LIP_RHINI
ID LIP_RHINI Reviewed; 392 AA.
AC P61871; O74166; P21811; Q12237;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Lipase II;
DE AltName: Full=RNL;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
OS Rhizopus niveus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10092492; DOI=10.1006/prep.1999.1029;
RA Kohno M., Enatsu M., Yoshiizumi M., Kugimiya W.;
RT "High-level expression of Rhizopus niveus lipase in the yeast Saccharomyces
RT cerevisiae and structural properties of the expressed enzyme.";
RL Protein Expr. Purif. 15:327-335(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kugimiya W., Kohno M., Sasaki M., Hashimoto Y., Morita Y.;
RT "Primary structure of Rhizopus niveus lipase from DNA and protein
RT analyses.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-392.
RX PubMed=1368341; DOI=10.1271/bbb.56.716;
RA Kugimiya W., Otani Y., Kohno M., Hashimoto Y.;
RT "Cloning and sequence analysis of cDNA encoding Rhizopus niveus lipase.";
RL Biosci. Biotechnol. Biochem. 56:716-719(1992).
RN [4]
RP PROTEIN SEQUENCE OF 44-53; 96-105 AND 124-134, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=NBRC 4759 / AS 3.4816;
RX PubMed=7765029; DOI=10.1271/bbb.58.1007;
RA Kohno M., Kugimiya W., Hashimoto Y., Morita Y.;
RT "Purification, characterization, and crystallization of two types of lipase
RT from Rhizopus niveus.";
RL Biosci. Biotechnol. Biochem. 58:1007-1012(1994).
RN [5]
RP MUTAGENESIS OF GLU-313, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11334664; DOI=10.1016/s0168-1656(01)00243-7;
RA Kohno M., Enatsu M., Funatsu J., Yoshiizumi M., Kugimiya W.;
RT "Improvement of the optimum temperature of lipase activity for Rhizopus
RT niveus by random mutagenesis and its structural interpretation.";
RL J. Biotechnol. 87:203-210(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 124-392, ACTIVE SITES, AND
RP DISULFIDE BOND.
RC STRAIN=NBRC 4759 / AS 3.4816;
RX PubMed=8902613; DOI=10.1093/oxfordjournals.jbchem.a021442;
RA Kohno M., Funatsu J., Mikami B., Kugimiya W., Matsuo T., Morita Y.;
RT "The crystal structure of lipase II from Rhizopus niveus at 2.2-A
RT resolution.";
RL J. Biochem. 120:505-510(1996).
CC -!- FUNCTION: Hydrolyzes ester bonds of triglycerides as well as of their
CC derived partial glycerides with a strong 1,3-positional specificity.
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 -!- ACTIVITY REGULATION: Lipase activity is maximal at a lipid-water
CC interface (interfacial activation), probably by an induced
CC conformational change that results in an increased accessibility of the
CC active site to the substrate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:11334664,
CC ECO:0000269|PubMed:7765029};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:11334664, ECO:0000269|PubMed:7765029};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- MISCELLANEOUS: Limited proteolysis produces a smaller peptide starting
CC at residue Ser-124, that has altered substrate specificity and
CC biophysicochemical properties.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase 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; AB013496; BAA31548.1; -; Genomic_DNA.
DR EMBL; D13206; BAA02493.1; -; Genomic_DNA.
DR EMBL; S39525; AAC60540.2; -; mRNA.
DR EMBL; D12680; BAA02181.1; -; mRNA.
DR PIR; JT0604; JT0604.
DR PIR; PC2171; PC2171.
DR PIR; PC2172; PC2172.
DR PDB; 1LGY; X-ray; 2.20 A; A/B/C=124-392.
DR PDBsum; 1LGY; -.
DR AlphaFoldDB; P61871; -.
DR SMR; P61871; -.
DR ESTHER; rhidl-lipas; Lipase_3.
DR EvolutionaryTrace; P61871; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..95
FT /evidence="ECO:0000269|PubMed:7765029"
FT /id="PRO_0000017733"
FT CHAIN 96..392
FT /note="Lipase"
FT /id="PRO_0000017734"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:8902613"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8902613"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8902613"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 152..391
FT /evidence="ECO:0000269|PubMed:8902613"
FT DISULFID 163..166
FT /evidence="ECO:0000269|PubMed:8902613"
FT DISULFID 358..367
FT /evidence="ECO:0000269|PubMed:8902613"
FT MUTAGEN 313
FT /note="E->V: Increases the optimum temperature to 50
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11334664"
FT CONFLICT 348
FT /note="I -> M (in Ref. 3; AAC60540/BAA02181)"
FT /evidence="ECO:0000305"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:1LGY"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1LGY"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1LGY"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 233..256
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:1LGY"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:1LGY"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1LGY"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1LGY"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1LGY"
SQ SEQUENCE 392 AA; 42139 MW; D08F651EE77AA5A3 CRC64;
MVSFISISQG VSLCLLVSSM MLGSSAVPVS GKSGSSNTAV SASDNAALPP LISSRCAPPS
NKGSKSDLQA EPYNMQKNTE WYESHGGNLT SIGKRDDNLV GGMTLDLPSD APPISLSSST
NSASDGGKVV AATTAQIQEF TKYAGIAATA YCRSVVPGNK WDCVQCQKWV PDGKIITTFT
SLLSDTNGYV LRSDKQKTIY LVFRGTNSFR SAITDIVFNF SDYKPVKGAK VHAGFLSSYE
QVVNDYFPVV QEQLTAHPTY KVIVTGHSLG GAQALLAGMD LYQREPRLSP KNLSIFTVGG
PRVGNPTFAY YVESTGIPFQ RTVHKRDIVP HVPPQSFGFL HPGVESWIKS GTSNVQICTS
EIETKDCSNS IVPFTSILDH LSYFDINEGS CL
