SWS_DROVI
ID SWS_DROVI Reviewed; 1483 AA.
AC B4M709;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Neuropathy target esterase sws {ECO:0000250|UniProtKB:Q9U969};
DE AltName: Full=Swiss cheese {ECO:0000250|UniProtKB:Q9U969};
DE EC=3.1.1.5;
GN Name=sws {ECO:0000250|UniProtKB:Q9U969}; ORFNames=GJ16892;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW62576.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW62576.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Phospholipase B that deacylates intracellular
CC phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of
CC PtdCho. Its specific chemical modification by certain organophosphorus
CC (OP) compounds leads to distal axonopathy. Plays a role in the
CC signaling mechanism between neurons and glia that regulates glia
CC wrapping during development of the adult brain. Essential for membrane
CC lipid homeostasis and cell survival in both neurons and glia of the
CC adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
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:Q9U969};
CC -!- SUBUNIT: Interacts with Pka-C3; interaction inhibits the catalytic
CC function of Pka-C3 and the esterase activity of sws. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the
CC membrane. {ECO:0000250|UniProtKB:Q9U969}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000255}.
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DR EMBL; CH940653; EDW62576.1; -; Genomic_DNA.
DR RefSeq; XP_002057090.2; XM_002057054.2.
DR AlphaFoldDB; B4M709; -.
DR SMR; B4M709; -.
DR STRING; 7244.FBpp0231309; -.
DR GeneID; 6633725; -.
DR KEGG; dvi:6633725; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B4M709; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; B4M709; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
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:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:EnsemblMetazoa.
DR GO; GO:0007272; P:ensheathment of neurons; IEA:EnsemblMetazoa.
DR GO; GO:0034349; P:glial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006643; P:membrane lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; ISS:UniProtKB.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:EnsemblMetazoa.
DR GO; GO:0072657; P:protein localization to membrane; IEA:EnsemblMetazoa.
DR GO; GO:0007608; P:sensory perception of smell; IEA:EnsemblMetazoa.
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; 3.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Developmental protein; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1483
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389227"
FT TOPO_DOM 1..34
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..1483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 927..1093
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 348..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 931..936
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 958..962
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1080..1082
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 350..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 960
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1080
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 174..301
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 456..585
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 574..701
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1483 AA; 167295 MW; 33D9FF4D68E8946A CRC64;
MDVLELLRAS ANGCYNTLFS DAWFQYVSKQ IATTMYWYGA LLVIGVLFIA WFLYFKRLAR
LRLRDEIARS LSAVTSSGGD HRGLRFRKRD KMLFYGRRML RKMKNVSGQM YSSGKGYKRR
AVMRFARRIL QLQRENRPLE MKTVEPPAEY LEETIEGSDR VPPDALYMLQ SIRIFGHFEK
PIFLKLCKHT QLLQLMAGDY LFKITDPDDS VYIVQSGMIN VYICNADGST LSLKTVRKGE
SVTSLLSFID VLSGNSSYYK TVTAKAMEKS VVIRLPMQAF EEVFEENPDV MIRVIQVIMI
RLQRVLFTAL RNYLGLNAEL VQNHMRTKGS SVVPNAVGGA VLAQASQASR PVVRAPTSPN
SRLSREEHTL SDPDPNPNAN ALLFAEVHGD APYIDLYHHQ QQQSSAVSVN QAGTRRSSTT
YGPSGESPNG NANTAPGTSI DQRLVQSSAV DSLRRELGLS EDDAQIIEPF VEVRELEPNV
TLITEGNAED VCVWFVMTGT LAVYQSNADA TRATKQDSKN DVLIHFVHPG EIVGGLAMLT
GEASAYTIRA RSNSRVAYIR RAAIYQIMRQ RPRIVLDLGN GVVRRLSPLV RQCDYALDWI
FLESGRAVYR QDESSDSTYI VLSGRMRSVI THPGGKKEII GEYGKGDLVG IVEMITETSR
TTTVMAVRDS ELAKLPEGLF NAIKLRYPIV VTRLISFLSH RFLGSMQTRG SNAAGGPVEA
NPVTHKYSTV ALVPITDDVP LTPFTYELYH SLCAIGPVLR LTSEVVRKQL GINIFEAANE
YRLTSWLAQQ EDRNIITLYQ CDSSLSPWTQ RCMRQADVVL IVGLGERSHL VGKFEREIDK
LAMRTQKELV LLYPETTNAK PANTLSWLNA RPWVTKHHHV LCVKRIFTRK SQYRINDLYS
RVLLSEPNMH SDFSRLARWL TGNSIGLVLG GGGARGAAHI GMLKAIQEAG IPIDMVGGVS
IGALMGALWC SERNITTVTQ KAREWSKKMT KWFLQLLDLT YPITSMFSGR EFNKTIHDTF
GDVSIEDLWI PYFTLTTDIT ASCHRIHTNG SLWRYVRSSM SLSGYMPPLC DPQDGHLLLD
GGYVNNLPGH LWRYCRASMS IAGVFPPFCD YRDGHLLLDG CYTNNVPADV MHNLGAAHII
AIDVGSQDDT DLTNYGDDLS GWWLLYKKWN PFTSPVKVPD LPDIQSRLAY VSCVRQLEEV
KNSDYCEYIR PPIDKYKTLA FGSFDEIRDV GYVFGKNYFD NMAKAGRLGR FNQWFNKEPP
KRGNHASLNE YTFIDLAQIV CKLPETYALN TADIFSEDED FDGYISEPTT LNMDRRRIQV
PRAGNSLSFS ETEMDSDVEI DLELERKVDK ATQSTPPTPN KQHALSPTSS QTNLLPLPPN
SKPKEKQPSY DKLDREHKRR QKSKQKQQQE RSSMQQRDSM VTLHPATMAE ATTQTAPHSS
EEDELNKPEQ QPEQKPVPET EEQQQKQQDQ QQQENLTKTD TKN
