SWS_DROYA
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 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=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 STRING; 7245.FBpp0262502; -.
DR GeneID; 6525370; -.
DR KEGG; dya:Dyak_GE17492; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; B4Q0P3; -.
DR Proteomes; UP000002282; Chromosome X.
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; 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
