ID B6K3L5_SCHJY Unreviewed; 652 AA.
AC B6K3L5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=plb2 {ECO:0000313|JaponicusDB:SJAG_03204};
GN ORFNames=SJAG_03204 {ECO:0000313|EMBL:EEB08072.1};
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:EEB08072.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB08072.1, 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; KE651167; EEB08072.1; -; Genomic_DNA.
DR RefSeq; XP_002174365.1; XM_002174329.2.
DR AlphaFoldDB; B6K3L5; -.
DR STRING; 402676.B6K3L5; -.
DR EnsemblFungi; EEB08072; EEB08072; SJAG_03204.
DR GeneID; 7049113; -.
DR JaponicusDB; SJAG_03204; plb2.
DR VEuPathDB; FungiDB:SJAG_03204; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_1_1; -.
DR OMA; FASCLAC; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
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: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 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:SF60; LYSOPHOSPHOLIPASE C1786.02-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 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..25
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 26..652
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005123665"
FT DOMAIN 61..609
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 652 AA; 71070 MW; 06F90EA5BC8C09C2 CRC64;
MRSLTCTQLL YAIALFFGLS QAVPASEDES ISEAVALSRR AWKRPPDPPS TDASYAPKIG
QCGNGTDLLT TIPSNSLPEL EADYITKRKT SADTALLKFL GQYNVTNHTL SNLVGENGPR
VGIAVSGGGF RSLFFAGGAL EAMDARTPNS SLGGLLQSST YLTGLDGGAW LVGSLAVNNF
RTVQNLSESA WYSRLGIFYI VDTHVGDNEN YYTNVCNEVD QKSAAGFNIS MTDYWGRALA
RRVTGMLRGG PNTTFSSVQN AAWFKNASFP YPVMVAEGLS SNLPKFHNGT QYNSSVYEIS
PYYFGTFDNG VRAVMPTYYL GTNLTNGSAT NGQCVTLYDN LGFLMGTTST RFNEALLGVS
MMESRMSRRL GHALRRMRVN GTHLSYYPNF VKDSSAAEDT TGASTNLSSA TYLNLYDGGS
DGQNIPVWPL LQPERGVDVV FALDSSSDTL TYWPNGTALV KTYERITKRS NVSAAGDYSV
KHFPYIPSVN TFINLGLNNK PTFFGCDGRN TTRGNVSVDA NTPPVIVYMP NAPWTMMSNT
ADDRYRYGQG SIRELVENGR GAASLGGSSE FAQCVACAVI QRSLERRNMS ASAKCQQCFQ
EYCWNGTLDD RLLANTKARV DYQPFVRSGA SATTKITLST LLLSLISYYF VF
//
