PLB1_SCHPO
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 25-MAY-2022, entry version 133.
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; 4896.SPAC1A6.04c.1; -.
DR iPTMnet; P78854; -.
DR MaxQB; P78854; -.
DR PaxDb; P78854; -.
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; NVKGFPY; -.
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: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 InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; SSF52151; 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
