PLPL7_RAT
ID PLPL7_RAT Reviewed; 1349 AA.
AC Q5BK26; Q5XIX2; Q8K3H9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 7;
DE EC=3.1.1.- {ECO:0000269|PubMed:12893290};
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:A2AJ88};
DE AltName: Full=Liver NTE-related protein 1;
DE AltName: Full=NTE-related esterase;
GN Name=Pnpla7; Synonyms=Nre, Ntel1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 668-1349, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF SER-980.
RC TISSUE=Brain, and Liver;
RX PubMed=12893290; DOI=10.1016/s0003-9861(03)00264-9;
RA Xie M., Yang D., Matoney L., Yan B.;
RT "Rat NTE-related esterase is a membrane-associated protein, hydrolyzes
RT phenyl valerate, and interacts with diisopropylfluorophosphate through a
RT serine catalytic machinery.";
RL Arch. Biochem. Biophys. 416:137-146(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-1277 AND THR-1281,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Lysophospholipase which preferentially deacylates unsaturated
CC lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Also
CC can deacylate, to a lesser extent, lysophosphatidylethanolamine
CC (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid
CC (C16:0). {ECO:0000250|UniProtKB:A2AJ88}.
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:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A2AJ88}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:A2AJ88}. Lipid droplet
CC {ECO:0000250|UniProtKB:A2AJ88}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, liver, kidney, lung and
CC testis. {ECO:0000269|PubMed:12893290}.
CC -!- DOMAIN: The 3 cNMP binding domains are required for localization to the
CC endoplasmic reticulum. The cNMP binding domain 3 is involved in the
CC binding to lipid droplets. {ECO:0000250|UniProtKB:A2AJ88}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-27 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH91230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC083547; AAH83547.2; -; mRNA.
DR EMBL; BC091230; AAH91230.1; ALT_INIT; mRNA.
DR EMBL; AY100477; AAM44077.1; -; mRNA.
DR RefSeq; NP_653339.2; NM_144738.2.
DR AlphaFoldDB; Q5BK26; -.
DR SMR; Q5BK26; -.
DR STRING; 10116.ENSRNOP00000011633; -.
DR iPTMnet; Q5BK26; -.
DR PhosphoSitePlus; Q5BK26; -.
DR jPOST; Q5BK26; -.
DR PaxDb; Q5BK26; -.
DR PRIDE; Q5BK26; -.
DR GeneID; 246246; -.
DR KEGG; rno:246246; -.
DR UCSC; RGD:708466; rat.
DR CTD; 375775; -.
DR RGD; 708466; Pnpla7.
DR eggNOG; KOG2968; Eukaryota.
DR InParanoid; Q5BK26; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; Q5BK26; -.
DR PRO; PR:Q5BK26; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP:RGD.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR CDD; cd00038; CAP_ED; 3.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1349
FT /note="Patatin-like phospholipase domain-containing protein
FT 7"
FT /id="PRO_0000293491"
FT TOPO_DOM 1..36
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..1349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 947..1113
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 340..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..964
FT /note="Involved in the binding to lipid droplets"
FT /evidence="ECO:0000250|UniProtKB:A2AJ88"
FT REGION 1297..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 951..956
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 978..982
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1100..1102
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 1300..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 980
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 170..297
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 496..599
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 610..715
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV29"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1281
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 980
FT /note="S->A,C,D,H: Abolishes hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:12893290"
FT CONFLICT 956..957
FT /note="GC -> CT (in Ref. 1; AAH91230)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="A -> S (in Ref. 1; AAH83547)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217..1219
FT /note="PAG -> RTV (in Ref. 1; AAH83547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1349 AA; 150024 MW; 4312292A0CFE2FDD CRC64;
MQKEEDVCPE AGYCLGTALS SWGLHFMEEH SQSTMLMGIG IGVLLTLAFV GLAAFFVYRK
VSRFRRAEPI PQYRFRKRDK VMFYGRKIMR KVTTLPHTLV GNTAAPRQRV RKRTKVLSLA
KRILRFKKEY PTLQPKEPPP SLLEADLTEF DVKNSHLPSE VLYMLKNVRV LGHFEKPLFL
ELCKHMVFVQ LQEGEHVFQP GEPDISIYVV QDGRLEVCIQ DADGTEVVVK EVLPGDSVHS
LLSILDVITG HTAPYKTVSA RAAVASTVLW LPAAAFQGVF EKYPETLVRV VQIIMVRLQR
VTFLALHNYL GLTTELFNPE SQAIPLLSVA SVAGRAKRQM SYGPEEQLER SPRLSEFNSS
DQRSVAVSGP LLKRSCSVPL PPIHGEIDEL RQAQGSGSNT SAFQESQEGA TSDLGMAYNR
ARILPHSEEQ LGSSLASKSK KSVVAETSAV FHYSEKPRDE PGPSGRTDAI FRAATKDLLT
LMKLDDPSLL DGRVAFLHVP AGTIVSKQGD QDVNILFVVS GMLHVYQQKI DSLEDTCLFL
THPGEMVGQL AVLTGEPLMF TIRANRDCSF LSISKAHFYE IMRKRPDVVL GVAHTVVRRM
SSFVRQIDFA LDWMEVEAGR AIYRQGDKSD CTYIVLSGRL RSVIRKDDGK KRLAGEYGRG
DLVGVVEMLT HQARATTVHA VRDSELAKLP AGALTSIKRR YPQVVTRLIH LLGEKILGSL
QQGSGTGHQL GFNTASSKWD LGNPPGNLST VAAMPVSEDV PLTAFALELQ HALSAIGPVL
LLTSDNIKQR LGSAALDSIH EYRLSSWLGQ QEDIHRIVLY QADSTLTPWT QRCIRQADCI
LIVGLGDQEP ALGELEQMLE STAVRAQKQL ILLHKEEGPA PSRTVEWLNM RSWCSGHLHL
CCPRRVFSKR SLPKLVEMYT RIFQRPPDRH SDFSRLARIL TGNAIALVLG GGGARGCAQV
GILRALAECG IPVDIIGGTS IGAFMGALFA EERSYSQIRI RAKQWAEDMT SMVKTILDLT
YPITSMFSGT GFNSSISNIF KDRQIEDLWL PYFAITTDIT ASAMRVHTDG ALWRYVRASM
SLSGYMPPLC DPKDGHLLMD GGYINNLPAD VARSMGAKVV IAIDVGSRDE TDLTNYGDAL
SGWWLLWKRW NPLATKVKVL NMAEIQTRLA YVCCVRQLEM VKNSDYCEYL RPPIDSYRTL
DFGKFDEICE VGYQHGPAGF DIWVRSGVLE KMLQDQQGTS KRMDCGVFTC PNSSFTDLAE
IVSRIEPAKV AAVDDESDYQ TEYEEELPAI PKETYADFQS TGIELDSDSE CEPSMSQGPH
SLTSPKQSQD SFPWLPNQDD QGPRLYRPS
