ID   PLB_NEUCR               Reviewed;         653 AA.
AC   O42790; O42791; Q6MUU7; Q7RW01;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Lysophospholipase;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B;
DE   Flags: Precursor;
GN   Name=lpl; ORFNames=5C2.110, NCU03141;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-45; VAL-115 AND
RP   ASP-597.
RC   STRAIN=74-OR23-1VA / FGSC 2489, and Lindegren 25a;
RA   Catcheside D.E.A., Yeadon P.J.;
RT   "Polymorphism around cog extends into adjacent structural genes.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       {ECO:0000250}.
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: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC03053.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF045574; AAC03052.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AF045575; AAC03053.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BX842637; CAE76554.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA34954.2; -; Genomic_DNA.
DR   RefSeq; XP_964190.2; XM_959097.3.
DR   AlphaFoldDB; O42790; -.
DR   SMR; O42790; -.
DR   STRING; 367110.O42790; -.
DR   GlyCosmos; O42790; 14 sites, No reported glycans.
DR   PaxDb; 5141-EFNCRP00000002857; -.
DR   EnsemblFungi; EAA34954; EAA34954; NCU03141.
DR   GeneID; 3880339; -.
DR   KEGG; ncr:NCU03141; -.
DR   VEuPathDB; FungiDB:NCU03141; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; O42790; -.
DR   OMA; SWWKANE; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..653
FT                   /note="Lysophospholipase"
FT                   /id="PRO_0000024638"
FT   DOMAIN          57..606
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         45
FT                   /note="D -> N (in strain: Lindegren 25a)"
FT                   /evidence="ECO:0000269|Ref.1"
FT   VARIANT         115
FT                   /note="I -> V (in strain: Lindegren 25a)"
FT                   /evidence="ECO:0000269|Ref.1"
FT   VARIANT         597
FT                   /note="E -> D (in strain: Lindegren 25a)"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   653 AA;  70111 MW;  BF8EFCF1F6515A35 CRC64;
     MHLPSSLLIA APLLANVSAE PIRIPQRDVS VVSTSQQLAV RALPDSPSGG YAPAVVDCPK
     TKPTLRKAVD LSNEEKNWLS IRRKNTIQPM RDLLKRANIT GFDSETFMNE AANNISQLPN
     VAIAISGGGY RALMNGAGFV AAADNRIQNT TGAGGIGGLL QSSTYLAGLS GGGWLVGSLF
     SNNFSSIETL LSENKVWDFE NSIFKGPKEA GLSTVNRIQY WSEVAKEVAK KKDAGFETSI
     TDYWGRALSY QLIGADMGGP AYTFSSIAQT DNFQKAETPF PILVADGRAP GDTIISLNAT
     NYEFNPFETG SWDPTVYGFA PTKYLGANFS NGVIPSGGKC VEGLDQAGFV MGTSSTLFNQ
     FLLANISSYD GVPDVLIEAV TSVLKEIGAK RDDVSQIIPN PFLDWNNRTN PNADTLELDL
     VDGGEDLQNI PLNPLTQPVR AVDVIFAVDS SADVTNWPNG TALRATYERT FGSISNGTLF
     PSIPDDWTFI NLGLNNRPSF FGCDVKNFTL NANQKVPPLI VYVPNAPYTA LSNVSTFDPS
     YTMSQRNDII GNGWNSATQG NGTLDSEWPT CVACAVISRS LDRLGRQTPA ACKTCFERYC
     WNGTVNSKDT GVYMPEFKIA DAHALDSGAV AIGKMVNVWS SVVVGVVAAT LLL
//