PLB3_ASPFC
ID PLB3_ASPFC Reviewed; 630 AA.
AC B0XZV8; Q4WYY4; Q6U819;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Lysophospholipase 3;
DE EC=3.1.1.5;
DE AltName: Full=Phospholipase B 3;
DE Flags: Precursor;
GN Name=plb3; ORFNames=AFUB_034540;
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 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: Strongly induced by lecithin. {ECO:0000269|PubMed:15451105}.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AY376593; AAQ85123.1; -; mRNA.
DR EMBL; DS499596; EDP52290.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XZV8; -.
DR SMR; B0XZV8; -.
DR Allergome; 8988; Asp f LPL3.
DR EnsemblFungi; EDP52290; EDP52290; AFUB_034540.
DR VEuPathDB; FungiDB:AFUB_034540; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR PhylomeDB; B0XZV8; -.
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; Glycoprotein; GPI-anchor; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..606
FT /note="Lysophospholipase 3"
FT /id="PRO_0000372613"
FT PROPEP 607..630
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372614"
FT DOMAIN 39..587
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT LIPID 606
FT /note="GPI-like-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 70
FT /note="Q -> E (in Ref. 1; AAQ85123)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="N -> D (in Ref. 1; AAQ85123)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="G -> S (in Ref. 1; AAQ85123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 67417 MW; 0E83E7D7F149CA08 CRC64;
MKALLSLLTA VAVATATPLD LSLRALPNAP DGYTPAKVSC PATRPSIRGA GSLSPNETSW
LEIRRKNTVQ PMTDLLGRLN LGFDAAGYID RVSSNASNLP NIAIAVSGGG YRALTNGAGA
IKAFDSRTQG STQSGHLGGL LQSATYVSGL SGGGWLVGSV YLNNFTTIAD LQSGDHGNVW
QFSTSILEGP KAKHLQFLST ADYWKDLLKA VDGKSDAGFN TSLTDYWGRA LSYQFINDRT
GNGGLSYTWS SIALTDPFRR GEMPLPILVA DGRNPGELLI GSNSTVYEFN PWEFGSFDPS
IFGFAPLEYL GSRFDNGQLP RGEPCVRGFD NAGFVMGTSS SLFNQFILRL NKTDLPDLAK
DVFSKILTAI GRDGDDIAVY GPNPFYGYRN STAAYSRSRE LDVVDGGEDG QNIPLHPLIQ
PVRHVDVIFA VDSSADGPYS WPNGSALVAT YERSLNSSGI GNGTVFPAVP DVNTFVNLGL
NTRPTFFGCD PANLSAPAPL VVYLPNAPYS THSNTSTFQL AYSDSERDEI ITNGYNVVTR
GNATVDKSWP SCVGCAILQR SMYRTNTSMP AVCNSCFKEY CWNGTVDSKT PRTYEPTLLL
GSTSTNAAYT QGVTWLVGIL AVGVAMGMTA
