ID   A0A078B146_STYLE        Unreviewed;       510 AA.
AC   A0A078B146;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Patatin {ECO:0000313|EMBL:CDW88051.1};
GN   Name=Contig18103.g19243 {ECO:0000313|EMBL:CDW88051.1};
GN   ORFNames=STYLEM_17166 {ECO:0000313|EMBL:CDW88051.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88051.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW88051.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW88051.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the patatin family.
CC       {ECO:0000256|ARBA:ARBA00010240}.
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DR   EMBL; CCKQ01016172; CDW88051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078B146; -.
DR   EnsemblProtists; CDW88051; CDW88051; STYLEM_17166.
DR   InParanoid; A0A078B146; -.
DR   OrthoDB; 5477952at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07199; Pat17_PNPLA8_PNPLA9_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR32176:SF92; PATATIN-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..510
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001729743"
FT   TRANSMEM        147..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..386
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   510 AA;  57521 MW;  5FC23853F03A7880 CRC64;
     MKINSVLSTA VAINLWLAIS SVNCQSAGSP NVQAAQNDEE IWNVLSLDGG GIRGIITATV
     VDYMEKYAYT YSSKYCLPKR ESKKVSMAEL FDMVSGTSTG SLLASSLVLP NPDKNSPQIN
     KFFASDALKI YTEFAPEVFQ KYQLPRIWRI VGSLGFAIVG GIIFFFVGLK LLTDTQFESA
     IKAFKEFAKV KKQNHDKTLD AQEIVMEATL FMNVSIKIKD IKNGEALKKQ ISEGDLDQIQ
     SAREEIRDHE AQYLERKGFK YLFLVLGFFF FGGIGYILMP KMHALTHSNY DRRGIEGLVT
     KLFGYVPIQD ALTPEVCIIA YEYNTHEPRI FSKFTAKTNP ETFNVSIGNA SEASSAAPLY
     FDPKVIGDQV LIDGGVIANN PSLYAYLHSR YANQKENIRF VSIGTGMTLP KPMKKEELTK
     VDWFMEIGNL LTTVEQLTHE YLMRKLSKEN YRFQALMDRD LALDSYSDEN IEELTSYGDK
     TILKYQSQIQ EAVNRVVDQK FSKKYSCSKP
//