ID   SWS_DROYA               Reviewed;        1467 AA.
AC   B4Q0P3;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=GE17492;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDX02314.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDX02314.1};
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; CM000162; EDX02314.1; -; Genomic_DNA.
DR   RefSeq; XP_002101206.2; XM_002101170.2.
DR   AlphaFoldDB; B4Q0P3; -.
DR   SMR; B4Q0P3; -.
DR   GeneID; 6525370; -.
DR   KEGG; dya:Dyak_GE17492; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   OMA; CIEDLWI; -.
DR   OrthoDB; 5303733at2759; -.
DR   PhylomeDB; B4Q0P3; -.
DR   Proteomes; UP000002282; Chromosome X.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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   CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 3.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1467
FT                   /note="Neuropathy target esterase sws"
FT                   /id="PRO_0000389229"
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..1467
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          958..1124
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          332..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1377..1467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           962..967
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           989..993
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1111..1113
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        991
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1111
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         488..615
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         604..731
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         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U969"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U969"
FT   MOD_RES         1205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ   SEQUENCE   1467 AA;  165017 MW;  DD679DAE7DA7509F CRC64;
     MDVLEMLRAS ASGSYNTIFS DAWCQYVSKQ ITATMYMYCA FGLMGVLFLA WFMYFKRLAR
     LRLRDELARS ISSVTNSYGD LRGLRFRKRD KMLFYGRRML RKMKNVSGQM YSSGKGYKRR
     AVMRFARRIL QLRRDNMPLE MRTVEPPAEY LEETIEGSDR VPPDALYMLQ SIRIFGHFEK
     PIFLRLCKHT QLLELMAGDY LFKITDPDDS VYIVQSGMIN VYISNADGST LSLKTVRKGE
     SVTSLLSFID VLSGNPSYYK TVTAKAIEKS VVIRLPMQAF EEVFQDNPDV MIRVIQVIMI
     RLQRVLFTAL RNYLGLNAEL VQNHMRYKSV STMSGPINSQ TSQSSRQATA NGPPMVINQL
     NLMQSAASGL GMGMGTGTGS GVSVTVTRPP PSPSRHSREE HTLSDPNPNP DGSVHGTSNL
     FTEVHGDAPN ADLFHQQQQS VGNLSTRRSS ITQMTPDGSH TCPQAPGVTT SIDMRLVQSS
     AVDSLRKELG LSEEDAHIIE PFVELRELEP NVTLITEGNA DDVCVWFVMT GTLAVYQSNQ
     DATRAKQDKN DMLIHFVHPG EIVGGLAMLT GEASAYTIRS RSNSRIAFIR RAAIYQIMRQ
     RPRIVLDLGN GVVRRLSPLV RQCDYALDWI FLESGRAVYR QDESSDSTYI VLSGRMRSVI
     THPGGKKEIV GEYGKGDLVG IVEMITETSR TTTVMAVRDS ELAKLPEGLF NAIKLRYPIV
     VTKLISFLSH RFLGSMQTRS GSGAPGAPVE ANPVTHKYST VALVPITDEV PLTPFTYELY
     HSLCAIGPVL RLTSDVVRKQ LGPNIFEAAN EYRLTSWLAQ QEDRNIITLY QCDSSLSAWT
     QRCMRQADVI LIVGLGDRSH LVGKFEREID RLAMRTQKEL VLLYPEATNA KPANTLSWLN
     ARPWVTKHHH VLCVKRIFTR KSQYRINDLY SRVLLSEPNM HSDFSRLARW LTGNSIGLVL
     GGGGARGAAH IGMLKAIQEA GIPVDMVGGV SIGALMGALW CSERNITTVT QKAREWSKKM
     TKWFLQLLDL TYPITSMFSG REFNKTIHDT FGDVSIEDLW IPYFTLTTDI TASCHRIHTN
     GSLWRYVRSS MSLSGYMPPL CDPKDGHLLL DGGYVNNLPG HLWRYCRASM SIAGVFPPFC
     DYRDGHLLLD GCYTNNVPAD VMHNLGAAHI IAIDVGSQDD TDLTNYGDDL SGWWLLYKKW
     NPFTSPVKVP DLPDIQSRLA YVSCVRQLEE VKNSDYCEYI RPPIDKYKTL AFGSFDEIRD
     VGYVFGKNYF ENMAKAGRLG RFNQWFNKEP PKRVNHASLN EYTFIDLAQI VCRLPETYAV
     NTAELFSEDE DCDGYISEPT TLNTDRRRIQ VPRAGNSLSF SETEMDSDVE LDLKLERKMD
     KSTQSTPPTS SRASVRGKEE ARHMDNWHWS VKHKVETASG ATEATNAMID QEQQHQQQAD
     QGVGAEQLAD KDEDKENRSS TYNETKN
//