ID A0A2A4K5R5_HELVI Unreviewed; 433 AA.
AC A0A2A4K5R5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN ORFNames=B5V51_795 {ECO:0000313|EMBL:PCG79409.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG79409.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG79409.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG79409.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG79409.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG79409.1}.
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; NWSH01000114; PCG79409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4K5R5; -.
DR STRING; 7102.A0A2A4K5R5; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF100; LIPASE-RELATED; 1.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000862};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..433
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012042737"
FT DOMAIN 54..116
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 433 AA; 48723 MW; B11507A36CF01DDA CRC64;
MGKMLHGGLY VVFATCVALA AARASLEGDQ IMEMLKSIDL RYSTDVAEDA RLDVPDLIRK
YRYPVEVHNV TTEDGYILQM HRIPHGRDAN NDPNRKRPVV FVMHGLLSSS ADFVIMGPGS
ALGYILAEEG FDVWMGNARG NYYSRRHIRL NPDAILSTAF WRFSWDEIGN IDVPTMIDYA
LEVSGQERLH YIGHSQGTTA FFVMGSMRPD YNEKVISMHA LAPVAYMANN RNLLLRVLAS
YSNNIESIAS LIGIGEFMPN SVVFTWAGQA MCRDEVIFQP ICSNILFLVG GWNEDQHNTT
MMPAIFGHTP AGASVRQFAH YGQGISDRGF RRYDQGSRLS NYRAYGSFRP PSYDLSKVTT
PVFLHYSDSD PLAHVNDVDR LFRELGRPIG KFRVPMSSFS HLDFIYAING KELLYDRVIN
LIKAMDVNAF GEV
//