PLB1_ASPFC
ID PLB1_ASPFC Reviewed; 633 AA.
AC B0Y665; Q4WPC0; Q6U820; Q9P8P5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Lysophospholipase 1;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B 1;
DE Flags: Precursor;
GN Name=plb1; ORFNames=AFUB_065820;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=15451105; DOI=10.1016/j.femsle.2004.08.019;
RA Shen D.-K., Noodeh A.D., Kazemi A., Grillot R., Robson G.D., Brugere J.-F.;
RT "Characterisation and expression of phospholipases B from the opportunistic
RT fungus Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 239:87-93(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [3]
RP PROTEIN SEQUENCE OF 89-100 AND 122-131, AND GPI-ANCHOR.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [4]
RP PROTEIN SEQUENCE OF 90-98, AND STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
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: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- INDUCTION: Induced by lecithin. {ECO:0000269|PubMed:15451105}.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AY376592; AAQ85122.1; -; mRNA.
DR EMBL; DS499598; EDP50250.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y665; -.
DR SMR; B0Y665; -.
DR Allergome; 8989; Asp f LPL1.
DR PRIDE; B0Y665; -.
DR EnsemblFungi; EDP50250; EDP50250; AFUB_065820.
DR VEuPathDB; FungiDB:AFUB_065820; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR PhylomeDB; B0Y665; -.
DR BRENDA; 3.1.1.5; 508.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein; Membrane;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..609
FT /note="Lysophospholipase 1"
FT /id="PRO_0000372611"
FT PROPEP 610..633
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372612"
FT DOMAIN 47..594
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT LIPID 609
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 68144 MW; 277A47E29FD74796 CRC64;
MKTTTVACAV AGLLFSCVSG APDPVHVEIQ QRALPNAPDG YTPSTVGCPA SRPTIRSAAS
LSPNETSWLE TRRGKTTSAM KDFFNHVKIQ DFDAAGYIDR HSSNSSDLPN IGIAVSGGGY
RALMNGAGAI KAFDSRTPNS TSAGQLGGLL QSATYLSGLS GGSWLVGSIY INNFTTISAL
QTHQKGTVWQ FQNSIFEGPD GGSIQILDSA TYYRDISNAV SGKSDAGYPT SITDYWGRAL
SYQMINATNG GPSYTWSSIA LTDAFQKAEM PMPLVVADGR YPGELLISSN ATVYEFNPWE
FGTFDPTVFG FAPLEYLGTK FNGGSVPSNE SCVRGFDNVG FVMGTSSTLF NQFLLQINST
ALPDWLKSVF TDILKDIGEN DEDIAQYAPN PFYHFSNTTN PSAAELELDL VDGGEDLQNI
PLHPLIQPER HVDVIFAVDS SADTTYSWPN GTALVATYER SLNSSGIANG TSFPAIPDQN
TFVNKGLNTR PTFFGCNSSN TTGPSPLIVY LPNYPYTAYS NFSTFQPDYT EQERDSTILN
GYDVVTMGNS TRDGNWSTCV GCAILSRSLE RTNTNVPEIC KQCFQRYCWD GSLNSTTPAG
YEPVTILDSA ASGIIPSIST VAMAVVFAAW TIF
