SWS_DROWI
ID SWS_DROWI Reviewed; 1481 AA.
AC B4N1W9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=GK16217;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW78358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW78358.1};
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; CH963925; EDW78358.1; -; Genomic_DNA.
DR RefSeq; XP_002067372.2; XM_002067336.2.
DR AlphaFoldDB; B4N1W9; -.
DR SMR; B4N1W9; -.
DR STRING; 7260.FBpp0245360; -.
DR PRIDE; B4N1W9; -.
DR GeneID; 6644825; -.
DR KEGG; dwi:6644825; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B4N1W9; -.
DR OMA; FMYFKRL; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; B4N1W9; -.
DR Proteomes; UP000007798; 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:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
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..1481
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389228"
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..1481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 967..1133
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 336..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 971..976
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 998..1002
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1120..1122
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 336..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1000
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1120
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 492..624
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 613..740
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 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1481 AA; 165348 MW; FF336B974557F11A CRC64;
MDVLELLRAS ANGCYNTIFS DAWSQYVSQQ ITSSLYLYIA LGILTVLFVA WFIYFKRLAR
LRLRDEIARS LNAVTSASGG DLRGLRFRKR DKMLFYGRRM LRKMKNVSGQ MYSSGKGYKR
RAVMRFARRI LQLRRENMPL EMRTVEPPAE YLEETIEGSD RVPPDALYML QSIRIFGHFE
KPVFLKLCKH TQVLELMAGD YLFKITDADD SVYIVQSGMI NVYISNADGS TLSLKTVRKG
ESVTSLLSFI DVLSGNPSYY KTVTAKAMEK SVVIRLPMQA FEEVFRENPD VMIRVIQVIM
IRLQRVLFTA LRNYLGLNAE LVQNHMRNKS ITISGHLNSQ SQSSQSMRQQ TTATATGGTS
ATALGGQQLP AAVPSLPLQR QPPPPTIAPP LRHSREEHTL SGPNPNPNSG NNVQLPEVHG
DAPNIDIYHQ QQHGGSTSTG NLSTRRGSLV QPSIGGGGGG STAQEGGCAA AGAPTIDMRL
IQSSAVESLR KELGLPNEDA HIIEPFVEVR ELEPNVTLIT EGNADDVCIW FVMTGTLAVY
QGVADATRSS TATTKSDKSD LLIHFVHPGE IVGGLAMLTG EASAYTIRSR NNSRVAYIRR
AAIYQIMRQR PRIVLDLGNG VVRRLSPLVR QCDYALDWIF LESGRAVYRQ DESSDSTYIV
LSGRMRSVIT NPGGKKEIVG EYGKGDLVGI VEMITETSRT TTVMAVRDSE LAKLPEGLFN
AIKLRYPIVV TKLISFLSHR FLGSMQTRGS TGAPGAPVEA NPVTHKYSTV ALVPITDEVP
LTPFTYELYH SLCAIGPVLR LTSEVVRKQL GQNIFEAANE YRLTSWLAQQ EDRNIITLYQ
CDNSLSPWTH RCMRQADVIL IVGLGDRSHL VGKFEREIDR LAMRTQKELV LLYPETTNAK
PANTLSWLNA RPWVTKHHHV LCVKRIFTRK SQYRINDLYS RVLLSEPNMH SDFSRLARWL
TGNSIGLVLG GGGARGAAHI GMLKAIQEAG IPIDMVGGVS IGALMGALWC SERNITTVTQ
KARQWSKKMT KWFLQLLDLT YPITSMFSGR EFNKTIHDTF GDVSIEDLWI PYFTLTTDIT
ASCHRIHTNG SLWRYVRSSM SLSGYMPPLC DPKDGHLLLD GGYVNNLPGH LWRYCRASMS
IAGVFPPFCD YRDGHLLLDG CYTNNVPADV MHNLGAAHII AIDVGSQDDT DLTNYGDDLS
GWWLLYKKWN PFTSPVKVPD LPDIQSRLAY VSCVRQLEEV KNSDYCEYIR PPIDKYKTLA
FGSFDEIRDV GYVFGKNYFE SMAKAGRLGR FNQWFNKEPP KRGNHASLNE YTFIDLAQIV
CKLPETYAVN TAEIFSEDED CDGYISEPST LNTDRRIQVP RAGNSLSLSE AEMDSDVEID
FRSDSKKDKA TQSTPPAPGK DNEDKTDAVD RIPLLTLERP LTDQQQQHSD ETDEQETPRA
MKDGTNTMTT QTTSPTTDAG SEWAGSESEL EKENKNVNTK N
