ID W9Y5Q3_9EURO Unreviewed; 721 AA.
AC W9Y5Q3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN ORFNames=A1O1_05090 {ECO:0000313|EMBL:EXJ88162.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ88162.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ88162.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ88162.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ88162.1}.
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DR EMBL; AMWN01000004; EXJ88162.1; -; Genomic_DNA.
DR RefSeq; XP_007724168.1; XM_007725978.1.
DR AlphaFoldDB; W9Y5Q3; -.
DR STRING; 1182541.W9Y5Q3; -.
DR GeneID; 19159967; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_2_2_1; -.
DR OrthoDB; 154387at2759; -.
DR Proteomes; UP000019484; 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-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:UP000019484};
KW Transmembrane {ECO:0000256|RuleBase:RU362055};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT TRANSMEM 86..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362055"
FT DOMAIN 283..474
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..712
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 81774 MW; B00D6331C9F60663 CRC64;
MITNGTKHES TPPAGDRSYD PSNLPDYETD FISQADLDSF AQALSAPTTE PLTALNDWGP
VHQKVKKTRA RRKSPRRSKD ETREGFVYTL LYYPLLFVVC GWIVVLFVIY NLTRFYIYAY
EHAFSWTGRR ETLRRRLQQA NTYEEWQAAA HELDEYLGNE RWKHSDPYSY YNHQTVRKVT
AQLAELHGKI QAEEVEKRDG VKGLTALDEL KSLLESCVKN NFVGIENPRL YSETYIGTKD
LIQSFLDQVE ECLTTVLRSN QMTDSDKVAF FRHLELNYGR TALCLSGGAT FAFYHFGVVK
ALLETGQLPE IITGTSGGAL VAALVATRTD EELKQLLVPA LAYRIRACHE GITTWMLRWW
RTGARFDSID WALQCSWFCR GSLTFREAYE RTGRILNVSC VPSDPHSPTI LNNHITSPDC
VIWSAVLASA AVPGILNPVV LMRKTKDGTL VPYSFGNKWK DGSLRTDIPL KALNLHFNVN
FSIVSQVNPH INLFFFSPRG EPGRPVTHRK GRGWRGGFLG STIETSVKLD LQKYLKILRH
LELLPRPLGQ DWSEIWLQRF SGTVTIWPKT ILSDFWNILN DPSPQRLERM IKAGERSCWP
KIKFISNRLK VERVILEGLR KGGPIDDSHR VPNPVQEQQA QEALLRARRR PNDSISSADE
AQAPPPSPRR HSSIFQELGR QASVLWSDDG PTDGEEDAVS TTTEEDEGDT AMDGDGVTTR
L
//
