ID E0VWM1_PEDHC Unreviewed; 1127 AA.
AC E0VWM1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEB17777.1};
GN Name=8231468 {ECO:0000313|EnsemblMetazoa:PHUM488870-PA};
GN ORFNames=Phum_PHUM488870 {ECO:0000313|EMBL:EEB17777.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB17777.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB17777.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB17777.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB17777.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM488870-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM488870-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR EMBL; AAZO01005921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAZO01005922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAZO01005923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235822; EEB17777.1; -; Genomic_DNA.
DR RefSeq; XP_002430515.1; XM_002430470.1.
DR AlphaFoldDB; E0VWM1; -.
DR STRING; 121224.E0VWM1; -.
DR EnsemblMetazoa; PHUM488870-RA; PHUM488870-PA; PHUM488870.
DR GeneID; 8231468; -.
DR KEGG; phu:Phum_PHUM488870; -.
DR CTD; 8231468; -.
DR VEuPathDB; VectorBase:PHUM488870; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; E0VWM1; -.
DR OMA; NCGPENL; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 3.
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; 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; 2.
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.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT DOMAIN 75..202
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 335..440
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 444..513
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 736..905
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 1060..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 771..775
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT COMPBIAS 1066..1081
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 773
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 892
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 1127 AA; 126769 MW; 941916A07751CBA8 CRC64;
MLRKVKSISG QVHQTKKRKL VMRFARRILH LKKDTSSMQL QVLEPPAEYL EEDITSKYDQ
GLPPDALYLL QSLRVFGHFE KPVFLMLCKH TEILTVPAGA FLFKIGDPDE NVYVVQSGCL
NVFITEHNGT MISLKYVKAG ESVTSLLSFT DVLTGSPSVY KTVSARAMED TTIVRLPIQA
FNEVFHDYPD IFIRVVQVIM VRLQRVTFTA LHQYLGLSAE LVRSNTHFVN NYQTINTSQK
SQRSSLGEEN NEVTKIRNVP FSGPLDFKII NQKFVPFSEI FLRQNAKIFA TNAGNQNAPI
ESEIQMTGHR RSMSGKVNSL AEDYDSLMQL AKAAFVRELN LENESILDGK IEIKDVPTGT
YLMRQDSHKD VALIYLLSGA LVLSQKMTDD QHEVHMFTAH PGEVIGGLAV LTGEPSFFTM
KAKHFSKIAM LSKSTFYEIV YLHKTVYILL FNNESVSQSS FICSPYRKLV GEYGKGDLVG
IVEMVTQTPR STTVMAVRDS ELAKLPEGLF NAIKLRFPIV VTRLINLLGH RLLGTKGHPG
VGLNPGAGAR PSQVNFSTVA IVPISDDVPL TAFGFELYHA LCAIGLTLRL TSDLIKKTLG
ATIMDPNNEY RLTSWLAQQE DQHKIALYQC DASLTPWTQR CVRQADCILI IGLAEKGPDL
GKMEKEVERL AVRTQKELVL LHRESTERPS NTVLWLNART WVSSHHHIKC NKRMFSRRSQ
YRINELYKKV LMSEPNIHSD FSRLARWLTG TSVGLVLGGG GAGIPIDMVG GVSIGSFVGG
LWAMEKTLRR DSKAREWSKK MTQWYRQILD LTYPVVSIFT GKDFNHTIYS TFGDINIEDL
WIPYFNVTTD ISASASRVHK HGFLWKYIRA SMSISGVLPP ICDPVDGHLL CDGCYVNNVP
ADVMRNEGAR HILAIDVGAH DDQDLTNYGD SLSGFWLLYK KWNPFTKPVK VPDLSDIQSR
LSYVCCVRQL EEVKNSDYCE YLRPPIDKYK TLQFALFDEI KEVGYTYGKT YFARLLKAGV
LPLFKTDIVA TRRPFASHPT YTFTDLAQMV CKVPRKHVTA DMSSSTSETE DDDDDDDDIN
VGYASEPSAF ILSKNSTANV PRRGQSLSEN ELDSETNFLT DEASDAR
//