LIP3_DIURU
ID LIP3_DIURU Reviewed; 549 AA.
AC P32947;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Lipase 3;
DE EC=3.1.1.3;
DE AltName: Full=Cholesterol esterase;
DE Flags: Precursor;
GN Name=LIP3;
OS Diutina rugosa (Yeast) (Candida rugosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Diutina.
OX NCBI_TaxID=5481;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506;
RX PubMed=8440480; DOI=10.1016/0378-1119(93)90760-z;
RA Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A.,
RA Alberghina L.;
RT "Cloning and analysis of Candida cylindracea lipase sequences.";
RL Gene 124:45-55(1993).
RN [2]
RP PROTEIN SEQUENCE OF 16-549, AND SUBUNIT STRUCTURE.
RX PubMed=8287964; DOI=10.1016/0014-5793(94)80257-2;
RA Kaiser R., Erman M., Duax W.L., Ghosh D., Joernvall H.;
RT "Monomeric and dimeric forms of cholesterol esterase from Candida
RT cylindracea. Primary structure, identity in peptide patterns, and
RT additional microheterogeneity.";
RL FEBS Lett. 337:123-127(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7788294; DOI=10.1016/s0969-2126(01)00158-7;
RA Ghosh D., Wawrzak Z., Pletnev V.Z., Li N., Kaiser R., Pangborn W.,
RA Joernvall H., Erman M., Duax W.L.;
RT "Structure of uncomplexed and linoleate-bound Candida cylindracea
RT cholesterol esterase.";
RL Structure 3:279-288(1995).
RN [4]
RP REVIEW.
RX PubMed=9778794;
RX DOI=10.1002/(sici)1097-0061(19980915)14:12<1069::aid-yea303>3.0.co;2-k;
RA Benjamin S., Pandey A.;
RT "Candida rugosa lipases: molecular biology and versatility in
RT biotechnology.";
RL Yeast 14:1069-1087(1998).
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 -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:8287964}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X66006; CAA46805.1; -; Genomic_DNA.
DR PIR; JN0551; JN0551.
DR PIR; S41735; S41735.
DR PDB; 1CLE; X-ray; 2.00 A; A/B=16-549.
DR PDB; 1LLF; X-ray; 1.40 A; A/B=16-549.
DR PDBsum; 1CLE; -.
DR PDBsum; 1LLF; -.
DR AlphaFoldDB; P32947; -.
DR SMR; P32947; -.
DR DrugBank; DB02092; Cholesteryl Linoleate.
DR DrugBank; DB03500; Tricosanoic acid.
DR ESTHER; canru-3lipa; Fungal_carboxylesterase_lipase.
DR BRENDA; 3.1.1.3; 1139.
DR EvolutionaryTrace; P32947; -.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
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; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cholesterol metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Signal; Steroid metabolism; Sterol metabolism.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:8287964"
FT CHAIN 16..549
FT /note="Lipase 3"
FT /id="PRO_0000008621"
FT ACT_SITE 224
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..112
FT /evidence="ECO:0000250"
FT DISULFID 283..292
FT /evidence="ECO:0000250"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:1CLE"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 466..472
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:1CLE"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:1CLE"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:1CLE"
SQ SEQUENCE 549 AA; 58755 MW; C5F95C31422975DA CRC64;
MKLALALSLI ASVAAAPTAK LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYS
GSLNGQKFTS YGPSCMQQNP EGTFEENLGK TALDLVMQSK VFQAVLPQSE DCLTINVVRP
PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVTKSVLM GKPIIHVAVN YRVASWGFLA
GDDIKAEGSG NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLIWNDGD
NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG NEIYDLFVSS AGCGSASDKL ACLRSASSDT
LLDATNNTPG FLAYSSLRLS YLPRPDGKNI TDDMYKLVRD GKYASVPVII GDQNDEGTIF
GLSSLNVTTN AQARAYFKQS FIHASDAEID TLMAAYPQDI TQGSPFDTGI FNAITPQFKR
ISAVLGDLAF IHARRYFLNH FQGGTKYSFL SKQLSGLPIM GTFHANDIVW QDYLLGSGSV
IYNNAFIAFA TDLDPNTAGL LVNWPKYTSS SQSGNNLMMI NALGLYTGKD NFRTAGYDAL
MTNPSSFFV
