LIP1_GEOFE
ID LIP1_GEOFE Reviewed; 563 AA.
AC P79066;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Lipase 1;
DE EC=3.1.1.3;
DE AltName: Full=Lipase I;
DE AltName: Full=TFL I;
DE Flags: Precursor;
GN Name=LIP1;
OS Geotrichum fermentans (Trichosporon fermentans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Dipodascus.
OX NCBI_TaxID=44066;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=WU-C12;
RX PubMed=9228786; DOI=10.1111/j.1574-6968.1997.tb10426.x;
RA Arai T., Yusa S., Kirimura K., Usami S.;
RT "Cloning and sequencing of the cDNA encoding lipase I from Trichosporon
RT fermentans WU-C12.";
RL FEMS Microbiol. Lett. 152:183-188(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-563, DISULFIDE BONDS, ACTIVE
RP SITE, PYROGLUTAMATE FORMATION AT GLN-20, AND GLYCOSYLATION AT ASN-302 AND
RP ASN-383.
RX PubMed=8464065; DOI=10.1006/jmbi.1993.1171;
RA Schrag J.D., Cygler M.;
RT "1.8 A refined structure of the lipase from Geotrichum candidum.";
RL J. Mol. Biol. 230:575-591(1993).
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: Homotrimer. {ECO:0000269|PubMed:9228786}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AB000260; BAA19072.1; -; mRNA.
DR PDB; 1THG; X-ray; 1.80 A; A=21-563.
DR PDBsum; 1THG; -.
DR AlphaFoldDB; P79066; -.
DR SMR; P79066; -.
DR ESTHER; geoca-2lipa; Fungal_carboxylesterase_lipase.
DR iPTMnet; P79066; -.
DR EvolutionaryTrace; P79066; -.
DR GO; GO:0005576; C:extracellular region; 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; 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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..563
FT /note="Lipase 1"
FT /id="PRO_0000008626"
FT ACT_SITE 236
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039,
FT ECO:0000269|PubMed:8464065"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:8464065"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:8464065"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8464065"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8464065"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8464065"
FT DISULFID 80..124
FT /evidence="ECO:0000269|PubMed:8464065"
FT DISULFID 295..307
FT /evidence="ECO:0000269|PubMed:8464065"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 373..377
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 470..474
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 486..490
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:1THG"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:1THG"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:1THG"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:1THG"
SQ SEQUENCE 563 AA; 61548 MW; 210A12C206F33881 CRC64;
MVSKSLFLAA AVNLAGVLAQ APTAVLNGNE VISGVLEGKV DTFKGIPFAD PPLNDLRFKH
PQPFTGSYQG LKANDFSPAC MQLDPGNSLT LLDKALGLAK VIPEEFRGPL YDMAKGTVSM
NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG AFVYGSSAAY PGNSYVKESI NMGQPVVFVS
INYRTGPFGF LGGDAITAEG NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM
SVAHQLIAYG GDNTYNGKKL FHSAILQSGG PLPYHDSSSV GPDISYNRFA QYAGCDTSAS
ANDTLECLRS KSSSVLHDAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA AYELFRSGRY
AKVPYISGNQ EDEGTAFAPV ALNATTTPHV KKWLQYIFYD ASEASIDRVL SLYPQTLSVG
SPFRTGILNA LTPQFKRVAA ILSDMLFQSP RRVMLSATKD VNRWTYLSTH LHNLVPFLGT
FHGNELIFQF NVNIGPANSY LRYFISFANH HDPNVGTNLL QWDQYTDEGK EMLEIHMTDN
VMRTDDYRIE GISNFETDVN LYG
