PLB4_SCHPO
ID PLB4_SCHPO Reviewed; 673 AA.
AC P0CU02; P78834; Q9P327;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Putative lysophospholipase SPAC977.09c;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B;
DE Flags: Precursor;
GN ORFNames=SPAC977.09c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-673.
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 {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; CU329670; CAB69631.1; -; Genomic_DNA.
DR EMBL; D89183; BAA13845.1; -; mRNA.
DR PIR; T50281; T50281.
DR RefSeq; NP_592772.1; NM_001020935.2.
DR RefSeq; NP_592781.1; NM_001018181.2.
DR AlphaFoldDB; P0CU02; -.
DR SMR; P0CU02; -.
DR STRING; 4896.SPAC977.09c.1; -.
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; SPAC977.09c; -.
DR VEuPathDB; FungiDB:SPAC977.09c; -.
DR VEuPathDB; FungiDB:SPBC1348.10c; -.
DR eggNOG; KOG1325; Eukaryota.
DR OMA; FARYCWN; -.
DR PhylomeDB; P0CU02; -.
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:P0CU02; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
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:0005634; C:nucleus; HDA: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 2: Evidence at transcript level;
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 SPAC977.09c"
FT /id="PRO_0000024642"
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
