PLPL7_CAEEL
ID PLPL7_CAEEL Reviewed; 1353 AA.
AC Q02331; Q6LDE9; Q6LDF0; Q95PX1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Patatin-like phospholipase domain-containing protein ZK370.4 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:A2AJ88};
GN ORFNames=ZK370.4 {ECO:0000312|WormBase:ZK370.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:ZK370.4b};
CC IsoId=Q02331-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZK370.4a};
CC IsoId=Q02331-2; Sequence=VSP_006718;
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; BX284603; CCD61723.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD61724.1; -; Genomic_DNA.
DR PIR; S44665; S44665.
DR RefSeq; NP_498926.2; NM_066525.2. [Q02331-2]
DR RefSeq; NP_498927.2; NM_066526.4. [Q02331-1]
DR AlphaFoldDB; Q02331; -.
DR SMR; Q02331; -.
DR STRING; 6239.ZK370.4b; -.
DR iPTMnet; Q02331; -.
DR EPD; Q02331; -.
DR PaxDb; Q02331; -.
DR PeptideAtlas; Q02331; -.
DR PRIDE; Q02331; -.
DR EnsemblMetazoa; ZK370.4a.1; ZK370.4a.1; WBGene00022718. [Q02331-2]
DR EnsemblMetazoa; ZK370.4b.1; ZK370.4b.1; WBGene00022718. [Q02331-1]
DR GeneID; 176225; -.
DR KEGG; cel:CELE_ZK370.4; -.
DR UCSC; ZK370.4b; c. elegans. [Q02331-1]
DR CTD; 176225; -.
DR WormBase; ZK370.4a; CE34454; WBGene00022718; -. [Q02331-2]
DR WormBase; ZK370.4b; CE34455; WBGene00022718; -. [Q02331-1]
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000168388; -.
DR InParanoid; Q02331; -.
DR OMA; GHHHIRI; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; Q02331; -.
DR Reactome; R-CEL-6814848; Glycerophospholipid catabolism.
DR PRO; PR:Q02331; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022718; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
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; IPR001423; LysoPLipase_patatin_CS.
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; 2.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1353
FT /note="Patatin-like phospholipase domain-containing protein
FT ZK370.4"
FT /id="PRO_0000172529"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 942..1108
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 49..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 946..951
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 973..977
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1095..1097
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 975
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1095
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 245..372
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 444..581
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 570..692
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 VAR_SEQ 494..504
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_006718"
SQ SEQUENCE 1353 AA; 152396 MW; 9DAA023A87A27197 CRC64;
MSFFYSLFAP LIFLVTFIYN HVLLILFTVC IIGAAAFFVS YYLFGYSNTP SSASSSATPS
SRNSPNKERS KKVPTILETD NEDDEIRVNG SPKSGTPTNT QTIEPPTSLN LNMVNSASGS
NLSGARRMRK RDWAKKLYKS LVQDSPGRTP TDESSDEENA NVVMGGGSVP RRRSKHGNSS
RRRQSTAFQL AKDLIRRGSR SYFRQNQENN KDTRVRPPQE FFEPTDLPEI PQNLQPEIFY
ILHNLKMLEL PSEWKLDPRE IEVRSFQAGD YIVKPGESDD AIYVAIDGEL TVHIRHMEGK
EYLVKCIPAG GSFFSLLSML DILMDFPSIF RTVALKAADP CRVAKFPITS FRESYHKNPE
AWIRPIQIVI TRLLHVTLTT LHQYMGLSSE LMRRRRDDDR HRNGSSTSKL QLSLSLKKKE
KPFNINDNEQ DQLIVARKWM AEAFGLVADD VVSEQIGSKI HLESYEAGHV IIEQGAEEEV
LMMVLHGNLI LAQYGSDFFA QIERESLFDE ENNEEDESAV IRVTARELVG GLQILTNEPS
FYTIRAAVQT RVAIMKKKDF SAFLEAHPEI YLPVAHSVLR RLSPFLRGVD FALDWVLVDS
GHACYRAGDM ADSLFVVLSG RLRSVEKKTV VEEFGRGDVL GMMEVLTKKP RATTVLAVRF
SQLARVPEGL LNFIKMQYPQ VGFRLVQLLG QYYSQTNRRA PFAAPTVIRT NELGATDPMS
HIKNLHTIAV VPASPDVPLV PFTCELYHAL SSNLRVLRLS SQKVAACLDP SVLEKQADFR
LMHWLNVQED TYPLVIYECD FTQTNWTRRC LRQADAILVV AIGGKTPEKQ TLMRELMNMN
QDGVRTNKEL ILLWPESTKT PSGTIEWLKN SYFSGHHHIR APKRMLQWNR KFRKMSRAEV
MTPTSVENEV IEYYEKNVFW TPDRRSDFSR LARILTGNAI GLVLGGGGAR GAAHVGVLRA
LREEGIPVDI VGGTSIGSLI GGLYAETPDD VVVETRAASW FNGMSSLWRK LLDLTYAHSA
MFTGAQFNFS IKDLFEERLI EDLWISYFCI STDISTSEMR VHRSGPLWAY CRASMSLAGY
LPPLCDPQDG HLLLDGGYVN NVPADVMRNL GARCVIACDV GSIEETNLYD YGDSLSGMWV
LLKRLNPFGT PPRILNMEEI QSRLAYVSCV RQLEVVKKAS YCRYLRPPIE PFKTLDFPKF
QEIMELGLKY GREACHELIT NDRAGILGDE KETRKFKRQQ SRREKPDVSR AVSFTDLAAA
MSKIPVVRPT LRHSMSLNPS ANGPVGRAGD HFLLDDDLFN DTDYYEEESS QSENGNESFT
EDEDLVIGPP SSSSSGGNVS ENPRGTTPRP PSS
