ID A0A0G4ET38_VITBC Unreviewed; 655 AA.
AC A0A0G4ET38;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN ORFNames=Vbra_13216 {ECO:0000313|EMBL:CEM01586.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM01586.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM01586.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PLPL family.
CC {ECO:0000256|ARBA:ARBA00006104}.
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DR EMBL; CDMY01000305; CEM01586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4ET38; -.
DR STRING; 1169540.A0A0G4ET38; -.
DR VEuPathDB; CryptoDB:Vbra_13216; -.
DR InParanoid; A0A0G4ET38; -.
DR OMA; CSWFTRG; -.
DR OrthoDB; 154387at2759; -.
DR PhylomeDB; A0A0G4ET38; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
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};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..396
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 568..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73795 MW; 39ACBF8BCEC9D2E0 CRC64;
MASVCRFARE VIVGALTGWP STQELLRWPL FFLFGFSALV ELAIYIVVRN AVRFIENLSQ
SSRVRRIREA LRGARSYEEY AKRARELDLV YKCEDWKREK QSEYYDCHLL ERRLSQLRKM
RRESNIEGIL QVLKLCIHTG FAGIFNETLY SQSYTGTKHL IETFIREVCE ALEYLRANAH
LYAPQLTRFI SACNSTWGTT ALCLSGGGMN CMHHFGVARS LLDHGLLPQV ISGASGGAVV
ASFLCTRTDD ELRAQLVPEY IQPRFQCMSP ASWFMRFWNM MTVGYMFDAE QWNNTMEILS
MGLTFEEAYR RTGRVLNVAV SRRADHSPPT VLNYLNAPHV LISSAVIASS AMPFLVQPQI
LKEKGPDGKL RSYAAYDTQF MCDGSVDADI PANALSEMWG VQWIITVQVN LHVFPWQAFR
NRGSAGAPLT WRHGGGKWRG GFVLSAFEVL LKEHMRLCIR LMALLDVFPH FFDINWGRVF
LQDYQGSSNV IMTPRRLFLN HFLLIGKDLT LPEVKWYMSE GLLMVWPKIP MITSRMRIEK
ALTGIELALN PNALFVQYGL STDITDESES RAANMDRTHG SGSSSRNNAY NAYNGSDDST
GAFDAAAGAS DGAEKNGGPS IVASGQHRKK DSREGGQRER AHTHTHSEMP NGPVG
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