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 13-SEP-2023, entry version 54. 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 Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya OS fumigata). 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=CBS 144.89 / FGSC A1163 / CEA10; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; B0Y665; 18 sites, No reported glycans. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of 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:SF62; LYSOPHOSPHOLIPASE; 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 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 //