ID   PLB3_ASPFU              Reviewed;         630 AA.
AC   P0C958; Q4WYY4; Q6U819;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Lysophospholipase 3;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B 3;
DE   Flags: Precursor;
GN   Name=plb3; ORFNames=AFUA_3G14680;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- INDUCTION: Strongly induced by lecithin.
CC   -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR   EMBL; AAHF01000002; EAL92119.1; -; Genomic_DNA.
DR   RefSeq; XP_754157.1; XM_749064.1.
DR   AlphaFoldDB; P0C958; -.
DR   SMR; P0C958; -.
DR   STRING; 330879.P0C958; -.
DR   Allergome; 8988; Asp f LPL3.
DR   GlyCosmos; P0C958; 15 sites, No reported glycans.
DR   EnsemblFungi; EAL92119; EAL92119; AFUA_3G14680.
DR   GeneID; 3512360; -.
DR   KEGG; afm:AFUA_3G14680; -.
DR   VEuPathDB; FungiDB:Afu3g14680; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; P0C958; -.
DR   OMA; FGHINMS; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   CDD; cd07203; cPLA2_Fungal_PLB; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..606
FT                   /note="Lysophospholipase 3"
FT                   /id="PRO_0000245558"
FT   PROPEP          607..630
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000245559"
FT   DOMAIN          39..587
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   LIPID           606
FT                   /note="GPI-like-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   630 AA;  67417 MW;  0E83E7D7F149CA08 CRC64;
     MKALLSLLTA VAVATATPLD LSLRALPNAP DGYTPAKVSC PATRPSIRGA GSLSPNETSW
     LEIRRKNTVQ PMTDLLGRLN LGFDAAGYID RVSSNASNLP NIAIAVSGGG YRALTNGAGA
     IKAFDSRTQG STQSGHLGGL LQSATYVSGL SGGGWLVGSV YLNNFTTIAD LQSGDHGNVW
     QFSTSILEGP KAKHLQFLST ADYWKDLLKA VDGKSDAGFN TSLTDYWGRA LSYQFINDRT
     GNGGLSYTWS SIALTDPFRR GEMPLPILVA DGRNPGELLI GSNSTVYEFN PWEFGSFDPS
     IFGFAPLEYL GSRFDNGQLP RGEPCVRGFD NAGFVMGTSS SLFNQFILRL NKTDLPDLAK
     DVFSKILTAI GRDGDDIAVY GPNPFYGYRN STAAYSRSRE LDVVDGGEDG QNIPLHPLIQ
     PVRHVDVIFA VDSSADGPYS WPNGSALVAT YERSLNSSGI GNGTVFPAVP DVNTFVNLGL
     NTRPTFFGCD PANLSAPAPL VVYLPNAPYS THSNTSTFQL AYSDSERDEI ITNGYNVVTR
     GNATVDKSWP SCVGCAILQR SMYRTNTSMP AVCNSCFKEY CWNGTVDSKT PRTYEPTLLL
     GSTSTNAAYT QGVTWLVGIL AVGVAMGMTA
//