SWS_DROAN
ID SWS_DROAN Reviewed; 1514 AA.
AC B3MRI9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=GF20991;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV34394.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV34394.1};
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; CH902622; EDV34394.1; -; Genomic_DNA.
DR RefSeq; XP_001963945.1; XM_001963909.2.
DR AlphaFoldDB; B3MRI9; -.
DR SMR; B3MRI9; -.
DR STRING; 7217.FBpp0124183; -.
DR EnsemblMetazoa; FBtr0125691; FBpp0124183; FBgn0097996.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B3MRI9; -.
DR OMA; FMYFKRL; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; B3MRI9; -.
DR Proteomes; UP000007801; 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..1514
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389220"
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..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 987..1153
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 337..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 991..996
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1018..1022
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1140..1142
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 337..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1020
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1140
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 515..644
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 633..760
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 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1514 AA; 169508 MW; FB75DE6E3CB5E827 CRC64;
MDVLELLRAS ATGSYTALFS DAWCQYVSKQ ITNSMYLYCA LGVLSMVFLA WFMYFKRLAR
IRLRDEASRS MSAVNSSSGG DLRGLRFRKR DKMLFYGRRM LRKMKNVSGQ MYSSGKGYKR
RAVMRFARRI LQLRRDNMPL EMRTVEPPAE YLEETIDGSD RVPPDALYML QSIRIFGHFE
KPVFLRLCKH TQLLELMAGD YLFKITDPDD SVYIVQSGMI NVYISNADGS TLSLKTVRKG
ESVTSLLSFI DVLSGNPSYY KTVTAKAIEK SVVIRLPMEA FEEVFQDNPD VMIRVIQVIM
IRLQRVLFTA LRNYLGLNAE LVQNHMRFKS STIMAPSTHS SQCSRQTGSQ PTLGVPAPTC
SNTTTTASPT TANTVHSGLA GANGVIGQSR PPISPSRHSR EEHTLSDPNP NPDVINTSVG
GASGTSMYAE VHGDAPNVDV FHQQQHSVGN LSTRRGSISQ MAPDLGPALS QPGLGQGQGL
GPGVTGAPPL MTGAPASKID MRLVHASAVD SLRKELGLPE EDSHIIEPFV EVRELEPNVT
LITEGNSDDV CVWFVMTGTL AVYQANQDAA RAKQQQEKND MLIHFVHPGE IVGGLAMLTG
EASAYTIRSR NNSRVAFIRR AAIYQIMRQR PRIVLDLGNG VVRRLSPLVR QCDYALDWIF
LESGRAVYRQ DEISDSTYIV LSGRMRSVIT HPGGKKEIIG EYGKGDLVGI VEMITETSRT
TTVLAVRDSE LAKLPEGLFN AIKLRYPIVV TKLISFLSHR FLGTMQTRSS SAAPGGPVEA
NPVTHKYSTV ALVPITDEVP LTPFTYELYH SLCAIGPVLR LTSDVVRKQL GPNIFEAANE
YRLTSWLAQQ EDRNIITLYQ CDNALSAWTQ RCMRQADVIL IVGLGNGSHL VGKFEREIDR
LAMRTQKELV LLYPETTNSK PANTLSWLNA RPWVTKHHHV LCVKRIFTRK SQYRINDLYS
RVLLSEPNMH SDFSRLARWL TGNSIGLVLG GGGARGAAHI GMLKAIQEAG IPIDMVGGVS
IGALMGALWC SERNITTVTQ KAREWSKKMT KWFLQLLDLT YPITSMFSGR EFNKTIHDTF
GDVSIEDLWI PYFTLTTDIT ASCHRIHTNG SLWRYVRSSM SLSGYMPPLC DPKDGHLLLD
GGYVNNLPGQ LWRYCRASMS IAGVFPPFCD YRDGHLLLDG CYTNNVPADV MHNLGAAHII
AIDVGSQDDT DLTNYGDDLS GWWLLYKKWN PFTSPVKVPD LPDIQSRLAY VSCVRQLEEV
KNSDYCEYIR PPIDKYKTLA FGSFDEIRDV GYVFGKNYFE NMAKAGRLGR FNQWFNKEPP
KRGNHASLNE YTFIDLAQIV CRLPETNAGN SADIFSEDED CDGYISEPTT LNTDRRRIQV
PRAGNSLSFS ENEMDSDVEL DLQLDRKTEK SIHSAATSVA RGSMRSREFH KLEQDRSVEI
TRLKDETERI MAPTNLDRKG DGQEQEKEPE QEQELETEEP NQENTEVEEE QRNQGEGNED
NKENKGGAYN ETKN
