ID A0A2U9BUX6_SCOMX Unreviewed; 1280 AA.
AC A0A2U9BUX6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative patatin-like phospholipase domain-containing protein 7 {ECO:0000313|EMBL:AWP07042.1};
GN ORFNames=SMAX5B_022052 {ECO:0000313|EMBL:AWP07042.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP07042.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP07042.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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; CP026251; AWP07042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BUX6; -.
DR Proteomes; UP000246464; Chromosome 9.
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; 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; 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:UP000246464};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..301
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 479..583
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 611..716
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 950..1116
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 1280 AA; 143089 MW; E83817E7EF9A3648 CRC64;
MEDDNEEESC IIPSLVPLGS EIGARIKQMV EERTEVNMWT AVLIGSVTVM SVIGVVVFLL
YRRYKRSKDE AGGTHYRFRK RDKVMFYGRK IMRKVKTLSS APASNTSLAS RQRVRKRTKV
LSIARKILRI RREPPTLQPK EPPPCLLEAD LTEFDVQNSH LPSEVLYMLK NVRVLGHFEK
PLFLELCRHM VLIPLHQGEG LFRPGDTDDS IYVVQDGRLE LCIHESDGTD AVVKEVLPGD
SVHSLLSILD IITGYPAPYK TVSAKAAVPS TVLRLPAAAF QSVFEKYPET LVRVIQIIMV
RLQRVTFLAL HNYLGLTTEL FNPESQAISL VSVTHVLGET HSLRGLRRQP SHSDDLGSEK
ADAGCRSHCL KVCSPFLMHT VTEKSSFSDI SSSKYKKSRS LSTPVAITGE MSFALNRVYE
RDRVAKEETV HHNPVKSILK KSVTMLHTPS AVYEYSDAGG GNLHQNKVNA IFQAAKKDLL
QVIQIQDHTL LEGRVNLRQV KAGTVVGHQG DQDVSVAFVI SGSLHVYQRM IDREEETLLF
VTHPGEMVGH LAVLTGEPLI FTVRAHRDCT FLSISKAHFY EMMREEPRVV LNVAHTVVKR
VSPFVRQIDF ALDWMAVEAG RAVYRQGDKS DSTFIVLSGR LRSVIAKDDG KKELAGEYGR
GDLIGVVEAL THMNRATTVH AVRDSELAKL PEGALNSIKR RYPQVVTRLI HLLGQKILGN
MQQVNGPLAA RSLALNAPTS KWDAGNPASN LSTVAILPVS EEVPLTSFTL ELQHALGGIG
PTQLLTSDII KQRLGSAALD SVHEYRLSSW LGQQEDIHRI VLYQSDSYLT PWTQRCIRQA
DCIIIVGLGE QEPTVGELER MLEGSAVRAQ KQLVLLHRED GPPPKGTAEW LNMRSWISRH
HHLSCPRRVF SKRSLPKLIE LYQRVFEKCP DRHSDFSRLA RILTGNSIAL VLGGGGARGC
SQVGILRALN EAGIPIDLVG GTSIGSLMGA LYAEEKSYSR MRVRAREWAM DMTSYFKKIL
DLTYPVTSMF SGASFNSGIS SVFKGKQIED LWLSYFNITT DITASSMRVH TDGSLWRYVR
ASMSLSGYLP PLCDPKDGHL LMDGGYINNL PADVARSMGA KVVIAIDVGS RDETNLTNYG
DSLNGWWLLW KRFNPLAEKV KVLNMAEIQT RLAYVCCVRQ LELVKDSEYC EYIRPPIDHY
GTLEFGKFDE IAEVGYQHGK TLFNVWQRSR VVDSMLKDRH QEEFHKTKPG HVVTCPNASF
TDLAEIVSRI EPVKNALING
//
