ID A0A1D8PPS2_CANAL Unreviewed; 609 AA.
AC A0A1D8PPS2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=PLB2 {ECO:0000313|CGD:CAL0000199062,
GN ECO:0000313|EMBL:AOW30136.1};
GN OrderedLocusNames=CAALFM_C602000WA {ECO:0000313|EMBL:AOW30136.1},
GN orf19.8309 {ECO:0000313|CGD:CAL0000199062};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW30136.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW30136.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW30136.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW30136.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
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DR EMBL; CP017628; AOW30136.1; -; Genomic_DNA.
DR RefSeq; XP_713823.2; XM_708730.2.
DR AlphaFoldDB; A0A1D8PPS2; -.
DR SMR; A0A1D8PPS2; -.
DR STRING; 237561.A0A1D8PPS2; -.
DR EnsemblFungi; C6_02000W_A-T; C6_02000W_A-T-p1; C6_02000W_A.
DR GeneID; 3644562; -.
DR KEGG; cal:CAALFM_C602000WA; -.
DR CGD; CAL0000199062; PLB2.
DR VEuPathDB; FungiDB:C6_02000W_A; -.
DR eggNOG; KOG1325; Eukaryota.
DR InParanoid; A0A1D8PPS2; -.
DR OMA; GPEQYSL; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..609
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5009026866"
FT DOMAIN 30..565
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 609 AA; 67254 MW; 72846694ECF69840 CRC64;
MLVWQSILLF LVGCVLSKSP TNLYTPGYVQ CPEGKLTRSS LDGINSNEKA YIDRRYANAK
SELSKFLHNA KIVDFDVDGF LETANPTIGL AFGGGGYRAM LVGAGELLAL DSRATNPSVL
SGILQSSSYI VGLSGGSWLV GSLASNDLIP VDQLLREDKL WDIQNSLVAY YGVNIVRNTA
MWGNINLQVQ TKQLAGFTVS ITDVYGRALS HQLLTNFDNQ GASFLWSDVT ETTSFQNNEM
PYPILTALGR EPNTVLMNFN STVFELTPYE VGSWDPSLRS FVDTKYIGTR LDDGAPVSKR
CVNGFDNAGF FMGTSSSLFN IVLQQLNNMP IPPFLKELIS KFTLDPVEKL NIDIAQYNPN
PFHKSNNSDT KIAQSRTLYL ADGGEDGQNV PLLPLIHRKV SAIFAFDQSA DKNNWPDGSA
LIKTFERQFS SQGDGIAFPY VPDQNTFRNL NLTSKPTFFG CDAQNLTSLT ENIYDVPVVI
YLANRPFTYF SNTSTFKLKY SDTERQGMIS NGYDVASRLN GKLDNEWAAC VGCAIIRREQ
ERLGIEQTEQ CKKCFENYCW DGTIYKGEPL GDNFSDEGLT TSAADYNSNN VAGINDGGIA
LVKRDDLSN
//
