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Database: UniProt
Entry: G3VFA2_SARHA
LinkDB: G3VFA2_SARHA
Original site: G3VFA2_SARHA 
ID   G3VFA2_SARHA            Unreviewed;       389 AA.
AC   G3VFA2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   Name=LOC100925402 {ECO:0000313|Ensembl:ENSSHAP00000001856.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000001856.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000001856.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000001856.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753;
CC         Evidence={ECO:0000256|ARBA:ARBA00000360};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932;
CC         Evidence={ECO:0000256|ARBA:ARBA00000360};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol +
CC         H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC         ChEBI:CHEBI:76979; Evidence={ECO:0000256|ARBA:ARBA00000773};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048;
CC         Evidence={ECO:0000256|ARBA:ARBA00000773};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001024};
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|PIRNR:PIRNR000862}.
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DR   AlphaFoldDB; G3VFA2; -.
DR   STRING; 9305.ENSSHAP00000001856; -.
DR   Ensembl; ENSSHAT00000001877.2; ENSSHAP00000001856.2; ENSSHAG00000001654.2.
DR   eggNOG; KOG2624; Eukaryota.
DR   GeneTree; ENSGT00940000154696; -.
DR   HOGENOM; CLU_010974_0_0_1; -.
DR   InParanoid; G3VFA2; -.
DR   TreeFam; TF315485; -.
DR   Proteomes; UP000007648; 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:SF15; GASTRIC TRIACYLGLYCEROL LIPASE; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000007648}.
FT   DOMAIN          26..87
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        161
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        335
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        364
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   389 AA;  44402 MW;  1DA46490BFFE51D8 CRC64;
     MSQALGTECI FYTHRLANPE VQMNVGQIIR HWGYPVEGYE VETKDSYILT LIRIPYGRMG
     NNMTAQRPVV FLQHGLLATS IIWVSNLPNN SLGFILADAG FDVWMGNSRG STYSRKHAFL
     PIDSKEYWAF SFDEMARYDL PASIDYIVKK TGQKIYYVGH SQGTLTGFLA FSTLPKIVQK
     VKTFFALAPV FYIRHIKSIP LLQIFSLRQP LFKILMGEKD FLPETALNRI LATTVCDNEI
     TSLLCGKIIF SLTGFDTKNL NMSRIDVYVA HFPGGTSAQN ILHYLQAFYE SRQILQAFDW
     GSEKENFAHY NQTIPPKYNV SKMKVPTALW SGGKDLLADP EDVSDLIPQI RSKIYHKTLP
     DYNHLDFIFG IDAPQEIYYE IIKMIKNTL
//
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