PLB2_SCHPO
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 25-MAY-2022, entry version 122.
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; 4896.SPAC1A6.03c.1; -.
DR PaxDb; O13857; -.
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; WDISHSI; -.
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 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 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
