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Database: UniProt
Entry: W5MQC5_LEPOC
LinkDB: W5MQC5_LEPOC
Original site: W5MQC5_LEPOC 
ID   W5MQC5_LEPOC            Unreviewed;      1389 AA.
AC   W5MQC5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Neuropathy target esterase-like {ECO:0000313|Ensembl:ENSLOCP00000010584.1};
GN   Name=PNPLA6 {ECO:0000313|Ensembl:ENSLOCP00000010584.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010584.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000010584.1}
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; AHAT01007547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01007548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015204592.1; XM_015349106.1.
DR   RefSeq; XP_015204593.1; XM_015349107.1.
DR   STRING; 7918.ENSLOCP00000010584; -.
DR   Ensembl; ENSLOCT00000010599.1; ENSLOCP00000010584.1; ENSLOCG00000008681.1.
DR   GeneID; 102698342; -.
DR   KEGG; loc:102698342; -.
DR   CTD; 10908; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   GeneTree; ENSGT00940000159130; -.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   InParanoid; W5MQC5; -.
DR   OMA; CIEDLWI; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000018468; Linkage group LG6.
DR   Bgee; ENSLOCG00000008681; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
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; 2.
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; 2.
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:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..294
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          499..581
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          609..714
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          948..1114
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          411..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1326..1389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1351
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1366..1381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1389 AA;  155395 MW;  EB3854E033E27BDC CRC64;
     MGQSNSEPDT DSSDDGLMNI KTFVEDQLQT SMMVGIVIGA GISIILIAIL IFFVLRRVQL
     RKLQAQEAPK YRFRKRDKVM FYGRKIMRKV SQSTSSLVGT TASRPRLKKK QKMLNIAKKI
     LRFKKEMPTL QMKEPPPSVL EADLTEFDVA NSHLPSEVLY MLKNVRVLGH FEKPLFLELC
     KHMVFLQFQQ GEYVFRPGQP DSSIYVVQDG KLELCLTGQD GKDGVVKEVY PGDSVHSLLS
     ILDVITGHQK PYRTVSARAA EMSTVLRLPV EAFLSIFEKY PESLVRVVQI IMVRLQRVTV
     LALHNYLGLT NELFSHEMQP LRLLPQASHP SRTSPVRHSK RFISTSICED HRDSTAKSGE
     LAGGDHVRDG ATVPTLSRAI SMPVDIAGIQ KGLRSDFDMA YERGRISVSL QEDGTASATP
     TFSRSVSQEP RERKSVTVEE QPSGVYLYPE EDVLDSLYGP LHGKHANNLF EEAKNEVLKL
     MRIEDAALLN GRITLHHAKA GSVLARQGDQ DVSLHFVLSG CLHVYQRMID KLEDVCLFIT
     QPGEMVGQLA VLTGEPLIFT IKAVRDCTFL KISKSDFYEI MREQPSVVLS AAHTVAVRMS
     AFVRQMDFAI DWMAVEAGRA LYRQGDQSDC TYIVLNGRLR SVIRKANGKK ELVGEYGRGD
     LIGVVEALTR QPRATTVHAV RDTELVKLPE GTLNNIKRRY PQVVTRLIHL LGQKILGNLQ
     QVRGPLSGSA LGLSAVGTSH DVTNPASNLS TVAVLPICDD VPVNAFNLEL SHALNAIGPT
     LLLTSDIIRE RLGASALDSI HEYRLSGWLA QQEDINRIVL YQTDSTMTPW TQRCIRQADC
     ILIIGLGDQE PTLGELEQML ENTAVRALKQ LVLLHKEDGP GPARTVEWLN MRSWCSGHLH
     LKCPRRVFSR RSPTRLREMY EKVFEKTVDR YSDFSRLARV LTGNSIALVL GGGGARGCSH
     VGVIKAMEEA GIPIDIVGGT SIGSFIGALY AEERSAVRTK QRAREWSKSM NSVFKTVLDL
     TYPITSMFSG SAFNTSISKV FEDKQIEDLW LPYFNVTTDI TASAMRVHKD GCVWRYVRAS
     ASYTPYLPPL CDPKDGHLLV DGCYVNNVPG SLWRYVRASM TLSGYLPPLC DPKDGNLLMD
     GGYINNLPAD MARNMGAKTV IAIDVGSQDE TDLCNYGDCL SGWWLLWKRI NPWAEKVKVP
     DMAEIQSRLA YVSCVRQLEV VKNSAYCEYI RPPIDRFKTM DFGKFDEIYD VGYQHGKVVF
     NAWSRGDIID NMLKDRRSAD FNESKKADIC PGADFTDLAE IVSRIEPVHS YVSAEAEESD
     CLTEYEDDGM DTVREEEGEE EEEEPEEQDD QSPGEWGQNG VFEVDELKSV RNRRKKTSDS
     NTCSEISDS
//
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