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Database: UniProt
Entry: T0KXA3_COLGC
LinkDB: T0KXA3_COLGC
Original site: T0KXA3_COLGC 
ID   T0KXA3_COLGC            Unreviewed;       783 AA.
AC   T0KXA3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, 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=CGLO_17240 {ECO:0000313|EMBL:EQB44051.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB44051.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB44051.1}.
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DR   EMBL; AMYD01004109; EQB44051.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KXA3; -.
DR   STRING; 1237896.T0KXA3; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_0_1; -.
DR   OMA; CSWFTRG; -.
DR   OrthoDB; 154387at2759; -.
DR   Proteomes; UP000015530; 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:UP000015530};
KW   Transmembrane {ECO:0000256|RuleBase:RU362055};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT   TRANSMEM        185..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362055"
FT   DOMAIN          383..574
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..775
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  88629 MW;  63D97C23A528F137 CRC64;
     MAEHTREQRE HHRVTFAPIS PSSSNNYNTD SYGFPPESFG SDGLPDFDTN FLDDADLEAF
     VNALHAPDPL QSPADETTSL RSPGLRSSSS LDITKRGSTY EDGNDDPSAV AAAAAAAAGD
     VTAPPQPNGN GHASQPNMFI TAQNDWAPVN QRVAKRGSRR RRNRAKGAAE ALLGTRTKDE
     TREGIFYALL KWPMLFFVGA WLAGLALTYL YTRLYIWVYE HFVTWRGTRE RLRRSMRRTN
     NYRDWVVAAK ELDSYLDRQR WKEENDFAYY DSKTVKRVWE QMRKCRHRAE AQENGEDDGE
     KGGKPAVEEL HALLSACVKS NFVGVENPRL YSQTYYGTKN LVQNFVDEVE RSIKFVLNTQ
     QLTMEEKRSI FKGMFNNYGR TALCLSGGAS FAYYHFGVVK SLLEADLLPE VITGTSGGAL
     VAALVATRTN DELKKLLVPA LAGKITACRE SFTTWIPRWW KTGARFDSVD WAKQCSWWTR
     GSMTFREAYE RTGRILNVSC VPADPHSPTI LCNYITSPDC VIWSAVLASA AVPGILNPVV
     LMMKQRDGTL IPYSFGHKWK DGSLRTDIPI KALNLHFNVN FTIVSQVNPH INLFFFSSRG
     SVGHPVTHRK GKGWRGGYVM SAVEHYLKLD MTKWLKFIRH AELLPRPLGQ DWSQLFLQQF
     SGTITIWPKT QPSDFYHILS DPDPPRLARM IHEGQQRGFP ILKFVSNRLK VEKVIEQGRR
     ETRPWIRRGS IETILSEDDL RSLLISGATD GEEDTTDAEG ETLLELEEEA IVDGDEDEKF
     ERR
//
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