SWS_DROSE
ID SWS_DROSE Reviewed; 1468 AA.
AC B4IL64;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=GM11957;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW53681.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW53681.1};
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; CH480865; EDW53681.1; -; Genomic_DNA.
DR RefSeq; XP_002044474.1; XM_002044438.1.
DR AlphaFoldDB; B4IL64; -.
DR SMR; B4IL64; -.
DR STRING; 7238.B4IL64; -.
DR EnsemblMetazoa; FBtr0194942; FBpp0193434; FBgn0166898.
DR GeneID; 6620266; -.
DR KEGG; dse:6620266; -.
DR HOGENOM; CLU_000960_1_0_1; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; B4IL64; -.
DR Proteomes; UP000001292; 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..1468
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389226"
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..1468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 950..1116
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 332..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 954..959
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 981..985
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1103..1105
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 332..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 983
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1103
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 480..607
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 596..723
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 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1468 AA; 165401 MW; FA02ED9424EA49FF CRC64;
MDVLEMLRAS ASGSYNTIFS DAWCQYVSKQ ITATVYMYCA LVMMSLLFIA WFLYFKRMAR
LRLRDELARS ISTATNSSGD LRGLRFRKRD KMLFYGRRML RKVKNVSGQM YSSGKGYKRR
AVMRFARRIL QLRRDNMPLE MRTVEPPAEY LEETIEGSDR VPPDALYMLQ SIRIFGHFEK
PVFLRLCKHT QLLELMAGDY LFKITDPDDS VYIVQSGMIN VYISNADGST LSLKTVRKGE
SVTSLLSFID VLSGNPSYYK TVTAKAIEKS VVIRLPMQAF EEVFQDNPDV MIRVIQVIMI
RLQRVLFTAL RNYLGLNAEL VQNHMRYKSV STMSGPINSQ TSQSSRQAPN GPPMVINQLN
LMQSAASGTG SGVSVTVTRP PSSPSRHSRE EHTLSDPNPN PDGSFHGTTN LFTEVHGDAP
NADLFQQQQQ PSVGNLSTRR SSITLMTPDG SHSCVQTPGV TTSIDMRLVQ SSAVDSLRKE
LGLSEEDSHI IEPFVELREL EPNVTLITEG NADDVCVWFV MTGTLAVYQS NQDATRAKQD
KSDMLIHFVH PGEIVGGLAM LTGEASAYTI RSRSYARIAF IRRAAIYQIM RQRPRIVLDL
GNGVVRRLSP LVRQCDYALD WIFLESGRAV YRQDESSDST YIVLSGRMRS VITHPGGKKE
IVGEYGKGDL VGIVEMITET SRTTTVMAVR DSELAKLPEG LFNAIKLRYP IVVTKLISFL
SHRFLGSMQT RSGSGAPGAP VEANPVTHKY STVALVPITD EVPLTPFTYE LYHSLCAIGP
VLRLTSDVVR KQLGSNIFEA ANEYRLTSWL AQQEDRNIIT LYQCDSSLSA WTQRCMRQAD
VILIVGLGDR SHLVGKFERE IDRLAMRTQK ELVLLYPEAT NAKPANTLSW LNARPWVTKH
HHVLCVKRIF TRKSQYRIND LYSRVLLSEP NMHSDFSRLA RWLTGNSIGL VLGGGGARGA
AHIGMLKAIQ EAGIPVDMVG GVSIGALMGA LWCSDRNITT VTQKAREWSK KMTKWFLQLL
DLTYPITSMF SGREFNKTIH DTFGDVSIED LWIPYFTLTT DITASCHRIH TNGSLWRYVR
SSMSLSGYMP PLCDPKDGHL LLDGGYVNNL PGHLWRYCRA SMSIAGVFPP FCDYRDGHLL
LDGCYTNNVP ADVMHNLGAA HIIAIDVGSQ DDTDLTNYGD DLSGWWLLYK KWNPFTSPVK
VPDLPDIQSR LAYVSCVRQL EEVKNSDYCE YIRPPIDKYK TLAFGSFDEI RDVGYVFGKN
YFENMAKAGR LGRFNQWFNK EPPKRVNHAS LNEYTFIDLA QIVCRLPETY AVNTAELFSE
DEDCDGYISE PTTLNTDRRR IQVSRAGNSL SFSETEMDSD VELDLKLERK MDKSTQSSPP
TSSRTDMRGK EEAKHMANWH WGVKHKDETG SGATVATHTQ TGQEQELQQQ QKLQQLQQDQ
GARAEQLVDK DKEEDKENRS SPNNETKN
