ID   W8C9S7_CERCA            Unreviewed;       421 AA.
AC   W8C9S7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   Name=LIP3 {ECO:0000313|EMBL:JAC00170.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC00170.1};
RN   [1] {ECO:0000313|EMBL:JAC00170.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAC00170.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR   EMBL; GAMC01006386; JAC00170.1; -; mRNA.
DR   AlphaFoldDB; W8C9S7; -.
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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF100; LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          81..213
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        176
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        355
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        385
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   421 AA;  48316 MW;  900F98C4F1A7B629 CRC64;
     MKFSLKFNEI YQLLLFAVLI VALNWCFTST DTNFTPRSIA QNNYPVEEHI VPTTDGYLLS
     IYRIPAATKA NTTPPKKTSE VVLLQHGFTL SSDVWLLRGP KNDLPYLLAE AGYDVWLGNH
     RGNEYGRKHI SLDPKRDRQH FWNFTWHEMG YYDLANTIDY MREATGQKSV HYVGYSQGGL
     VALVLLTTRP EYAAKFKSMQ FTAPTVYMEN IKVPLPTAWI SGLGNYFSRF LEWWGHSETL
     QHARWNFHKQ MCSVLCDDGA WLRPIYLKIF SMFGGPVDAS ENYEHILTKM CGNVPVGASS
     KQVLHYVQQY VTGGFNQFDY GTVDSNIRQY GQPSPPSYNV SSVRNCISLY YSETDYMCAA
     EDVRRLGRDL QCAELNRMPY TAWNHGDFVW SRYARKALHE PIIARISSWS EAAGDRAEVK
     N
//