ID   A0A2T7P0P8_POMCA        Unreviewed;      1113 AA.
AC   A0A2T7P0P8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Hormone-sensitive lipase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_12146 {ECO:0000313|EMBL:PVD26997.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD26997.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD26997.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD26997.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD26997.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00010515}.
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:PVD26997.1}.
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DR   EMBL; PZQS01000007; PVD26997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7P0P8; -.
DR   STRING; 400727.A0A2T7P0P8; -.
DR   EnsemblMetazoa; XM_025244673.1; XP_025100458.1; LOC112567841.
DR   OrthoDB; 2941058at2759; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR010468; HSL_N.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR   PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   Pfam; PF06350; HSL_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          17..323
FT                   /note="Hormone-sensitive lipase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06350"
FT   DOMAIN          349..506
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          1024..1086
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   REGION          625..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ   SEQUENCE   1113 AA;  122882 MW;  FB902177F2708B13 CRC64;
     MDFDNSESPS KFFTSIVKEL KNIAISNIKY FKDGKQSHHA KFHVSFCLLF EYLDLGIEPC
     YREIDKRVHE FDASPKEKGN GYRSLLRIVQ KCCLHLLQLS RNISTNRDTI LFRRQFYMKE
     LEAYVATLGQ LRACLYYAQK LMTYCQPGNL FADEETLDEA VAEQLMADVE MLSQDCFYGR
     CLGFQFCESM QRPLQIVAIA MASFSEGYQE NSQIMKVATS LFNSPKYLIN PEVRAQQVVN
     ITRTADIQFC KAFWSITESE IMHPLPSLVY PNVQVDEVFH LGPDAFEMLS VNGEEITITP
     PCAHTGPAPV QVRLLSYQLR EGQEQHLKSS RSPGAKTPSP KTQRARGLLI HCHGGGFVAQ
     SSRSHEVYLR HWAKDLDVPI LSVDYSLAPE SPFPRALEEC FYAYAWAVHN CEKLGSTGEI
     ICMAGDSAGG NLVISTAMRA SSFNIRKPDG ILAVYTPVLV RYTPSPARLL SLMDPLLPAG
     ILSRCLAAYA GVSDELSSQL AASVTCHIES SAATLNMSSQ DVSESDWVLI SQDSAARVNT
     TLSTLQQKVQ MSGSSHLSSL ERNDSQEEVE LFMRPKIAVA SVASTVADAK DKIMSYVGSC
     SQILVNSLSG WSAEGEVCSK TLQAVSSPGE ESIEEESKQE ESLETPSFYT PLTSPDEGQE
     SLVSCDMVTG STPNDGTDRD LSDSYSESTS DMLESPDNFF SRKVSSEMKS NKDAGKKEGS
     EHDVPDGLLA SDLSFRHTCS RESDASLGKS FLALSSPCMP LLTEEKAQLL RQEVENSAFV
     PECEVEDQPE MSHSFIDDSS DMNVYEVLAD ENQTVVVTVY KEGIPPQDID NAEYVSSPLS
     EGAKQSSIKE VANLKENLQK SEETGITVTK HAKEDQLCSK DETFNLSDPS IISNFQIGSG
     LKTESISTAK SDLHFSTGNL SSDSGCLSDD TMRPGPSVSP SCILSEVTVM DSAVSPSHLR
     RMQLHLDLPT KSSKLSLPRS ASTPAFISPA DFSRYSPSMS PSDFKRERHL AQSPLRAIRH
     IPIVKNPYMS PLLAPDSLLE GLPYISLVAC HLDPLIDDSI MFTRRLRSLG KSIDLMMLDD
     LPHGFLNFSM LSQDAKRGSD ICVKKLKEML FPQ
//