PLB1_CANAL
ID PLB1_CANAL Reviewed; 605 AA.
AC Q9UWF6; A0A1D8PPS3; O74207; Q59W35;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Lysophospholipase 1;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:P39105};
DE AltName: Full=CaPLB1;
DE AltName: Full=Phospholipase B 1;
DE Flags: Precursor;
GN Name=PLB1 {ECO:0000303|PubMed:9748287}; Synonyms=PLB;
GN OrderedLocusNames=CAALFM_C601990WA; ORFNames=CaO19.689;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=9748287; DOI=10.1074/jbc.273.40.26078;
RA Leidich S.D., Ibrahim A.S., Fu Y., Koul A., Jessup C., Vitullo J.,
RA Fonzi W., Mirbod F., Nakashima S., Nozawa Y., Ghannoum M.A.;
RT "Cloning and disruption of caPLB1, a phospholipase B gene involved in the
RT pathogenicity of Candida albicans.";
RL J. Biol. Chem. 273:26078-26086(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SS;
RX PubMed=9809417; DOI=10.1111/j.1574-6968.1998.tb13223.x;
RA Hoover C.I., Jantapour M.J., Newport G., Agabian N., Fisher S.J.;
RT "Cloning and regulated expression of the Candida albicans phospholipase B
RT (PLB1) gene.";
RL FEMS Microbiol. Lett. 167:163-169(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
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 [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/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 -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids
CC (By similarity). Phospholipase B may well contribute to pathogenicity
CC by abetting the fungus in damaging and traversing host cell membranes,
CC processes which likely increase the rapidity of disseminated infection
CC (PubMed:9748287). {ECO:0000250|UniProtKB:P39105,
CC ECO:0000269|PubMed:9748287}.
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:0000250|UniProtKB:P39105};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Expressed during candidal infection of mice.
CC {ECO:0000269|PubMed:9748287}.
CC -!- DISRUPTION PHENOTYPE: Reduces dramatically the ability to penetrate
CC host cells. {ECO:0000269|PubMed:9748287}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; U59710; AAC61890.1; -; Genomic_DNA.
DR EMBL; AF045558; AAC72296.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30135.1; -; Genomic_DNA.
DR RefSeq; XP_713822.1; XM_708729.2.
DR AlphaFoldDB; Q9UWF6; -.
DR SMR; Q9UWF6; -.
DR STRING; 237561.Q9UWF6; -.
DR GeneID; 3644561; -.
DR KEGG; cal:CAALFM_C601990WA; -.
DR CGD; CAL0000177213; PLB1.
DR VEuPathDB; FungiDB:C6_01990W_A; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q9UWF6; -.
DR OMA; EPLGENF; -.
DR OrthoDB; 564952at2759; -.
DR PHI-base; PHI:105; -.
DR PHI-base; PHI:7565; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
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; IDA:CGD.
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 GO; GO:0044001; P:migration in host; IMP:CGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..605
FT /note="Lysophospholipase 1"
FT /id="PRO_0000024630"
FT DOMAIN 30..565
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 471
FT /note="K -> N (in Ref. 2; AAC72296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 66417 MW; 2222F8342379F60C CRC64;
MILHHLLILL IINYCVATSP TNGYAPGPVS CPSSQLIRSG SQGINPNEQS YINARYPIAK
QALSKFLHNA NLQNFDVDSF LAHSNPTIGL AFSGGGYRAM LTGAGEISSL DSRTKTNTPV
LAGILQASSY IAGLSGGSWL VGSLASNNLN SVDDMLSQGL WELTHSFLSY YGIEHPIKQV
EEWVNVGNQV ASKRNANFNV SLTDIYGRLL SYPLLTNTED EGDAYLWSDV TSASNFQSHQ
MPFPILISDG RAPDTTIINL NSTVIELTPY EFGSWDPSLN EFVDTRYLGT KLDNGRPTGK
CYNGFDNAGF FMGTSSALFN EAVLSITEAN IPSFLKDIID DILVDPILKS NIDVSAYNPN
PFFKSSGSNT AISQSKNLYL VDGGEDGQNI PISPLLHRNV SAIFAFDNSN DVLNWPDGTS
LVKTYERQFS SQGNGIAFPY VPDQYTFRNL NLTSKPTFFG CDAKNLTSLT KDIYDVPLVI
YLANRPFTYW SNTSTFKLTY DDNERQGMIS NGFEIATRSS GSLDDEWAAC VGCAIIRREQ
ERQGIEQTEQ CKRCFENYCW DGTIYKGEPL GENFSDDGLT NSATEYNSNN VAGFNDGGTS
ILKKA
