ID SWS_DROGR Reviewed; 1464 AA.
AC B4JLX2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=GH24540;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV91733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV91733.1};
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; CH916371; EDV91733.1; -; Genomic_DNA.
DR RefSeq; XP_001992026.1; XM_001991990.1.
DR AlphaFoldDB; B4JLX2; -.
DR SMR; B4JLX2; -.
DR STRING; 7222.B4JLX2; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B4JLX2; -.
DR OMA; CIEDLWI; -.
DR PhylomeDB; B4JLX2; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
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; 2.
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;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1464
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389222"
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..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 928..1094
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 329..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 932..937
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 959..963
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1081..1083
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 329..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 961
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1081
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 176..303
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 456..586
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 575..702
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 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1464 AA; 165239 MW; 4D2B9897F9EE0930 CRC64;
MDVLELLRAS ATGCYNTIFS EAWHQYVHKQ IAAAVYWYGA LFLLGVLLFV WFLYFKRLAR
LRLRDEIARS LSAVTSAATG VDHRGLRFRK RDKMLFYGRR MLRKMKNVSG QMYSSGKGYK
RRAVMRFARR ILQLQRENRP LEMKTVEPPA EYLEETIEGS DRVPPDALYM LQSIRIFGHF
EKPIFLKLCK HTQILQLMAG DYLFKITDPD DSVYIVQSGM INVYICNADG STLSLKTVRK
GESVTSLLSF IDVLSGNSSY YKTVTAKAIE KSVVIRLPMQ AFEEVFDENP DVMIRVIQVI
MIRLQRVLFT ALRNYLGLNA ELVQNHMRNK NSSNPMATGQ TTSNVQSQTS QATQSRPSGT
TRTPTSPMLR LSREEHTLSD PDPNPNANNL HYHEMHGDAP YIDLYHYQQQ QQSLNSPRRN
STAHVSEAAA ASTASSPTTI DQRLVQSSAV DSLRRELGLG EEDAHIIEQF VLVRELEPNV
TLITEGNADD VCIWFVMTGN LAVYQSNADA TRASAKQDAK PEMLIHFVHP GEIVGGLAML
TGEASAYTIR SRNNSRVAFI RRAAIYQIMR QRPRIVLGLG NGVVRRLSPL VRQCDYALDW
IFLESGRAVY RQDESSDSTY IVLSGRMRSV ITQPNGKKEI VGEYGKGDLV GIVEMITETS
RTTTVMAVRD SELAKLPEGL FNAIKLRYPI VVTRLISFLS HRFLGSMQTR GSNAYGTPVE
ANPVTHKYST VALVPITDDV PLTPFTYELY HSLCAIGPVL RLTSEVVGKQ LGVNIFDTAN
EYRLTSWLAQ QEDRNIITLY QCDSSLSPWT QRCMRQADVI LIVGLGERSH LVGKFEREID
KLAMRTQKEL VLLYPETTNA KPANTLSWLN ARPWVTKHHH VLCVKRIFTR KSQYRINDLY
SRVLLSEPNM HSDFSRLARW LTGNSIGLVL GGGGARGAAH IGMLKAIQEA GIPIDMVGGV
SIGALMGALW CSERNITTVT QKAREWSKKM TKWFLQLLDL TYPITSMFSG REFNKTIHDT
FGDVTIEDLW IPYFTLTTDI TASCHRIHTN GSLWRFVRSS MSLSGYMPPL CDPQDGHLLL
DGGYVNNLPG HLWRYCRASM SIAGVFPPFC DYRDGHLLLD GCYTNNVPAD VMHNLGAAHI
IAIDVGSQDD TDLTNYGDDL SGWWLLYKKW NPFTSPVKVP DLPDIQSRLA YVSCVRQLEE
VKNSDYCEYI RPPIDKYKTL AFGSFDEIRD VGYVFGKNYF DTMAKAGRLG RFNQWFNKEP
PKRGNHASLN EYTFIDLAQI VCKLPETYVR LGTPDLFSED EDEDFDGYIS EPTTLNTDRR
RIQVHRAGNS LSFSEAELDS DVELDLEMEN KVDKATQSTP TLPDKRSVQT PTPSLFNLTM
PIAVDEIDKS SGRVKRKLEA TNTASIAEPE ASPSIKAEAT TQTTPPTSKR TEQDEHELEH
EQVVEKQQVM DKQQGNTTNN DTKN
//
