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Database: UniProt
Entry: PLPL_CHAGB
LinkDB: PLPL_CHAGB
Original site: PLPL_CHAGB 
ID   PLPL_CHAGB              Reviewed;         854 AA.
AC   Q2HA54;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein CHGG_02900;
DE            EC=3.1.1.-;
GN   ORFNames=CHGG_02900;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ90965.1; -; Genomic_DNA.
DR   RefSeq; XP_001229416.1; XM_001229415.1.
DR   AlphaFoldDB; Q2HA54; -.
DR   STRING; 306901.Q2HA54; -.
DR   GeneID; 4389131; -.
DR   VEuPathDB; FungiDB:CHGG_02900; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_0_1; -.
DR   InParanoid; Q2HA54; -.
DR   OMA; CSWFTRG; -.
DR   OrthoDB; 154387at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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-KW.
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; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..854
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   CHGG_02900"
FT                   /id="PRO_0000295555"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          387..578
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           418..422
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        70..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        420
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        565
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   854 AA;  94412 MW;  76D312484F5C204A CRC64;
     MAGPGYDRVD SKDDEPPNIQ IPSRTYGFPP EAFDWSRLPD FDTNFLPPEH VEAFIQALSA
     PDPIPPTPDG GATGSSSYRL NSPAWHRGST TSFDLDLARR PESSGVGFHD EDRTARDSPA
     GAATAAAAGV ATPGPPLSRR ASSNSLFISA RNDWAPISQR RVARAKTAPQ SSSRNDKKKK
     RARSKDETRE GYLYPLLKWP LLGVVTCWLV GLSVVHVLAR LYITVYERYW AWRGERGRLR
     RAMRATARYS DWVAAARRMD DFLGNDSWKV DDAFAYYDNK TVRRVLAEMR RSRRRAEEAG
     GRDTEQGREA IEDLKVLIEA CVKNNFAGIE NPRLYSQTYY GTKNLVQNFI DEVERSLKFL
     VETERLSKEE KRVMFKGICA NYGRTALCLS GGATFAYYHF GVVKALLEED YLPDIITGTS
     GGALVAALVA TRTNEELKEL LIPALACRIT ACREPISVWF RRWWATGARF DSVDWARQCA
     WWTRGSLTFR EAYERTGRIL NVSCVPADQH SPTILCNYLT SPDCVIWSAV LASAAVPGIL
     NPVVLLMKTR SGQLLPYSFG HKWKDGSLRT DIPIKALNLQ FNVNFTIVSQ VNPHINLFFF
     SSRGSVGQPV THRRGRGWRG GYLGTVLVQF TKLDLTKWLR VLRSLELLPR PLGQDWSLLW
     LQDFGGTVTV WPRCLLSDFA RILSDPDPAR LARMIHEGQQ SAFPKLRFVA NRLRVERLVE
     RGRRENRRGG GLGDGGVGSS GGAGGGAGGG QAEAVAGQAA GPGTGQRRPS FESILSEDDL
     RSLLKKRRVE RGGIGSGETE SEDETSDLDA DFYEGITYDG GDDDAGLEFG AAGMRQPGVA
     TPAGLGGVER GDLS
//
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