ID A0A1I8M435_MUSDO Unreviewed; 1421 AA.
AC A0A1I8M435;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Neuropathy target esterase sws {ECO:0000256|ARBA:ARBA00019369};
DE AltName: Full=Swiss cheese {ECO:0000256|ARBA:ARBA00030862};
GN Name=101897743 {ECO:0000313|EnsemblMetazoa:MDOA001032-PC};
GN Synonyms=LOC101897743 {ECO:0000313|RefSeq:XP_005181335.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA001032-PC};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA001032-PC}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA001032-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005181335.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005181335.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025020}.
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:0000256|ARBA:ARBA00000960};
CC -!- SUBUNIT: Interacts with Pka-C3; interaction inhibits the catalytic
CC function of Pka-C3 and the esterase activity of sws.
CC {ECO:0000256|ARBA:ARBA00011476}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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 RefSeq; XP_005181335.1; XM_005181278.3.
DR STRING; 7370.A0A1I8M435; -.
DR EnsemblMetazoa; MDOA001032-RC; MDOA001032-PC; MDOA001032.
DR GeneID; 101897743; -.
DR VEuPathDB; VectorBase:MDOA001032; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 3.
DR CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
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; 1.
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 {ECO:0000256|ARBA:ARBA00022473};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..297
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 489..563
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 569..696
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 921..1087
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 321..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 160810 MW; CF2DA6BC0698D2F1 CRC64;
MDIIGVIRTT AQDYGDIFSD AWWHLLNMEF KTAMTLYITV GLLTLILIIW YIFYRRYIRD
RERQKLLLAQ SSYASADMRG LRFRKRDKML FYGRRMLRKV KNVSGQVYGG QGRKRRAVMR
FAKRLLQLRR ENIPLQMKTV EPPAEYLEET MEGSDRVPPD ALYMLQSIRI FGHFEKPIFL
KLCKHTETLT LDPGDFLFKI TDADDSVFIV QSGQINVFIS NADGSTLSLK TVRKGESVTS
LLSFVDVLSG NPSYYKTVTA KAVEKSVVIR LPMQAFKEVF DENPDIMIRV IQVIMIRLQR
VLFTALRNYL GLNSELVQNH MRHKKSQNNA QQTPQSAGVQ QQQQQQQQSS ATATQQQTQV
KHSPGHRRSQ GETMPPPQHS LSDPIPPPDM LQDVASYEAL IANGSAQYAA HSSVGNLSTR
RYSMTPAEIN VNASSIDMQL VNMSAVDSFL KELGLPEEDR AFLEPFVEVR EVDVDVTLIK
EGNSDDICVW FVMTGGLAVY QSGVDPIRHF QSDRVDCFIH HVHPGEIVGG LAVLTGEASA
YTITSLYPSR VAFIRRPAIY QIMRERPKIV LDLGNGVVRR LSPLVRQCDY ALDWIFLESG
RAVYRQDEMS DSTYIVLSGR MRSVITQSSG KKEIVGEYGK GDLVGIVEMI TETCRTTTVM
AVRDSELAKL PEGLFNAIKL RYPIVVTKLI SLLSHRILGT MQSRSAGNAA PLEANPVTHK
YSTVALVPVS EDVPLTAFTY ELFHSLCAIG PTLRLTSEVV RKQLGVHTFE QSNEYRLTSW
LAQQEDRYII TLYQCDPSLS AWTQRCMRQA DVILIVGLGD RAPTVGKFER EIDRLAMRTQ
KELVLLYSET DSSKPMNTLQ WLNARPWVTK HHHIQCVKRM FTRKSQYRIN DLYSRVLMSE
PNMHSDFSRL ARWLTGNSIG LVLGGGGARG AAHIGMMKAI QEAGIPIDMV GGVSIGALMG
ALWCSDRNIT TVTQKAREWC KKMTKWFLQL LDLTYPITSM FSGREFNKSI RETFGDVSIE
DLWIPYFTLT TDITASCHRV HTNGHLWRYV RASMSIAGVF PPFCDYKDGH LLLDGCYTNN
VPADVMRNLG AAHIIAIDVG SQDDTDLTNY GDDLSGWWLL YKKWNPFTSP VKVPDLPDIQ
SRLAYVSCVR QLEEVKNSDY CEYIRPPIDK YKTLAFGSFD EIRDVGYVFG KNYFESMAKA
GRLGRFNQWF NKEPPKKDNH ASLSEYTFID LAQIVCKIPD LDHPLHTMDQ HQHNYFYSED
EDYDGYISEP SIYNRNQIKM KRTGTSLSLS ENEMDSDIEV DLSLAIRQHQ NLKTRSSPQT
PVNLPCSLSN IDNIDGRQNN VSVAPTPEDD GGMTMQMRYK SLDNMSTNTT TPKQINPQLG
GDDNNGNEEN ADSNKLSTED DNSSSNKTNT NNSTTTKAKT S
//
