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PLB7_SCHPO
ID   PLB7_SCHPO              Reviewed;         673 AA.
AC   P0CU03; P78834; Q9P327;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Putative lysophospholipase SPBC1348.10c;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B;
DE   Flags: Precursor;
GN   ORFNames=SPBC1348.10c;
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 [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).
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}.
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DR   EMBL; CU329671; CAB94277.1; -; Genomic_DNA.
DR   PIR; T50281; T50281.
DR   RefSeq; NP_592772.1; NM_001020935.2.
DR   RefSeq; NP_592781.1; NM_001018181.2.
DR   AlphaFoldDB; P0CU03; -.
DR   SMR; P0CU03; -.
DR   STRING; 284812.P0CU03; -.
DR   EnsemblFungi; SPAC977.09c.1; SPAC977.09c.1:pep; SPAC977.09c.
DR   EnsemblFungi; SPBC1348.10c.1; SPBC1348.10c.1:pep; SPBC1348.10c.
DR   GeneID; 2541836; -.
DR   GeneID; 5802732; -.
DR   KEGG; spo:SPAC977.09c; -.
DR   KEGG; spo:SPBC1348.10c; -.
DR   PomBase; SPBC1348.10c; -.
DR   VEuPathDB; FungiDB:SPAC977.09c; -.
DR   VEuPathDB; FungiDB:SPBC1348.10c; -.
DR   OMA; FARYCWN; -.
DR   PhylomeDB; P0CU03; -.
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:P0CU03; -.
DR   Proteomes; UP000002485; Chromosome II.
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:0042597; C:periplasmic space; ISO:PomBase.
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   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   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..673
FT                   /note="Putative lysophospholipase SPBC1348.10c"
FT                   /id="PRO_0000437228"
FT   DOMAIN          74..615
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   REGION          631..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   673 AA;  74596 MW;  B39A773E76CD694B CRC64;
     MYVNYIGLFA FVQISLTLAY PPGRVEISEI YDFEESSSYK GQDIDTSVLY TLSKRKPALV
     KRSTDASYAP FNVTCSNDNL LRPASEGLNE GEQSYINKRI SKVNSELRSF ISKTGLNVDL
     DKVVNSSDGP RLGIAFSGGG LRAMVNGGGA FNAFDSRFES DSPLSGLLQS AMYISGLSGG
     SWLVGSVAIN NFTNITYLRD NVWNLEHSVF APHGDNVIEN LNYYNDLRKE IDQKKHAGFD
     CSLTDLWGRA LSRKLVDAER GGPGITYSSM RNQSWFQNAD YPYPIIVADS RLEEETAIPA
     NTSIFEFTAY EFGTWDNGIK AFIPMEYVGT HLLDGVPPDK SCIHNYDNAG FVMGTSATLF
     NSFLLDWNEN VKKNDTYYDI LHAILEDLSK HQDDIAPYPN PYQNYTTSNT SVVNAFEPYD
     TIDLVDGGED RENIPLWPLL HPQRFVDVVF AIDSTYNDPY GWPLGSSIVA TYERVVTFNA
     NKSVDVRGFP YIPDENTIIS LGLNTRPTFF GCDGKNTTAG NHDVDNNTPP LLVYFPNYPW
     TYYSNISTFT MSMDDKMANG ILENAFMSTT QNNNESFAVC LACAIIQRSL ERKKLSTPTQ
     CSSCFQEYCW DGTLATSTAS VYDPTVMSAA TTSRAPSGTT SGTASSTTSS SVASATPTHK
     HWWDSIFEAK ENP
 
 
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