SWS_DROPE
ID SWS_DROPE Reviewed; 1435 AA.
AC B4H3U8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=GL15243;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW31049.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479207; EDW31049.1; -; Genomic_DNA.
DR RefSeq; XP_002025527.1; XM_002025491.1.
DR AlphaFoldDB; B4H3U8; -.
DR SMR; B4H3U8; -.
DR STRING; 7234.FBpp0179350; -.
DR EnsemblMetazoa; FBtr0180858; FBpp0179350; FBgn0152847.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; B4H3U8; -.
DR Proteomes; UP000008744; 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..1435
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389224"
FT TOPO_DOM 1..35
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..1435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 944..1110
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 361..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 948..953
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 975..979
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1097..1099
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 437..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 977
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1097
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 176..303
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 474..601
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 590..717
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 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1435 AA; 161521 MW; EB711ED07D5D9BB0 CRC64;
MDVLELLRVS GSNMYYSTFL ADAWCYYISN QITMTMYLYC ALGVLSMLFI GWFVYFKRLA
RLRLRHEIAR SLSAVTMASG GDLRGPRFRK RDKMLFYGRR MLRKMKNVSG QMYSSGKGYK
RRAVIRFARR ILQLRRENMP LEVRTVEPPA EYLEETMEGS DRVPPDALYM LQSIRIFGHF
EKPIFLRLCK HTQLLELMGG DYLFKITDPD DSVYIVQSGM INVYISNADG STLSLKTVRK
GESVTSLLSF IDVLSGNPSY YKTVTAKAIE KSVVIRLPMA AFQEVFKDSP DVMIRVIQVI
MIRLQRVLFT ALRNYLGLNA ELVQNHMRFK GSSQGAGPSV YCSQTTRQAT GSASATATAA
AASGTAGSTH TAVPRPASSL SRYSQDEQHT LSDPNPGIPN LELSGDSVNT LFGEVNGGAR
LNSYPPLYHQ RESDGNLSTR RGSITQQEQP EVGPVPSIDM RLVKSSAVDS LRKELGLPEQ
DAHIIDPFVE VREMEPNVTL ITEGNADDVC VWFVMTGTLA VYQGNADATR IKQDKTDLLI
HYVHPGEIVG GLAMLTGEAS AYTIRSRNHS RVAFIRRAAI YQIMRQRPRI VLDLGNGVVR
RLSPLVRQCD YALDWIFLES GRALYRQDES SDSTYIVLSG RMRSVITHPG GKKEIVGEYG
KGDLVGIVEM ITETSRTTTV MAVRDSELAK LPEGLFNAIK LRYPIVVTKL ISFLSHRFLG
SMQTRTTTGA PGAPVEANPV THKYSTVALV PITDDVPLTP FTYELYHSLC AIGPVLRLTS
DLARKQLGMN IFDASNEYRL TSWLAQQEDR NIITLYQCDN ALSPWTQRCM RQADVVLIVG
LGDHSHLVGK FEREIDRLAL RTQKELVLLY PETASSKPAN TLSWLNARPW VTKHHHVLCV
KRIFTRKSQY RINDLYSRVL LSEPNMHSDF SRLARWLTGN SIGLVLGGGG ARGAAHIGML
KAIQEAGIPI DMVGGVSIGA LMGALWCSER NITTVTQKAR EWSKKMTKWF LQLLDLTYPI
TSMFSGREFN KTIHETFGDV NIEDLWIPYF TLTTDITASC HRIHTNGSLW RYVRSSMSLS
GYMPPLCDPK DGHLLLDGGY VNNLPGHLWR YCRASMSIAG VFPPFCDYRD GHLLLDGCYT
NNVPADVMHN LGAAHIIAID VGSQDDTDLT NYGDDLSGWW LLYKKWNPFT APVKVPDLPD
IQSRLAYVSC VRQLEEVKNS DYCEYIRPLI NKYQTLSCAG CPETYGLNPS DLFSEDEDCD
GYISEPTTLN TDVRRYQVPR GGNSLSLSET EMDMDSDVEM DLKMERKMDK ATQSTPPLQS
KAQILRRKHS KEEARHEWEI KREQKQELAR EQELEREREL SQKGTTAGAT GYTPNAVIAT
QTSLIFMDEE DEMDKKKTKD NDRDEVRGSA EDTGKEKEED KENRSNTNNE TKNYL
