ID B6JZP8_SCHJY Unreviewed; 608 AA.
AC B6JZP8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=plb1 {ECO:0000313|JaponicusDB:SJAG_02091};
GN ORFNames=SJAG_02091 {ECO:0000313|EMBL:EEB07016.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07016.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07016.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
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).
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 Evidence={ECO:0000256|RuleBase:RU362103};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family.
CC {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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DR EMBL; KE651168; EEB07016.1; -; Genomic_DNA.
DR RefSeq; XP_002173309.1; XM_002173273.2.
DR AlphaFoldDB; B6JZP8; -.
DR STRING; 402676.B6JZP8; -.
DR EnsemblFungi; EEB07016; EEB07016; SJAG_02091.
DR GeneID; 7052026; -.
DR JaponicusDB; SJAG_02091; plb1.
DR VEuPathDB; FungiDB:SJAG_02091; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR OMA; ESSATKM; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
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: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:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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:SF61; LYSOPHOSPHOLIPASE 1; 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 Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU00555};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 22..608
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005123649"
FT DOMAIN 56..592
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 608 AA; 66700 MW; EA5A3B8FA608F2A1 CRC64;
MLKGLFVWTL YLASNLLSAS AFPADGAGSI AHVLKKRDSS SKDSKKKPSY APYYTDCPSD
NIVESVSSGS IPAAERSYLS THKSVADPAM KQYFINAGLP GINADDLVGS KGPVVGIAIS
GGGFRSMLTG AGALSAMDSR HNNHTVLTGL LQAASYVTGV DGGAWLLGSM AVNNFSTVNH
LKEKIWRLQR DILFPKSIIL YNADFYKDLV TETAEKKAAG FDISLSDYFG RVLSRPFVDP
KWGAPNVSFS SIESQEWYAD AEFPYPIVMA TTKKPDTQLN RLNDTIIEIS PSAFGTFDHG
VRAFVPTEYI GTTLDNGKSD NGSCVANYDN FGLIMAIAST QFNGLMRNFN DSSTKNGRVL
QDYLKGNFTE ANQDIEPIPN PFKGLSSAAN ADGLSDSDSL YLADASESQN LGIWPLIQKG
RDVDVIIAVD NSANTEYLWP DGSALVATYE RALAEKDKED SNVKGFPYIP SQESFVNLHY
NDRPVFFGCD GRNTTYGNHT VTRNTPPLVV YLPNVPYIYY TNISTERLYY TEDQEKQLLT
NGLIGATYNN NTYFGQCVAC AVIKRTLERQ NMTASPQCQE CYARFCWSGV QDNTESDTTY
LYDPKLAL
//
