ID   PLB2_SCHPO              Reviewed;         662 AA.
AC   O13857;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 4.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Putative lysophospholipase SPAC1A6.03c;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B;
DE   Flags: Precursor;
GN   ORFNames=SPAC1A6.03c;
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).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   ALTERNATIVE SPLICING.
RX   PubMed=24929437; DOI=10.1038/nsmb.2843;
RA   Duncan C.D., Mata J.;
RT   "The translational landscape of fission-yeast meiosis and sporulation.";
RL   Nat. Struct. Mol. Biol. 21:641-647(2014).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O13857-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O13857-2; Sequence=VSP_058508;
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB16353.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CU329670; CAB16353.3; ALT_SEQ; Genomic_DNA.
DR   PIR; T38006; T38006.
DR   RefSeq; NP_593194.3; NM_001018590.3.
DR   AlphaFoldDB; O13857; -.
DR   SMR; O13857; -.
DR   BioGRID; 278694; 122.
DR   STRING; 284812.O13857; -.
DR   iPTMnet; O13857; -.
DR   PaxDb; 4896-SPAC1A6-03c-1; -.
DR   EnsemblFungi; SPAC1A6.03c.1; SPAC1A6.03c.1:pep; SPAC1A6.03c. [O13857-1]
DR   GeneID; 2542220; -.
DR   KEGG; spo:SPAC1A6.03c; -.
DR   PomBase; SPAC1A6.03c; -.
DR   VEuPathDB; FungiDB:SPAC1A6.03c; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; O13857; -.
DR   OMA; FGHINMS; -.
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:O13857; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IC:PomBase.
DR   GO; GO:0005576; C:extracellular region; IC:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; ISS:PomBase.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0004622; F:lysophospholipase activity; ISO: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: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   Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..662
FT                   /note="Putative lysophospholipase SPAC1A6.03c"
FT                   /id="PRO_0000024641"
FT   DOMAIN          76..617
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        411
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
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        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        613
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         642..662
FT                   /note="VRAKPIVFYLFASLLTVSLLL -> TTKASPTHTPWYESLFDLKELKSID
FT                   (in isoform 2)"
FT                   /id="VSP_058508"
SQ   SEQUENCE   662 AA;  73042 MW;  807C64FDF6FEBE79 CRC64;
     MLFNCFGILA LLQILPALAY PPCREQMSDP YEFGESDLMR PGMHDTPLSL MQKREALAIS
     LSKRDSVGSY APYNVTCPSD YMLRPASDGI SSGEQSFIDK RIPKINTQMR SFISNTGLDV
     DVNSVINDSD GPRLGLAFSG GGLRAMVHGG GVLNAFDSRN GNGSSLAGIL QSAMYIAGLS
     GGSWLVGSVA VNNFANITYL RDNVWNLEHS VFAPHGDNVV ENLAYYDDLD DEIDQKKDAG
     FDTSLTDLWG RALSRKLVDA TQGGPNITFS SIRNQTWFQN ADYPYPIIIS DSRLEEEKAI
     PANTSIFEFT PYEFGTWDNG IKAFLPMEYV GTHLKNGVPP DHKCIRNYDN AGFVMGTSAT
     LFNTFLLEWS QEVTSNSTLY DIIHKVFEKL SEDQNDIAPY PNPYQNFTTT NTTVKNPFER
     FDTIDLVDGG EDDENIPIWP LLHPQRFVDV IFAVDATYDD SNGWPDGSSI VTTYERIITY
     NANKSVDVRG FPYIPDEDTI ISLGLNTHPT FFGCDGRNTT AGNHTVDNNT PPLLVYFPNY
     PWVYYSNIST FTMSMNDTLS SGILENAALS ATQNNSDSFA VCLACAMIQR SLERKNMSTP
     SQCSSCFEQY CWNGTTVNNP SAVSNYAPTV LSASTTSGTS SVRAKPIVFY LFASLLTVSL
     LL
//