PLB3_CANAX
ID PLB3_CANAX Reviewed; 754 AA.
AC Q9UVX1; O94046;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Lysophospholipase 3;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B 3;
DE Flags: Precursor;
GN Name=PLB3; Synonyms=PLB1; ORFNames=Ca41C10.12;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SS;
RA Theiss S., Koehler G.A.;
RT "Putative phospholipase B precursor of Candida albicans.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Taylor K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC Phospholipase B may well contribute to pathogenicity by abetting the
CC fungus in damaging and traversing host cell membranes, processes which
CC likely increase the rapidity of disseminated infection (By similarity).
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; AF038128; AAF08980.1; -; Genomic_DNA.
DR EMBL; AL033501; CAA21996.1; -; Genomic_DNA.
DR PIR; T18238; T18238.
DR AlphaFoldDB; Q9UVX1; -.
DR SMR; Q9UVX1; -.
DR VEuPathDB; FungiDB:C1_08230C_A; -.
DR VEuPathDB; FungiDB:CAWG_00600; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..754
FT /note="Lysophospholipase 3"
FT /id="PRO_0000024632"
FT DOMAIN 114..670
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 25..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 377
FT /note="N -> D (in Ref. 1; AAF08980)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> E (in Ref. 1; AAF08980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 81412 MW; 8291D959B005B554 CRC64;
MKVNLKLIIG SILISQAQAI WPFDSSGSSS SSDSSPSETG SSGGTFPFDL FGSGSSLTQS
SSAQASSTKS TSDSASSTDS SLFSSSNSGS SWYQTFLDGD SGDQKTDYAP FNLTCPSKKT
FIRTASELSQ QEKDYIHKRQ ETTNKNLIDF LSKRANLSDF DAKSFINDNA PNHNITIGLS
FSGGGYRAML AGAGQILGLD GRYEDANKHG LGGLLDSSTY VVGLSGGNWL VGSLALNDWL
SVGDIVNGKS TIWQLQDSIL NPSGMRIDKT IAYYYGLAQA VQAKEDAGFQ TSVTDTWGRA
LSYQFFEEDD SGTGGANITW SSIRNLSSFQ DHSMPYPIVV ANGRTPGTYI INENSTIFEI
SPYELGSWDP SLKSFSNIQY LGSSVNNGNP NNTDICVNNF DNAGFIMGTS SSLFNQILLQ
LDNYSINSII KMILEKVLTD VSDEEYDIAV YEPNPFFGAD SAGIKSITTN DTLYLCDGGE
DLQNVPFYPL IQNKRGVDVI FAFDNSADTN SSWPNGTSIQ ETYKRQFSKQ GKGTPFPFAP
DYKTFLDKNM GDKPVFFGCN SSDLEDLVAW HENDKINVTD VPLVVYTSNT RMSYNSNFST
FKLSYSDQEK FGAIRNGFET VTRNNLTDDE NWSTCVGCAI IRRQQERLGE EQSDECKKCF
QEYCWTGGFK DAASVSSVSG ISGLAAKTHT SGGTSSTTQQ TSTTTGSSAN GGSSSTGSSS
SSKKKNGGDL VNGGVPSSIF LVFNSLLGLI IAYL
