SWS_DROMO
ID SWS_DROMO Reviewed; 1488 AA.
AC B4L535;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=GI21654;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW06294.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW06294.1};
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; CH933811; EDW06294.1; -; Genomic_DNA.
DR RefSeq; XP_002010639.2; XM_002010603.2.
DR AlphaFoldDB; B4L535; -.
DR SMR; B4L535; -.
DR STRING; 7230.FBpp0170871; -.
DR GeneID; 6584999; -.
DR KEGG; dmo:Dmoj_GI21654; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B4L535; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; B4L535; -.
DR Proteomes; UP000009192; 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..1488
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389223"
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..1488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 929..1095
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 339..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 933..938
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 960..964
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1082..1084
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 341..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 962
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1082
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 175..302
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 458..587
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 576..703
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 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1488 AA; 167474 MW; 9118C9BA05DC5A56 CRC64;
MDVLELLRAS VNGCYNTLFS DAWSQYVSKQ IATTTYWYGA LLAIGALFIA WFLYFKRLAS
LRLRDESART LSALTAASGG DHRGLRFRKR DKMLFYGRRM LRKMKNVSGQ MYSSGKGYKR
RAVMRFARRI LQLQRENRPL EMKTVEPPAE YLEETIDGSD RVPPDALYML QSIRIFGHFE
KPIFLKLCKH TQLLQLMAGD YLFKITDPDD SVYIVQSGMI NVYICNADGS TLSLKTVRKG
ESVTSLLSFI DVLSGNSSYY KTVTAKAMEK SVVIRLPMQA FEEVFNENPD VMIRVIQVIM
IRLQRVLFTA LRNYLGLNAE LVQNHMRIKG SNPVPVTVPG PVLSQASQAS RAMASRPATS
PVTRMSREEH TLSDPDPNPN ASAMLFAEVH GDAPYIDLYH HQQQQSSGVS VGGTHRSSGA
CTPTGSGGES PDGTGNATIT NIDQRLVQSS AVDSLRRELG LSEEDTSIIE PFVEVRELEP
NVTLITEGNA EDVCIWFVMT GTLAVYQSNA DATRAAKQDS KNDMLIHFVH PGEIVGGLAM
LTGEASAYTI RARSNSRIAY IRRAAIYQIM RQRPRIVLDL GNGVVRRLSP LVRQCDYALD
WIFLESGRAV YRQDESSDST YIVLSGRMRS VITHPGGKKE IVGEYGKGDL VGIVEMITET
SRTTTVLAVR DSELAKLPEG LFNAIKLRYP IVVTRLISFL SHRFLGSMQT RGANASSAPV
EANPVTHKYS TVALVPITDD VPITPFTYEL YHSLCAIGPV LRLTSEVVRK QLGNNIFEAA
NEYRLTSWLA QQEDRNIITL YQCDSALSPW TQRCMRQADV VLIVGLGERS HMVGKFEREI
DKLAMRTQKE LVLLYPETTN ARPANTLSWL NARPWVTKHH HVLCVKRIFT RKSQYRINDL
YSRVLLSEPN MHSDFSRLAR WLTGNSIGLV LGGGGARGAA HIGMLKAIQE AGIPIDMVGG
VSIGALMGAL WCSERNITTV TQKAREWSKK MTKWFLQLLD LTYPITSMFS GREFNKTIHD
TFGDVSIEDL WIPYFTLTTD ITASCHRIHT NGSLWRYVRS SMSLSGYMPP LCDPQDGHLL
LDGGYVNNLP GHLWRYCRAS MSIAGVFPPF CDYRDGHLLL DGCYTNNVPA DVMHNLGAAH
IIAIDVGSQD DTDLTNYGDD LSGWWLLYKK WNPFTSPVKV PDLPDIQSRL AYVSCVRQLE
EVKNSDYCEY IRPPIDKYKT LAFGSFDEIR DVGYVFGKNY FDNMAKAGRL GRFNQWFNKE
PPKRGNHASL NEYTFIDLAQ IVCKLPETYA LNAVDIFSED EDFDGYISEP TTLNMDRHRI
QVPRAGNSLS FSETELDSDV EIDLELERKV DKSTQSTPPT PNKKHPSTPT SSQGNLMHLP
LSMKAKDKMQ ILDKLEREHK RRQKSKHKRD RSMQRDSKAT LHPAPMAEAT TQTPSSDVDI
DAKLDQLRKL QQELEQGNES EQEQEQEQEQ EQGHIQEPEN VTEADTKN
