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Database: UniProt
Entry: A0A2A4IU41_HELVI
LinkDB: A0A2A4IU41_HELVI
Original site: A0A2A4IU41_HELVI 
ID   A0A2A4IU41_HELVI        Unreviewed;       427 AA.
AC   A0A2A4IU41;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=PLAT domain-containing protein {ECO:0000259|PROSITE:PS50095};
DE   Flags: Fragment;
GN   ORFNames=B5V51_13635 {ECO:0000313|EMBL:PCG62794.1};
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:PCG62794.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG62794.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG62794.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG62794.1};
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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:PCG62794.1}.
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DR   EMBL; NWSH01007821; PCG62794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4IU41; -.
DR   STRING; 7102.A0A2A4IU41; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF178; FI22312P1; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          389..427
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        230
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        318
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         249
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PCG62794.1"
FT   NON_TER         427
FT                   /evidence="ECO:0000313|EMBL:PCG62794.1"
SQ   SEQUENCE   427 AA;  46916 MW;  96766E10161FB72B CRC64;
     AELESWRGAG RPATAAQEAE DEKRDIELLE AVKESMKEWE QKRARTRSKR SQGSVCYGEF
     GCFEDAGPFA YLETLPSSPQ EVGTHFLLYS TVSRGDQPLL AVSASNMSAA WGWAARAFEP
     NRPTRVIVHG FGSNCDNVWV YEMRSALMAV EECNVVCVDW EGGASMPNYL RAAANTRLVG
     KQLAMLLQGF AKHIDLRFED VHLIGFSLGA HVAGFAGSEL RNISRITGLD PAGPLFEFQD
     PRARLDRSDA KFVDVIHSNG ETLILGGLGA AQPLGHVDFY PNGGRVQHGC SNLFVGAVSD
     FVLPWAAASP EGRSLCNHRR AYKFFTDSVS PKCHFPAFPC ADYDTFLEGR CFPCDGQRRC
     GNMGYYADRS LGRGQLYLLT REEEPFCAHQ YHVSVWAGSG SGDKANFGRV TLTLHGDSGL
     NESFPMT
//
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