PLB1_ASPFU
ID PLB1_ASPFU Reviewed; 633 AA.
AC P0C957; Q4WPC0; Q6U820; Q9P8P5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Lysophospholipase 1;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B 1;
DE Flags: Precursor;
GN Name=plb1; ORFNames=AFUA_4G08720;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-498 AND 590-ASN--VAL-593,
RP AND INDUCTION.
RC STRAIN=ATCC 90240 / AF-10;
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=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- INDUCTION: Induced by lecithin. {ECO:0000269|PubMed:15451105}.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AF223004; AAF64038.2; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89914.1; -; Genomic_DNA.
DR RefSeq; XP_751952.1; XM_746859.1.
DR AlphaFoldDB; P0C957; -.
DR SMR; P0C957; -.
DR STRING; 746128.CADAFUBP00006407; -.
DR Allergome; 8989; Asp f LPL1.
DR EnsemblFungi; EAL89914; EAL89914; AFUA_4G08720.
DR GeneID; 3509318; -.
DR KEGG; afm:AFUA_4G08720; -.
DR VEuPathDB; FungiDB:Afu4g08720; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; P0C957; -.
DR OMA; FGTWDPT; -.
DR OrthoDB; 564952at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..609
FT /note="Lysophospholipase 1"
FT /id="PRO_0000245555"
FT PROPEP 610..633
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245556"
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"
FT VARIANT 498
FT /note="S -> N (in strain: ATCC 90240 / AF-10)"
FT /evidence="ECO:0000269|PubMed:15451105"
FT VARIANT 590..593
FT /note="DGSL -> NGTV (in strain: ATCC 90240 / AF-10)"
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
