ID   PLPL_ASPCL              Reviewed;         712 AA.
AC   A1CRG6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein ACLA_029670;
DE            EC=3.1.1.-;
GN   ORFNames=ACLA_029670;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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).
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
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DR   EMBL; DS027059; EAW08237.1; -; Genomic_DNA.
DR   RefSeq; XP_001269663.1; XM_001269662.1.
DR   AlphaFoldDB; A1CRG6; -.
DR   STRING; 344612.A1CRG6; -.
DR   EnsemblFungi; EAW08237; EAW08237; ACLA_029670.
DR   GeneID; 4700957; -.
DR   KEGG; act:ACLA_029670; -.
DR   VEuPathDB; FungiDB:ACLA_029670; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   OMA; CSWFTRG; -.
DR   OrthoDB; 154387at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:EnsemblFungi.
DR   GO; GO:1990748; P:cellular detoxification; IEA:EnsemblFungi.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006642; P:triglyceride mobilization; IEA:EnsemblFungi.
DR   CDD; cd07232; Pat_PLPL; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF66; TRIACYLGLYCEROL LIPASE PTL2; 1.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..712
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   ACLA_029670"
FT                   /id="PRO_0000295549"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          275..466
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           306..310
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        649..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        453
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   712 AA;  81401 MW;  2FA3CE0EA03AC030 CRC64;
     MTSAEKSATR NIYDPSALPD YDTQFIKPDE LHQFEKALNA PAAAPLVAIN DWRPINQRVR
     KNRRTKPRRS KDETREGVLY TVLKWPFLFI VFAWITVLGI AYALTRLYIF LYEQCVTWRG
     KRERLRRELS VQTNYRDWLT AAQALDTHLG NQKWKETDEY AYYDHLTINK VVAQLKQARK
     AAESEVHNGR SGVSDLPAVE DLCALLEACV KNNFAGVENP RLYSESYSGT KDLVQEYIDE
     VQACMQLILD SKQIPAEEKY QHFKHLDTNF GRTALCLSGG ATFAYYHFGV IRALLDNDVL
     PEIITGTSGG ALVAALVATR TDEELKQLLV PALAYRIRAC HEGFTTWVWR WWRTGARFDT
     VDWARQCSWF CRGSTTFREA YERTGRILNV SCVPSDPHSP TILANYLTSP DCVIWSAVLA
     SAAVPGILNP VVLMTKKRDG TLAPYSFGHK WKDGSLRTDI PIKALNLHFN VNFTIVSQVN
     PHINLFFFSS RGTVGRPVTH RKGRGWRGGF LGSAIEQYIK LDMNKWLRVL RHLELLPRPL
     GQDWSEIWLQ KFSGTITIWP KSIPSDFYHI LSDPSPERLA RMLHVGKQSA FPKIQFIKNR
     LKIENTIMQG LQQSSPGGDR VLLPILSRRL QNRAQEHADA MVERLDHSFP ERHSDYKDES
     HYTEVSDSLS TNSSRPHTPD ARRGSIFEEM RRQSAVFFDD PDMYGDEDAI AT
//