LIP4_DIURU
ID LIP4_DIURU Reviewed; 549 AA.
AC P32948;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Lipase 4;
DE EC=3.1.1.3;
DE Flags: Precursor;
GN Name=LIP4;
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 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 -!- SIMILARITY: Belongs to the type-B carboxylesterase/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; X66007; CAA46806.1; -; Genomic_DNA.
DR PIR; JN0552; JN0552.
DR AlphaFoldDB; P32948; -.
DR SMR; P32948; -.
DR ESTHER; canru-4lipa; Fungal_carboxylesterase_lipase.
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; 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Signal.
FT SIGNAL 1..15
FT CHAIN 16..549
FT /note="Lipase 4"
FT /id="PRO_0000008622"
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 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"
SQ SEQUENCE 549 AA; 58571 MW; 39C7160852F7E655 CRC64;
MKLALVLSLI VSVAAAPTAT LANGDTITGL NAIINEAFLG IPFAQPPVGN LRFKPPVPYS
ASLNGQKFTS YGPSCMQMNP LGNWDSSLPK AAINSLMQSK LFQAVLPNGE DCLTINVVRP
SGTKPGANLP VMVWIFGGGF EVGGSSLFPP AQMITASVLM GKPIIHVSMN YRVASWGFLA
GPDIKAEGSG NAGLHDQRLG LQWVADNIAG FGGDPSKVTI FGESAGSMSV MCQLLWNDGD
NTYNGKPLFR AAIMQSGAMV PSDPVDGPYG TQIYDQVVAS AGCGSASDKL ACLRSISNDK
LFQATSDTPG ALAYPSLRLS FLPRPDGTFI TDDMFKLVRD GKCANVPVII GDQNDEGTVF
ALSSLNVTTD AQARQYFKES FIHASDAEID TLMAAYPSDI TQGSPFDTGI FNAITPQFKR
IAAVLGDLAF TLPRRYFLNH FQGGTKYSFL SKQLSGLPVI GTHHANDIVW QDFLVSHSSA
VYNNAFIAFA NDLDPNKAGL LVNWPKYTSS SQSGNNLLQI NALGLYTGKD NFRTAGYDAL
FTNPSSFFV