ID PLPL6_CAEEL Reviewed; 1095 AA.
AC Q21534; Q20023;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Putative patatin-like phospholipase domain-containing protein M110.7 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q3TRM4};
GN ORFNames=M110.7 {ECO:0000312|WormBase:M110.7};
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=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 -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90264.3; -; Genomic_DNA.
DR EMBL; Z49966; CAA90264.3; JOINED; Genomic_DNA.
DR PIR; T21745; T21745.
DR RefSeq; NP_495734.3; NM_063333.3.
DR AlphaFoldDB; Q21534; -.
DR SMR; Q21534; -.
DR STRING; 6239.M110.7.1; -.
DR EPD; Q21534; -.
DR PaxDb; 6239-M110-7; -.
DR EnsemblMetazoa; M110.7.1; M110.7.1; WBGene00010915.
DR GeneID; 187474; -.
DR KEGG; cel:CELE_M110.7; -.
DR UCSC; M110.7; c. elegans.
DR AGR; WB:WBGene00010915; -.
DR WormBase; M110.7; CE43244; WBGene00010915; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; Q21534; -.
DR OMA; LISKCWK; -.
DR OrthoDB; 5303733at2759; -.
DR PhylomeDB; Q21534; -.
DR Reactome; R-CEL-6814848; Glycerophospholipid catabolism.
DR PRO; PR:Q21534; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010915; Expressed in adult organism and 1 other cell type or tissue.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.
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:SF21; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN M110.7-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
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; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1095
FT /note="Putative patatin-like phospholipase domain-
FT containing protein M110.7"
FT /id="PRO_0000172530"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 768..935
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 75..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 772..777
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 799..803
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 922..924
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 75..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 801
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 922
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 144..237
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 327..416
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 450..509
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"
SQ SEQUENCE 1095 AA; 124856 MW; A52D68E2BC62CB98 CRC64;
MLHYLLSVLL LIFENILELC MCITLVILIY YFWPSKQLED ATLQYFPDTT QNSSEVFIDP
PERNPIFYPI SPLRHKKRSS KEEMTPDKKR DSSEKISKQP PRELFEPNEQ EQVPSHIKPE
IFFVLKALEG LELPTTWQLD PKDVETLSID TGSVVLSPGR ANDVIVVVIS GELGIFTNVS
LGDKRYDCNI KTLRSGESYF SQTSIIEILM NEKPNNKYIH LKALTSCRVA TYHLTSFHTS
FIANPQQWIR TIQVVMTRLQ QCTLITCNMY LGIGGKCLNA KRKLPDSGKF KDFNKLTEAE
QLNKGVEAIA QAMGIPDQSD KLREKVRKYE CQAGTVVTEE NSFEIDMIFV VFGKLRLKRG
DLEHDDTGTS LTFDVYPGDM LPSMQILTNE PAMCSAKALE KTIYFKICRD EYIQFLFAHP
VIYLRLAFHA LQFISPFARV FDMAVHWHRI ETGQALFRQG DKSDSMHIVM GGRLRAVDST
KIIEEYGRLD LIGITDMAEK RPRRNTVMAV RFSHIVCIPE NLLSFVKIRY PQVGNKLLKL
ISKCWKAPTP ETMSHVETTR NQNLRTIAIV PASRRVPLTE FTCELYNQLS KHVKTLRLSS
SVVENYFESE VITKKADYGL MHWLNVQEIA YSLVLYQCDF HKTNWTRRCL RMADAILMVA
LGTESKEEQV LAEALLSCNE KGVRQSKELV FLWPIDTPTP SGTAAWIKES YYSGYHHLRA
PNRLFSFPLK TREKKIVEYY ETTVYGEISY QSDFSRLARI LTGNAIGIVF GGGGARGAAH
AGALRALIEK KVQIDMVGGT SIGALFGSLY ATTPDIRAVG RMKDFFTDRL RNNILDVVRD
LTWPYCGILT GHRFNLCVQR MLNDVNIEDC WVSFFCITTD LTSSSMRIHR NGIMWPVVRS
SMSIAGYVPP ICDPQDGHLL LDGAYVNNLP ADIMRSLGAN VVIAIDVGMS DDNTNLRNYG
FSISGTWCLF KRWWPFGEEL RVLNMNEVQN RLAYVCCVNQ MEIVKNAQYC YYVKLPIESF
GIFDFSKFDQ AAQIGYDITK QKMEEFFEDS VATRRKLLGC ARNVRQTPQK SKNDNILSFV
NMPVLPKPPS DIKSD
//
