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Database: UniProt
Entry: H0XES9_OTOGA
LinkDB: H0XES9_OTOGA
Original site: H0XES9_OTOGA 
ID   H0XES9_OTOGA            Unreviewed;      1375 AA.
AC   H0XES9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Patatin like phospholipase domain containing 6 {ECO:0000313|Ensembl:ENSOGAP00000014469.2};
GN   Name=PNPLA6 {ECO:0000313|Ensembl:ENSOGAP00000014469.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000014469.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000014469.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC         octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC         Evidence={ECO:0000256|ARBA:ARBA00024569};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC         Evidence={ECO:0000256|ARBA:ARBA00024569};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC         Evidence={ECO:0000256|ARBA:ARBA00000355};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC         Evidence={ECO:0000256|ARBA:ARBA00000355};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000256|ARBA:ARBA00000150};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein
CC       {ECO:0000256|ARBA:ARBA00004643}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004183}; Single-pass type III membrane protein
CC       {ECO:0000256|ARBA:ARBA00004183}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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DR   EMBL; AAQR03185630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03185631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03185632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03185633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03185634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 30611.ENSOGAP00000014469; -.
DR   Ensembl; ENSOGAT00000016165.2; ENSOGAP00000014469.2; ENSOGAG00000016150.2.
DR   eggNOG; KOG2968; Eukaryota.
DR   GeneTree; ENSGT00940000159130; -.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   InParanoid; H0XES9; -.
DR   OMA; CIEDLWI; -.
DR   TreeFam; TF300519; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 3.
DR   CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF26; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 6; 1.
DR   Pfam; PF00027; cNMP_binding; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 3.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 3.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 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:UP000005225};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          195..322
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          511..616
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          644..749
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          981..1147
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  151117 MW;  D4ED3B3E4192F5D1 CRC64;
     MEAPLQTGVS RAPGEGAAPN SSGVKVTEKD GPRDVLAPGE GSAGRICGAQ PVPFVPQVLG
     VMIGAGLAVL VTAVLILLVV RRLRVPKTPA PDGPRYRFRK RDKVLFYGRK IMRKVSQSTS
     SLVDASVSTT SRPRMKKKLK MLNIAKKILR IQKETPTLQR KEPPPAVLEA DLTEGDLANS
     HLPSEVLYML KNVRVLGHFE KPLFLELCRH MVFQRLSQGD YVFRPGQPDA SIYVVQDGLL
     ELCLPGPDGK ECVVKEVVPG DSVNSLLSIL DVITGHQHPQ RTVSARAARD STVLRLPVEA
     FSAVFTKYPE SLVRVVQIIM VRLQRVTFLA LHNYLGLTNE LFSHEIQPLR LFPSPGLPSR
     TSPVRGSKRV VSTSATEEPR ETPGRPPEPT GAPLPGPTGD PVKPMSLEAP SAPLLSRCIS
     MPVDISGLQG GPRSDFDMAY ERGRISMSLQ EEASGGPQAA TARTPTQETR EQPAGACEYS
     YCEDESATGG CPFGPYQGRQ TSSIFEAAKR ELAKLMRIED PSLLNSRVLL HHAKAGTIIA
     RQGDQDVSLH FVLWGCLHVY QRMIDKAEDV CLFVAQPGEL VGQLAVLTGE PLIFTLRAQR
     DCTFLRISKS DFYEIMRAQP SVVLSAAHTV AARMSPFVRQ MDFAIDWTAV EAGRALYRQG
     DRSDCTYIVL NGRLRSVIQR GTGKKELVGE YGRGDLIGVV EALTRQPRAT TVHAVRDTEL
     AKLPEGTLGH IKRRYPQVVT RLIHLLSQKI LGNLQQLQGP FPAGSGLGVP PHSELTNPAS
     NLATVAVLPV CAEVPMVAFT LELQHALQAI GPTLLLNSDI IRARLGASAL DSIQEFRLSG
     WLAQQEDAHR IVLYQTDASL TPWTVRCLRQ ADCILIVGLG DQEPTLGQLE QMLENTAVRA
     LKQLVLLHRE EGPGPTRTVE WLNMRSWCSG HLHLRCPRRL FSRRSPAKLH ELYEKVFSRR
     ADRHSDFSRL ARVLTGNTIA LVLGGGGARG CSHIGVVKAL EEAGVPVDLV GGTSIGSFIG
     ALYAEERSAS RTKQRAREWA KSMTSVMEPV LDLTYPVTSM FTGSAFNRSI HRVFQDKQIE
     DLWLPYFNVT TDITASAMRV HKDGSLWRYV RASMTLSGYL PPLCDPKDGH LLMDGGYINN
     LPADIARSMG AKTVLAIDVG SQDETDLSTY GDSLSGWWLL WKRLNPWADK VKVPDMAEIQ
     SRLAYVSCVR QLEVVKSSSY CEYLRPPIDC FKTMDFGKFD QIYDVGYQYG KAVFGGWSRG
     DVIEKMLTDR RSADLNESRR ADVLAFPTSG FTDLAEIVSR IEPPTSYVSD GCADGEESDC
     LTEYEEDAGP DCSRDEGGSP EGASPSTASE MEEEKAILRQ RRCVPQDLPS SISDT
//
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