ID I1RRC7_GIBZE Unreviewed; 767 AA.
AC I1RRC7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN Name=FG06645.1 {ECO:0000313|EnsemblFungi:CEF84193};
GN ORFNames=FGRAMPH1_01T22815 {ECO:0000313|EMBL:CEF84193.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF84193.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF84193, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF84193};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF84193, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF84193};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PH-1;
RA King R., Urban M., Hassani-Pak K., Hammond-Kosack K.;
RT "A revised Fusarium graminearum genomic reference sequence using whole
RT shotgun re-sequencing.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEF84193.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF84193.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [5] {ECO:0000313|EnsemblFungi:CEF84193}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF84193};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
CC -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362055}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362055}.
CC -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000256|ARBA:ARBA00006104,
CC ECO:0000256|RuleBase:RU362055}.
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; HG970335; CEF84193.1; -; Genomic_DNA.
DR RefSeq; XP_011326269.1; XM_011327967.1.
DR AlphaFoldDB; I1RRC7; -.
DR STRING; 229533.I1RRC7; -.
DR EnsemblFungi; CEF84193; CEF84193; FGRRES_06645.
DR GeneID; 23553769; -.
DR KEGG; fgr:FGSG_06645; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G22815; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_2_0_1; -.
DR InParanoid; I1RRC7; -.
DR OrthoDB; 154387at2759; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362055};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362055};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362055}; Membrane {ECO:0000256|RuleBase:RU362055};
KW Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW Transmembrane {ECO:0000256|RuleBase:RU362055};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT TRANSMEM 170..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362055"
FT DOMAIN 359..550
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 46..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 87125 MW; 20173C63CB686CB5 CRC64;
MSSSSYSSLL PRDPVYGFPP EAFDTSLLPD VDTEFVSAQD LEAFEKALQA PDPLQSPTDE
TGARSPRSPS SFSVTKRPSQ VESGFADDVA AVAAAADATS GGLPQPLSQG TFITAQNDWA
PVNEKVYRHR RGSKRNKRKR RNGKGAVEGL LGTRTKDETR EGYLYQLSKW PLLIFVFAWL
GGLAAMYMST RLYIWVYEHF FTWRGQRERL RRNLRNASKY EDWVSAAKEL DTYLGRQTWR
EENDFAYYDS KTARRVWEQM KKTRLRAEEQ ENKSEKDDGG KAVGELKALI EACVKNNFVG
IENARLYSQT YFGTKNLVQN FLDEEEKCIK FLASTKQLDM EQKRILFKHV YANYGRTALC
LSGGAAFAYY HIGVVRALLD ANLLPDVITG TSGGALVAAL VATRTNEELD QLLVPALSER
INACRESITT WFPRWWRTGA RFDSVDWARR CGWWTYGSLT FKEAFERTGR ILNVTCVPAD
PHSPTILCNY LTSPDCVIWS AVLASAAVPG ILNPVVLMMK TRDGSLEPYS FGHKWKDGSL
RTDIPIKALN THFNVNFTIV SQVNPHINLF FFSSRGSVGH PVTHRKGRGW RGGYLMSAFE
HYLKLDMNKW LKFIRHAELL PRPLGQDWSQ LWLQQFSGTI TIWPKSRVSD FWHILNDPDP
HRLSHMIHEG KQSAFPKLKF IENRLKIERL VERGRTDSRP WVRRGSIQTI LSEEDLRSIL
VEEMENSVTE EETDGDDLSA LGLGMTVADG DVLYEEPKEK SDSEGTD
//