LIP2_DIURU
ID LIP2_DIURU Reviewed; 548 AA.
AC P32946;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Lipase 2;
DE EC=3.1.1.3;
DE Flags: Precursor;
GN Name=LIP2;
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=1610906; DOI=10.1016/0167-4781(92)90085-e;
RA Longhi S., Fusetti F., Grandori R., Lotti M., Vanoni M., Alberghina L.;
RT "Cloning and nucleotide sequences of two lipase genes from Candida
RT cylindracea.";
RL Biochim. Biophys. Acta 1131:227-232(1992).
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 15-548, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-365.
RX PubMed=14499609; DOI=10.1016/j.jmb.2003.08.005;
RA Mancheno J.M., Pernas M.A., Martinez M.J., Ochoa B., Rua M.L.,
RA Hermoso J.A.;
RT "Structural insights into the lipase/esterase behavior in the Candida
RT rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A
RT resolution.";
RL J. Mol. Biol. 332:1059-1069(2003).
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}.
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DR EMBL; X64704; CAA45958.1; -; Genomic_DNA.
DR PIR; S32615; S32615.
DR PDB; 1GZ7; X-ray; 1.97 A; A/B/C/D=15-548.
DR PDBsum; 1GZ7; -.
DR AlphaFoldDB; P32946; -.
DR SMR; P32946; -.
DR ESTHER; canru-2lipa; Fungal_carboxylesterase_lipase.
DR iPTMnet; P32946; -.
DR EvolutionaryTrace; P32946; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Signal.
FT SIGNAL 1..14
FT CHAIN 15..548
FT /note="Lipase 2"
FT /id="PRO_0000008620"
FT ACT_SITE 223
FT /note="Acyl-ester intermediate"
FT ACT_SITE 355
FT /note="Charge relay system"
FT ACT_SITE 463
FT /note="Charge relay system"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14499609"
FT DISULFID 74..111
FT /evidence="ECO:0000269|PubMed:14499609"
FT DISULFID 282..291
FT /evidence="ECO:0000269|PubMed:14499609"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 191..206
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:1GZ7"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 483..491
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:1GZ7"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 533..540
FT /evidence="ECO:0007829|PDB:1GZ7"
FT HELIX 543..546
FT /evidence="ECO:0007829|PDB:1GZ7"
SQ SEQUENCE 548 AA; 58865 MW; E0DBCFF2501E7614 CRC64;
MKLCLLALGA AVAAAPTATL ANGDTITGLN AIVNEKFLGI PFAEPPVGTL RFKPPVPYSA
SLNGQQFTSY GPSCMQMNPM GSFEDTLPKN ARHLVLQSKI FQVVLPNDED CLTINVIRPP
GTRASAGLPV MLWIFGGGFE LGGSSLFPGD QMVAKSVLMG KPVIHVSMNY RVASWGFLAG
PDIQNEGSGN AGLHDQRLAM QWVADNIAGF GGDPSKVTIY GESAGSMSTF VHLVWNDGDN
TYNGKPLFRA AIMQSGCMVP SDPVDGTYGT EIYNQVVASA GCGSASDKLA CLRGLSQDTL
YQATSDTPGV LAYPSLRLSY LPRPDGTFIT DDMYALVRDG KYAHVPVIIG DQNDEGTLFG
LSSLNVTTDA QARAYFKQSF IHASDAEIDT LMAAYTSDIT QGSPFDTGIF NAITPQFKRI
SALLGDLAFT LARRYFLNYY QGGTKYSFLS KQLSGLPVLG TFHGNDIIWQ DYLVGSGSVI
YNNAFIAFAN DLDPNKAGLW TNWPTYTSSS QSGNNLMQIN GLGLYTGKDN FRPDAYSALF
SNPPSFFV
