ID   PLB1_SCHPO              Reviewed;         613 AA.
AC   P78854;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Lysophospholipase 1;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B 1;
DE   Flags: Precursor;
GN   Name=plb1; ORFNames=SPAC1A6.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=12715160; DOI=10.1007/s00438-003-0820-8;
RA   Yang P., Du H., Hoffman C.S., Marcus S.;
RT   "The phospholipase B homolog Plb1 is a mediator of osmotic stress response
RT   and of nutrient-dependent repression of sexual differentiation in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Mol. Genet. Genomics 269:116-125(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 294-613.
RA   Kawamukai M.;
RT   "S.pombe phospholipase B homolog.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-613.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       Required for survival under high osmolarity, for normal osmotic stress-
CC       induced gene expression, and for nutrient-mediated repression of sexual
CC       differentiation. {ECO:0000269|PubMed:12715160}.
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}.
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DR   EMBL; AY235223; AAO46159.1; -; mRNA.
DR   EMBL; CU329670; CAB16354.1; -; Genomic_DNA.
DR   EMBL; AB005603; BAA21498.1; -; mRNA.
DR   EMBL; D89204; BAA13865.1; -; mRNA.
DR   PIR; T38007; T38007.
DR   RefSeq; NP_593196.1; NM_001018592.2.
DR   AlphaFoldDB; P78854; -.
DR   SMR; P78854; -.
DR   BioGRID; 278956; 109.
DR   DIP; DIP-59118N; -.
DR   IntAct; P78854; 1.
DR   STRING; 284812.P78854; -.
DR   GlyCosmos; P78854; 13 sites, No reported glycans.
DR   iPTMnet; P78854; -.
DR   MaxQB; P78854; -.
DR   PaxDb; 4896-SPAC1A6-04c-1; -.
DR   EnsemblFungi; SPAC1A6.04c.1; SPAC1A6.04c.1:pep; SPAC1A6.04c.
DR   GeneID; 2542497; -.
DR   KEGG; spo:SPAC1A6.04c; -.
DR   PomBase; SPAC1A6.04c; plb1.
DR   VEuPathDB; FungiDB:SPAC1A6.04c; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; P78854; -.
DR   OMA; PYEFYSN; -.
DR   PhylomeDB; P78854; -.
DR   Reactome; R-SPO-111995; phospho-PLA2 pathway.
DR   Reactome; R-SPO-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-SPO-1482798; Acyl chain remodeling of CL.
DR   Reactome; R-SPO-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-SPO-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-SPO-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-SPO-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-SPO-1483115; Hydrolysis of LPC.
DR   Reactome; R-SPO-1483152; Hydrolysis of LPE.
DR   Reactome; R-SPO-1483166; Synthesis of PA.
DR   Reactome; R-SPO-2142753; Arachidonic acid metabolism.
DR   Reactome; R-SPO-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-SPO-432142; Platelet sensitization by LDL.
DR   Reactome; R-SPO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   PRO; PR:P78854; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR   GO; GO:0005576; C:extracellular region; IC:PomBase.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004622; F:lysophospholipase activity; ISS:PomBase.
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:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
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:SF61; LYSOPHOSPHOLIPASE 1; 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   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..613
FT                   /note="Lysophospholipase 1"
FT                   /id="PRO_0000024640"
FT   DOMAIN          55..593
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
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        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
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        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   613 AA;  67119 MW;  EE7C8B5D78A8FFFD CRC64;
     MLFRGLSLWM LFLASCLSAL ALPAAEDDGS VKVFKRAKKH STKQEGPSYA PYYVDCPSDN
     IVESLSSNEI PSAESEYLST RSTITNTAMK DFLRNANLPG LNADTLSGSE GPSIGIALSG
     GGLRAMILGS GALSAMDARH DNHTVLTGLL QASDYLVGTD GSAWTVGGIA LNNFSTINDF
     SKLWAFNHPL MYPKSAIVFN AHFYSSIMNE VAEKANAGFN ISLSDYWGRV ISRTLGDTTY
     GFPNVSLSSI TSQEWYRNAN FPYPIITFAT QNYGEDISNV NTTFFEASPN VFGTFDHGIN
     SFIPTEYLGT TLNNGASSNG SCVINYDNFG FMMGASSTYF NKIMRNFNDS STKNGRIIQQ
     YLKGNFSENG QQIISIPNPF QGVESANSDA ANNLGSSSSL NLVDTFLTGE KIPLWPLLQK
     GRDVDVIVAV DNGDDSEWLW PNGNSLVQTY ERVVAAQAAG NTNVKGFPYV PSQQSFVSLH
     FNDRPVFFGC DGRNTTAGNH TVTRDTPPLV IYLPNVPYNY FTNISTDRTY YTEDMIQQLL
     TNGLISSTVD NDTYFGQCFA CAVVKRTLER NNITASPECQ QCYYNYCWSG LYDDSAANDD
     IVYNPTCRLG EGI
//