SWS_DROPS
ID SWS_DROPS Reviewed; 1494 AA.
AC B5DKS8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=GA22927;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EDY72128.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379063; EDY72128.1; -; Genomic_DNA.
DR AlphaFoldDB; B5DKS8; -.
DR SMR; B5DKS8; -.
DR STRING; 7237.FBpp0273301; -.
DR PRIDE; B5DKS8; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; B5DKS8; -.
DR OMA; FMYFKRL; -.
DR Proteomes; UP000001819; Genome assembly.
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..1494
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000389225"
FT TOPO_DOM 1..35
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..1494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 944..1110
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 362..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 948..953
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 975..979
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1097..1099
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 437..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 977
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1097
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 474..601
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 590..717
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 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9U969"
SQ SEQUENCE 1494 AA; 168444 MW; 6F53A60DFB6E7999 CRC64;
MDVLELLRVS GSNMYYSTFL ADAWCYYISN QITMTMYLYC ALGVLSMLFI GWFVYFKRLA
RLRLRHEIAR SLSAVTMASG GDLRGPRFRK RDKMLFYGRR MLRKMKNVSG QMYSSGKGYK
RRAVIRFARR ILQLRRENMP LEVRTVEPPA EYLEETMEGS DRVPPDALYM LQSIRIFGHF
EKPIFLRLCK HTQLLELMGG DYLFKITDPD DSVYIVQSGM INVYISNADG STLSLKTVRK
GESVTSLLSF IDVLSGNPSY YKTVTAKAIE KSVVIRLPMA AFQEVFKDSP DVMIRVIQVI
MIRLQRVLFT ALRNYLGLNA ELVQNHMRFK GSSQGAGPSV YCSQTTRQAT GSASATASAA
AASGTAGSTH TAVPRPASSL SRYSQDEQHT LSDPNPGIPN LELSGDSVNT LFGEVNGGAR
LNSYPPLYHQ RESDGNLSTR RGSITQQEQP EVGPVPSIDM RLVKSSAVDS LRKELGLPEQ
DAHIIDPFVE VREMEPNVTL ITEGNADDVC VWFVMTGTLA VYQGNADATR IKQDKTDLLI
HYVHPGEIVG GLAMLTGEAS AYTIRSRNHS RVAFIRRAAI YQIMRQRPRI VLDLGNGVVR
RLSPLVRQCD YALDWIFLES GRALYRQDES SDSTYIVLSG RMRSVITHPG GKKEIVGEYG
KGDLVGIVEM ITETSRTTTV MAVRDSELAK LPEGLFNAIK LRYPIVVTKL ISFLSHRFLG
SMQTRTTTGA PGAPVEANPV THKYSTVALV PITDDVPLTP FTYELYHSLC AIGPVLRLTS
DLARKQLGMN IFDASNEYRL TSWLAQQEDR NIITLYQCDN ALSPWTQRCM RQADVVLIVG
LGDHSHLVGK FEREIDRLAL RTQKELVLLY PETASSKPAN TLSWLNARPW VTKHHHVLCV
KRIFTRKSQY RINDLYSRVL LSEPNMHSDF SRLARWLTGN SIGLVLGGGG ARGAAHIGML
KAIQEAGIPI DMVGGVSIGA LMGALWCSER NITTVTQKAR EWSKKMTKWF LQLLDLTYPI
TSMFSGREFN KTIHETFGDV NIEDLWIPYF TLTTDITASC HRIHTNGSLW RYVRSSMSLS
GYMPPLCDPK DGHLLLDGGY VNNLPGHLWR YCRASMSIAG VFPPFCDYRD GHLLLDGCYT
NNVPADVMHN LGAAHIIAID VGSQDDTDLT NYGDDLSGWW LLYKKWNPFT APVKVPDLPD
IQSRLAYVSC VRQLEEVKNS DYCEYIRPPI DKYKTLAFGS FDEIRDVGYV FGKNYFEGMA
KAGRLGRFNQ WFSKEPPKRG NHASLNEYTF IDLAQIVCRL PETYGLNPSD LFSEDEDCDG
YISEPTTLNT DVRRYQVPRG GNSLSLSETE MDMDSDVEMD LKMERKMDKA TQSTPPLQSK
AQILRRKHSK EEARHEWEIK REQKQELARE QELERERELS QKGTTAGATG YTPNAVIATQ
TSLIFMDEED EMDKKKTKDN DRDEVRGSAE DKGKEKEEDK ENRSNTNNET KNYL
