ID A0A060X101_ONCMY Unreviewed; 1261 AA.
AC A0A060X101;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 7 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSONMT00037649001 {ECO:0000313|EMBL:CDQ71019.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ71019.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ71019.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ71019.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; FR904744; CDQ71019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060X101; -.
DR STRING; 8022.A0A060X101; -.
DR PaxDb; 8022-A0A060X101; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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 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; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF23; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 7; 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.
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:UP000193380};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..311
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 506..591
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 619..724
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 958..1124
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 141170 MW; D2C5A6E0738A2112 CRC64;
MDDKVDDKDE DSCSIYPSLV PLGSEIKARM QHWMEDRTET AMPLPLWTGV LVVAVLTVLA
VSLIGMVVFL FYRRYKQYKE QQPHYRFRKR DKVMFYGRKI MRKVQTLSST STPTSTSESQ
KQRIRKRTKV LSIARKILRI RREPPTLVAK EPPPSLLEAD LTEFDVQNSH LPSEVLYMLK
NVRVLGHFEK PLFLELCRHM VFVQLHEMET LFRPGDIDDS IYVVQDGRLE LCIRESDGTD
VVVKEVFPGD SVHSLLSILD VITGHSAPYK TVSARAATPS TILRLPAAAF HSVFEKYPET
LVRVIQIIMV RLQRVTFLAL HNYLGLTTEL FNAERQAVPL VAVHSVIGEA NPNRGRDRHQ
SRSDESGHEK GPSDTEIGER KSCLSNSSPT TKGKRSRSQS TPLAVSSATS ADLNMAYQRA
RITEEAAKAD TPPPSPQVPH KSILKKSVTM VHTPSAVFHY SEAGGGQSGH IHHSKVNAIF
QAAKKDLQRL IQLQDPSLLE GRVTLRQVKA GCVLNSQGDQ DASVQFVISG ALHVYQRTID
REEDTLLFLT HPGEMVGHLA VLTGEPLIFS VRAHRDCTFL SISKAAFYEI MREEPRVVLN
VAHTVVKRVS GFVRQIDFAL DWMAVEAGRT VYRQGDKSDS TFIVLSGRLR SVIAKDDGKK
ELAGEYGRGD LIGVVEALTH MNRATTVHAI RDSELAKLPE GALSSIKRRY PQVVTRLIHL
LGQKILGNMQ QVHGPLAARG LTLQPPSSKW DSGSPASNLS TVTILPVSEE VPLTAFTLEL
QHALSAIGPT LLLTSDIIKQ RLGAAALDSV HEYRLSSWLG QQEDIHRIVL YQSDDTLTPW
TQRCIRQADC IIIVGLGEAE PTVGELERML EGSAVRAQKQ LILLHREDGP PPQGTVEWLN
MRSWISRHLH LSCPHRVFSK RSLPKLREMY QRVFQKPPDR HSDFSRLARV LTGNTIALVL
GGGGARGCCQ VGILRALNEA GIPVDMVGGT SIGSLMGALY AEEKSNSRMR VRAREWAMDM
RSIFKKVFDL TYPVTSMFSG ASFNNSVSAV FKGKQIEDLW IPYFNITTDI TASSMRVHTD
GSLWRYVRAS MSLSGYLPPL CDPKDGHLLM DGGYINNLPA DVARSMGAKV VIAIDVGSQD
ETNLTNYGDS LSGWWLLWKR FNPLAKKVQV LNMAEIQTRL AYVCCVRQLE LVKDSEYCEY
IRPPIDHYGT LEFGKFDEIA EVGYQHCKTV FDMWSRSGVV DKMMKDRHQE EFHNTKSGNV
R
//
