ID A0A1I8PPC7_STOCA Unreviewed; 460 AA.
AC A0A1I8PPC7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Lipase domain-containing protein {ECO:0000259|Pfam:PF00151};
GN Name=106086197 {ECO:0000313|EnsemblMetazoa:SCAU009931-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU009931-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU009931-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU009931-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR RefSeq; XP_013106220.1; XM_013250766.1.
DR AlphaFoldDB; A0A1I8PPC7; -.
DR STRING; 35570.A0A1I8PPC7; -.
DR EnsemblMetazoa; SCAU009931-RA; SCAU009931-PA; SCAU009931.
DR KEGG; scac:106086197; -.
DR VEuPathDB; VectorBase:SCAU009931; -.
DR OrthoDB; 3120262at2759; -.
DR Proteomes; UP000095300; 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; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF151; LIPASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 2.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 29..315
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 460 AA; 52081 MW; BA5BBDD7A99880E0 CRC64;
MAPAAATTTM PPKNRDIQLG PCLWAIDRKC PDKDITFYLY TRKNPADRQY IQVDGTLQDS
NLTESFFDKN HPSKILIHGY NADMFLHPLY MMKNDYIFTE YLAKGDYNVF FVDWSKLAIG
PCYTSAVHNL RHSGACVAQL VQRIVDTGTT DIHVIGFSLG GQLGNYIANK LDSFLLPRIT
ALDPAMPLFV TSSKQDKLDP SDAEFVDVIH TNALVQGKME RCGHADFYIN GGIVQPGCNA
DNPINPFACS HHRSIDYYLE SIRSTKGFWG WACSSYMAYL LGMCPPTNYL LEAGENTKKT
TKGMFFVTTN EKSPYAQGKW TDLPTLGVKK PIASQSPPSI TIMQPPQRGD PLLKNIDPWG
KLDYNFNNFH EHEIGSLYYD HDPYLHNWTY FNDGESTENT NDLNDNSVEE QDMNEYSYVK
VENDSEEINQ ADFPWQEYKR NASEGFIESS LFGLPTLDRG
//
