PLPL_EMENI
ID PLPL_EMENI Reviewed; 749 AA.
AC Q5BGC2; C8VTH8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Patatin-like phospholipase domain-containing protein AN0408;
DE EC=3.1.1.-;
GN ORFNames=AN0408;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000007; EAA66507.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89546.1; -; Genomic_DNA.
DR RefSeq; XP_658012.1; XM_652920.1.
DR AlphaFoldDB; Q5BGC2; -.
DR STRING; 162425.CADANIAP00002291; -.
DR EnsemblFungi; CBF89546; CBF89546; ANIA_00408.
DR EnsemblFungi; EAA66507; EAA66507; AN0408.2.
DR GeneID; 2876185; -.
DR KEGG; ani:AN0408.2; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_2_0_1; -.
DR InParanoid; Q5BGC2; -.
DR OMA; DMNKWLR; -.
DR OrthoDB; 425613at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
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 InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 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..749
FT /note="Patatin-like phospholipase domain-containing protein
FT AN0408"
FT /id="PRO_0000295559"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 280..471
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 311..315
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 749 AA; 85251 MW; C85DEBBB00EA5B71 CRC64;
MEKSAAGDNI DKYSPSSIPD YDTEFLNPDD LRAFEKALTD QDADPLVALN DWRPVYQRVV
RRGRGRRKSA AAAPRRTKDE TREGVLYTVL KWPFLLFVLG WITFLSVGYA LTRIYIFLYE
QWVTWRGKRE SLRRELYKHE NYDDWLHAAQ ALDEYLGNQR WKKIDEYAYY DHLTIRKLGR
QLRTVRMQVE EEMKRGESGS TVVVEELCNL LEACVKANFA GVENPRLYSE AYSGTKDLVQ
DYIDEVHACV KVITDSRQAR NEEKYSHFKH LDTNFGRTAL CLSGGATFAY YHFGVVRALL
DNEVLPSIIT GTSGGALVAA LVGTRTDDEL KQLLVPALAH KIKACSEGFT TWARRWWRTG
ARFDTMDWAR QCSWFCRGST TFREAYERTG RILNVSCVPS DPHSPTILAN YLTSPNCVIW
SAVLASAAVP GILNPVVLMT KKRDGTLAPY SFGHKWKDGS LRTDIPIKAL NLHFNVNFTI
VSQVNPHINL FFFSSRGAVG RPVTHRKGRG WRGGFLGSAI EQYIKLDLNK WLKVLRHLEL
LPRPLGQDWS EIWLQKFSGT VTIWPKTVPS DFYHILSDPS PERLARMLRT GQQSTFPKIQ
FIKNRLKIEY AILEGLHRFS ADGESVGATS IQPFPFDNGA AGADQKSNDP REERLNRNFP
ERSSEYSYDY VKSFSDFSDD PIVSAENSSV DDNYIVPSRQ RDAGAEAGVG TGTAERRGSF
SSLFNLEEMR RQSAVFFDDP DLYRDGGDL
