ID A0A1B0CSP7_LUTLO Unreviewed; 1319 AA.
AC A0A1B0CSP7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Neuropathy target esterase sws {ECO:0000256|ARBA:ARBA00019369};
DE AltName: Full=Swiss cheese {ECO:0000256|ARBA:ARBA00030862};
OS Lutzomyia longipalpis (Sand fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Lutzomyia; Lutzomyia.
OX NCBI_TaxID=7200 {ECO:0000313|EnsemblMetazoa:LLOJ007896-PA, ECO:0000313|Proteomes:UP000092461};
RN [1] {ECO:0000313|Proteomes:UP000092461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jacobina {ECO:0000313|Proteomes:UP000092461};
RA Richards S., Qu C., Dillon R., Worley K., Scherer S., Batterton M.,
RA Taylor A., Hawes A., Hernandez B., Kovar C., Mandapat C., Pham C., Qu C.,
RA Jing C., Bess C., Bandaranaike D., Ngo D., Ongeri F., Arias F., Lara F.,
RA Weissenberger G., Kamau G., Han H., Shen H., Dinh H., Khalil I., Jones J.,
RA Shafer J., Jayaseelan J., Quiroz J., Blankenburg K., Nguyen L., Jackson L.,
RA Francisco L., Tang L.-Y., Pu L.-L., Perales L., Lorensuhewa L.,
RA Munidasa M., Coyle M., Taylor M., Puazo M., Firestine M., Scheel M.,
RA Javaid M., Wang M., Li M., Tabassum N., Saada N., Osuji N., Aqrawi P.,
RA Fu Q., Thornton R., Raj R., Goodspeed R., Mata R., Najjar R., Gubbala S.,
RA Lee S., Denson S., Patil S., Macmil S., Qi S., Matskevitch T.,
RA Palculict T., Mathew T., Vee V., Velamala V., Korchina V., Cai W., Liu W.,
RA Dai W., Zou X., Zhu Y., Zhang Y., Wu Y.-Q., Xin Y., Nazarath L., Kovar C.,
RA Han Y., Muzny D., Gibbs R.;
RT "Whole Genome Assembly of Lutzomyia longipalpis.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBC1175139.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Jacobina {ECO:0000313|EMBL:MBC1175139.1};
RC TISSUE=Midgut {ECO:0000313|EMBL:MBC1175139.1};
RA Coutinho-Abreu I.V., Serafim T.D., Meneses C., Kamhawi S., Oliveira F.,
RA Valenzuela J.G.;
RT "Leishmania infection induces a limited differential gene expression in the
RT sand fly midgut.";
RL BMC 21:608-608(2020).
RN [3] {ECO:0000313|EnsemblMetazoa:LLOJ007896-PA}
RP IDENTIFICATION.
RC STRAIN=Jacobina {ECO:0000313|EnsemblMetazoa:LLOJ007896-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
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DR EMBL; AJWK01026359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GITU01006436; MBC1175139.1; -; Transcribed_RNA.
DR EnsemblMetazoa; LLOJ007896-RA; LLOJ007896-PA; LLOJ007896.
DR VEuPathDB; VectorBase:LLOJ007896; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000092461; Unassembled WGS sequence.
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; 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 {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};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 170..297
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 403..515
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 548..630
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 864..1030
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 1266..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 149022 MW; FC9ADE8A96853557 CRC64;
MNVFSVFKSS PSAEEDTEVA DTTYYVVFSE CVKDSVFWTV GAFAFTVLMI CLYRWRKWHV
ESLEKIAAKA LWMSGYENTP YRFRKRDKVM FYGRRMLRKM KSLSDQAYSG QGRKRRAVMR
FAKRILQMQK DNMPMQLKVL EPPAEFLEES HEGSLGMPPD VLYMLQSIRI FGHFEKPVFF
RLCKFTEVIS LQSGEYLFKI GDTDDSVYVV QTGSVNVSIN NADGTTMSLK IIRKGESVTS
LLSFIDVLAG SPSIYKTVTA RAMEPTQVIR LPMYAFKDVF SESPDLLVRV VQVIMVRLER
VTFTALRNYL GLHAELVYHA PKASKKPEKM KNSPGHRRTN STYLEEVMAL YGHSGDRPDM
LADLATTECA TGSCARKLSS TKMCDEKSIH YVYALDSFTR ELGLPDEDKH LLEGAMEVRE
YQPGDTIIRE GDNTDDVSLL FLLSGSLQVY QFRYTYSNNG NIKQENTEVH VLSIHPGEFD
GGLAVITGEA SLYTIRAKHF SRVAMLSRST VYNIMRERPT IVLDIANMVV RKLSPLVRQC
DFALDWMFLE SGRAVFRQDE QSDSTYIVLS GRVRSVATHA NGKKEIVGEY GKGDLVGLVE
MITDTTRTTT AMAVRDSELA KLPQGLFNAI KLRHPMVVTQ LFGLLSHRLL GSVQGRHSSR
MAPQTVEPTH IKHKYSTVAI VPVNEDVPLS AFTYELYHSL CAIGPTLRLT SDVVRKTLGA
NILDSANEYR LTSWLAQQED RNMIALYQCD NIVSPWTQRC WRQADVILIV GVGDHGPGVG
SMEREIDRLM LRTQKELVIL HPDNSTTKPT NTVQWLNMRS WVMKHHHIQC KKRMFTRKSQ
YRIPNLHSDF SRLARWLTGN SVGLVLGGGG ARGAAHVGML KAIQEAGIPI DMVGGVSIGA
FMGALWCSEK NITTVTQKAR EWSKKMTQWG RQLLDLTYPI TSMFSGRDFN KTIRDTFGEI
YIEDLWIPYF TLTTDITASC ARVHTHGSLW RYIRSSMSLS GYMPPLCDPK DGHLLLDGGY
VNNLPVSRKV VYCRASMSVA GIYPPFCDYT DGHLLLDGCY VNNVPADVLR AQGAAHIIAI
DVGSQDETNL TDYGDYLSGW WLIYKKFNPF TTPVKVPNLP DIQSRLAYVS CVRQLEEVKN
SDYCEYIRPP IDQYKTLAFG QFDTIKDVGF AHGKQVFENM AKSGRISFFN QWSLKDGGVP
KATPHSLNEY TFTDLAQIVC RVPETYTENQ YSSTDEDVYF DGYISEPSSL YPMGQPLKLK
RTGGSLSLSE NEMDSDELEV PTLLQLSGKT KERLESQEFE KKKATEENPQ IPTNSTTSQ
//
