ID   Q9P4F6_TUBBO            Unreviewed;       211 AA.
AC   Q9P4F6;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Phospholipase A2 group XIII {ECO:0000313|EMBL:AAF80454.1};
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251 {ECO:0000313|EMBL:AAF80454.1};
RN   [1] {ECO:0000313|EMBL:AAF80454.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 96540 {ECO:0000313|EMBL:AAF80454.1};
RX   PubMed=11566873; DOI=10.1093/emboj/20.18.5079;
RA   Soragni E., Bolchi A., Balestrini R., Gambaretto C., Percudani R.,
RA   Bonfante P., Ottonello S.;
RT   "A nutrient-regulated, dual localization phospholipase A(2) in the
RT   symbiotic fungus Tuber borchii.";
RL   EMBO J. 20:5079-5090(2001).
RN   [2] {ECO:0000313|EMBL:AAF80454.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 96540 {ECO:0000313|EMBL:AAF80454.1};
RX   PubMed=16698294; DOI=10.1016/j.fgb.2006.04.001;
RA   Montanini B., Gabella S., Abba S., Peter M., Kohler A., Bonfante P.,
RA   Chalot M., Martin F., Ottonello S.;
RT   "Gene expression profiling of the nitrogen starvation stress response in
RT   the mycorrhizal ascomycete Tuber borchii.";
RL   Fungal Genet. Biol. 43:630-641(2006).
RN   [3] {ECO:0007829|PDB:4AUP}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 89-211, AND DISULFIDE BONDS.
RX   PubMed=23192346; DOI=10.1074/jbc.M112.384156;
RA   Cavazzini D., Meschi F., Corsini R., Bolchi A., Rossi G.L., Einsle O.,
RA   Ottonello S.;
RT   "Autoproteolytic Activation of a Symbiosis-regulated Truffle Phospholipase
RT   A2.";
RL   J. Biol. Chem. 288:1533-1547(2013).
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DR   EMBL; AF162269; AAF80454.1; -; mRNA.
DR   PDB; 4AUP; X-ray; 1.90 A; A/B=89-211.
DR   PDBsum; 4AUP; -.
DR   AlphaFoldDB; Q9P4F6; -.
DR   SMR; Q9P4F6; -.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR015141; PLipase_A2_prok/fun.
DR   Pfam; PF09056; Phospholip_A2_3; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4AUP}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..211
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004332059"
FT   REGION          45..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        128..144
FT                   /evidence="ECO:0007829|PDB:4AUP"
FT   DISULFID        180..194
FT                   /evidence="ECO:0007829|PDB:4AUP"
SQ   SEQUENCE   211 AA;  23155 MW;  6D0DF990AE317B9D CRC64;
     MVKIAAIILL MGILANAAAI PVSEPAALNK RGNAEVIAEQ TGDVPDFNTQ ITEPTGEGDR
     GDVADETNLS TDIVPETEAA SFAASSVSAA LSPVSDTDRL LYSTAMPAFL TAKRNKNPGN
     LDWSDDGCSK SPDRPAGFNF LDSCKRHDFG YRNYKKQHRF TEANRKRIDD NFKKDLYNEC
     AKYSGLESWK GVACRKIANT YYDAVRTFGW L
//