ID A0A2I3T410_PANTR Unreviewed; 1300 AA.
AC A0A2I3T410; A0A2J8J675;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Patatin like phospholipase domain containing 6 {ECO:0000313|Ensembl:ENSPTRP00000083950.1};
GN Name=PNPLA6 {ECO:0000313|Ensembl:ENSPTRP00000083950.1,
GN ECO:0000313|VGNC:VGNC:6648};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000083950.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000083950.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000083950.1}
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; AACZ04060065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000104962.1; ENSPTRP00000083950.1; ENSPTRG00000010393.6.
DR VGNC; VGNC:6648; PNPLA6.
DR GeneTree; ENSGT00940000159130; -.
DR Proteomes; UP000002277; Chromosome 19.
DR Bgee; ENSPTRG00000010393; Expressed in superior frontal gyrus and 21 other cell types or tissues.
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; 2.
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:UP000002277};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..274
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 474..542
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 570..675
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 906..1072
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 304..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 143397 MW; F02E239BB4CC69BA CRC64;
MEAPLQTGMV LGVMIGAGVA VVVTAVLILL VVRRLRVPKT PAPDGPRYRF RKRDKVLFYG
RKIMRKVSQS TSSLVDTSVS TTSRPRMRKK LKMLNIAKKI LRIQKETPTL QRKEPPPAVL
EADLTEGDLA NSHLPSEVLY MLKNVRVLGH FEKPLFLELC RHMVFQRLGQ GDYVFRPGQP
DASIYVVQDG LLELCLPGPD GKECVVKEVV PGDSVNSLLS ILDVITGHQH PQRTVSARAA
RDSTVLRLPV EAFSAVFTKY PESLVRVVQI IMVRLQRVTF LALHNYLGLT NELFSHEIQP
LRLFPSPGLP TRTSPVRGSK RMVSTSATDE PRETPGRPPD PTGAPLPGPT GDPVKPTSLE
TPSAPLLSRC VSMPGDISGL QGGPRSDFDM AYERGRISVS LQEEASGGSL AAPARTPTQE
PREQPAGACE YSYCEDESAT GGCPFGPYQG RQTSSIFEAA KQELAKLMRI EDVSLHFVLW
GCLHVYQRMI DKAEDVCLFV AQPGELVGQL AVLTGEPLIF TLRAQRDCTF LRISKSDFYE
IMRAQPSVVL SAAHTVAARM SPFVRQMDFA IDWTAVEAGR ALYRQGDRSD CTYIVLNGRL
RSVIQRGSGK KELVGEYGRG DLIGVVEALT RQPRATTVHA VRDTELAKLP EGTLGHIKRR
YPQVVTRLIH LLSQKILGNL QQLQGPFPGS GLGVPPHSEL TNPASNLATV AILPVCAEVP
MVAFTLELQH ALQAIGPTLL LNSDIIRARL GASALDSIQE FRLSGWLAQQ EDAHRIVLYQ
TDASLTPWTV RCLRQADCIL IVGLGDQEPT LGQLEQMLEN TAVRALKQLV LLHREEGAGP
TRTVEWLNMR SWCSGHLHLR CPRRLFSRRS PAKLHELYEK VFSRRADRHS DFSRLARVLT
GNTIALVLGG GGARGCSHIG VLKALEEAGV PVDLVGGTSI GSFIGALYAE ERSASRTKQR
AREWAKSMTS VLEPVLDLTY PVTSMFTGSA FNRSIHRVFQ DKQIEDLWLP YFNVTTDITA
SAMRVHKDGS LWRYVRASMT LSGYLPPLCD PKDGHLLMDG GYINNLPADI ARSMGAKTVI
AIDVGSQDET DLSTYGDSLS GWWLLWKRLN PWADKVKVPD MAEIQSRLAY VSCVRQLEVV
KSSSYCEYLR PPIDCFKTMD FGKFDQIYDV GYQYGKAVFG GWSRGNVIEK MLTDRRSTDL
NESRRADVLA FPSSGFTDLA EIVSRIEPPT SYVSDGCADG EESDCLTEYE EDAGPDCSRD
EGGSPEGASP STASEMEEEK SILRQRRCLP QELPGSATDA
//
