ID H0V9V9_CAVPO Unreviewed; 397 AA.
AC H0V9V9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN Name=LIPF {ECO:0000313|Ensembl:ENSCPOP00000006616.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000006616.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000006616.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000006616.3};
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 EMBL; AAKN02020732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003473591.2; XM_003473543.3.
DR AlphaFoldDB; H0V9V9; -.
DR STRING; 10141.ENSCPOP00000006616; -.
DR Ensembl; ENSCPOT00000007411.3; ENSCPOP00000006616.3; ENSCPOG00000007339.4.
DR GeneID; 100724215; -.
DR KEGG; cpoc:100724215; -.
DR CTD; 8513; -.
DR VEuPathDB; HostDB:ENSCPOG00000007339; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000161066; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; H0V9V9; -.
DR OMA; WSRRNLY; -.
DR OrthoDB; 5474043at2759; -.
DR TreeFam; TF315485; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
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:SF15; GASTRIC TRIACYLGLYCEROL LIPASE; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..397
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011711834"
FT DOMAIN 81..376
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 397 AA; 45000 MW; 015E6CF286E6828F CRC64;
MWLLLTVTSL ISALGTTHGF LGKVADSPEV NMNISQMISY WGYPSEEYDV VTEDGYILGI
YRIPYGKKNS ENRGQRPVAF LQHGFLASAT NWIANLPNNS LAFILADAGF DVWLGNSRGN
TWSRRNLYYS PNSVEFWAFS FDEMAKYDLP ATIDFIVEKT GQEKLHYVGH SQGTTIGFIA
FSTNPTLAKK VKTFYALAPV ATVKYVTSPL KKLSYVPTSL LKLIFGEKLF MPHNFFDQLL
ATEICSREMV DRLCRNALFI FCGFDSKNFN TSRLDVYLSH NPAGTSVQDV LHWAQECRSG
KFQAFDWGSP YQNMLHFNQS TPPYYNVTAM SVPIAVWNGG QDMLADPRDV ANLLPKLSNL
IYHKEILPYN HLDFIWAMNA PQEVYNEIVS LMVEDKN
//
