ID   LIP3_MORS1              Reviewed;         315 AA.
AC   P24640;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lipase 3;
DE            EC=3.1.1.3;
DE   AltName: Full=Triacylglycerol lipase;
DE   Flags: Precursor;
GN   Name=lip3; Synonyms=L3;
OS   Moraxella sp. (strain TA144).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella; unclassified Moraxella.
OX   NCBI_TaxID=77152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2001407; DOI=10.1016/0167-4781(91)90073-u;
RA   Feller G., Thiry M., Gerday C.;
RT   "Nucleotide sequence of the lipase gene lip3 from the antarctic psychotroph
RT   Moraxella TA144.";
RL   Biochim. Biophys. Acta 1088:323-324(1991).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active at temperatures close to 0 degree Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X53869; CAA37863.1; -; Genomic_DNA.
DR   PIR; S14276; S14276.
DR   AlphaFoldDB; P24640; -.
DR   SMR; P24640; -.
DR   ESTHER; morsp-3lipa; ABHD6-Lip.
DR   GO; GO:0005886; C:plasma membrane; 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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein;
KW   Membrane; Palmitate; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..315
FT                   /note="Lipase 3"
FT                   /id="PRO_0000008547"
FT   DOMAIN          69..296
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   315 AA;  34774 MW;  9007D9741EE04DFB CRC64;
     MLLKRLGLAA LFSLSMVGCT TAPNTLAVNT TQKIIQYERS KSDLEVKSLT LASGDKMVYA
     ENDNVTGEPL LLIHGFGGNK DNFTRIADKL EGYHLIIPDL LGFGNSSKPM TADYRADAQA
     TRLHELMQAK GLASNTHVGG NSMGGAISVA YAAKYPKEIK SLWLVDTAGF WSAGVPKSLE
     GATLENNPLL INSKEDFYKM YDFVMYKPPY IPKSVKAVFA QERINNKALD TKILEQIVTD
     NVEERAKIIA KYNIPTLVVW GDKDQVIKPE TTELIKEIIP QAQVIMMNDV GHVPMVEAVK
     DTANDYKAFR DGLKK