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Database: UniProt
Entry: J8PWN8_SACAR
LinkDB: J8PWN8_SACAR
Original site: J8PWN8_SACAR 
ID   J8PWN8_SACAR            Unreviewed;       684 AA.
AC   J8PWN8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=SU7_3175 {ECO:0000313|EMBL:EJS41778.1};
OS   Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS41778.1, ECO:0000313|Proteomes:UP000006968};
RN   [1] {ECO:0000313|EMBL:EJS41778.1, ECO:0000313|Proteomes:UP000006968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-6 / AS 2.3317 / CBS 10644
RC   {ECO:0000313|Proteomes:UP000006968};
RX   PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA   Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA   Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA   Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT   "High quality de novo sequencing and assembly of the Saccharomyces
RT   arboricolus genome.";
RL   BMC Genomics 14:69-69(2013).
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   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJS41778.1}.
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DR   EMBL; ALIE01000179; EJS41778.1; -; Genomic_DNA.
DR   AlphaFoldDB; J8PWN8; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000006968; Chromosome XV.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0009395; P:phospholipid catabolic process; IEA:InterPro.
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   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..594
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   684 AA;  75185 MW;  B396AD8D03713B18 CRC64;
     MIHPLCSNLI IAYIFIIFSR FLVVPTNAWS PTDNYGPGMV SCPDDINLVR EATSISQNET
     AWLEKRNKVT SVALEDFLIR ATANFSDSSE ILSKLFDDNN NENLPKIAVA ISGGGYRSML
     TGAGILAAMD NRTEGAYEHG LGGLLQSTTY LSGASGGNWL VGTLALNNWT SVQEILDDMH
     NDDSIWDLSD SIVTPGGINI FKTAKRWDDI SNAVESKQSC NYNTSLADIW GRALAYNFFP
     SLHRGGIGLT WSSIRDFPAF KNAEMPFPIS VSDGRYPGTK VINLNATVFE FNPFEMGSWD
     PSLNSFTNVR YLGTNVSNGV PLERGKCTAG FDNAGFIMGT SSTLFNQFLL RINSTHLPGF
     ITRLARHFLK DLSQDFNDIA VYSPNPFKDT KFLDSDYTTS IVDSDSLFLV DGGEDDENVP
     VLPLIQKERD VDVIFAVDNS ADMRLAWPDG SSLVHTYERQ FVKQGQGMSF PYVPDTNTFV
     NLGLNKRPTF FGCDANNLTS LQYVPPLVIY LPNAEYSFES NQSAFKLSYS ESQRRSMIQN
     GFEIATRNNF TDDPNFMGCV GCAIMRRKQQ ELNVTLPAEC EACFTNYCWN GTLDTSPLPD
     IEKDVHHSFI TVGNFNSSAG QQIDHLIGPE DSESLSSSSS SVTPSATTTL EKKIAANTGS
     HISGISTKLA AIMILVVFTL TGGI
//
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