptera venoms (PubMed:15753912).
CC {ECO:0000269|PubMed:15753912, ECO:0000269|PubMed:3192865}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AY684998; AAT95008.1; -; mRNA.
DR EMBL; GL762181; EFZ21865.1; -; Genomic_DNA.
DR RefSeq; NP_001291510.1; NM_001304581.1.
DR RefSeq; XP_011173569.1; XM_011175267.1.
DR AlphaFoldDB; Q68KK0; -.
DR SMR; Q68KK0; -.
DR Allergome; 3481; Sol i 1.0101.
DR Allergome; 630; Sol i 1.
DR ESTHER; solin-q68kk0; Insect_Phospholipase.
DR EnsemblMetazoa; NM_001304581.1; NP_001291510.1; LOC105205761.
DR GeneID; 105205761; -.
DR KEGG; soc:105205761; -.
DR HOGENOM; CLU_1870320_0_0_1; -.
DR OrthoDB; 1468006at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hemolysis; Hydrolase; Lipid degradation; Lipid metabolism;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..37
FT /evidence="ECO:0000305|PubMed:15753912"
FT /id="PRO_0000401922"
FT CHAIN 38..346
FT /note="Phospholipase A1"
FT /evidence="ECO:0000269|PubMed:15753912"
FT /id="PRO_5000093784"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 130
FT /note="N -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> R (in Ref. 4; EFZ21865)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="C -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="MV -> VPS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="C -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Q -> QE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38417 MW; B0A88EC6C3D876BF CRC64;
MRKFAAIFVV FFVQCTHLYS LAQARAEPDP GVVEYLKQSC VYGNSSYINV YLYNSRFQGK
NLGNQQSCQD INASLPVVFI THGFTSSAQV STFKDLANAF VQKGHTAFIV DWSEAACTDG
LPGVQFAEYN AAASNTYDIG QLMAKYTVDL MNKCKIPLNN IQYVGHSLGS HVCGFAAKHV
KKLINKTMPY ILALDPADPS FGSNKCGERI CKSDAKRIVV FKTSILGIGE NIIGHLLIVF
DGGKSQPACS WYDVPCSHSE SIVYATGMVS GRCQHLAVPW TAQQRINPIQ WKFWRVFTSN
IPAYPTSDTT NCVVLNTNVF KNDNTFEGEY HAFPDCARNL FKCRQQ
