P17573 (LIP1_GEOCN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipase 1
EC=3.1.1.3

Alternative name(s):
GCL I
Lipase I

Gene names

Name:

LIP1

Organism

Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum)

Taxonomic identifier

27317 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Galactomyces

Protein attributes

Sequence length	563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19
	Chain	20 – 563	544	Lipase 1		PRO_0000008624
Sites
	Active site	236	1	Acyl-ester intermediate By similarity
	Active site	373	1	Charge relay system By similarity
	Active site	482	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	20	1	Pyrrolidone carboxylic acid Ref.1
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	383	1	N-linked (GlcNAc...) Potential
	Disulfide bond	80 ↔ 124
	Disulfide bond	295 ↔ 307
Natural variations
	Natural variant	37	1	E → G in strain: NRRL Y-553.
	Natural variant	91	1	L → W in strain: NRRL Y-553.
	Natural variant	102	1	I → L in strain: NRCC 205002 and NRRL Y-553.
	Natural variant	201	1	N → S in strain: NRCC 205002.
	Natural variant	259	1	Q → K in strain: NRRL Y-553.
	Natural variant	297	1	A → T in strain: NRCC 205002.
	Natural variant	300	1	G → S in strain: NRCC 205002 and NRRL Y-553.
	Natural variant	303	1	E → D in strain: NRCC 205002.
	Natural variant	400	1	E → Q in strain: NRCC 205002.
	Natural variant	405	1	S → P in strain: NRRL Y-552.
	Natural variant	421	1	A → S in strain: NRCC 205002.
	Natural variant	520	1	K → Q in strain: NRCC 205002.
	Natural variant	528	1	S → A in strain: NRCC 205002, NRRL Y-552 and NRRL Y-553.
	Natural variant	538	1	I → V in strain: NRRL Y-553.
Experimental info
	Sequence conflict	170	1	V → L AA sequence Ref.1
	Sequence conflict	492 – 496	5	VDLGP → AGPWS AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17573 [UniParc]. Last modified February 16, 2004. Version 2. Checksum: 732E43AE060BB95F	FASTA	563	61,199
	10 20 30 40 50 60 MVSKTFFLAA ALNVVGTLAQ APTAVLNGNE VISGVLEGKV DTFKGIPFAD PPVGDLRFKH 70 80 90 100 110 120 PQPFTGSYQG LKANDFSSAC MQLDPGNAIS LLDKVVGLGK IIPDNLRGPL YDMAQGSVSM 130 140 150 160 170 180 NEDCLYLNVF RPAGTKPDAK LPVMVWIYGG AFVFGSSASY PGNGYVKESV EMGQPVVFVS 190 200 210 220 230 240 INYRTGPYGF LGGDAITAEG NTNAGLHDQR KGLEWVSDNI ANFGGDPDKV MIFGESAGAM 250 260 270 280 290 300 SVAHQLVAYG GDNTYNGKQL FHSAILQSGG PLPYFDSTSV GPESAYSRFA QYAGCDASAG 310 320 330 340 350 360 DNETLACLRS KSSDVLHSAQ NSYDLKDLFG LLPQFLGFGP RPDGNIIPDA AYELYRSGRY 370 380 390 400 410 420 AKVPYITGNQ EDEGTILAPV AINATTTPHV KKWLKYICSE ASDASLDRVL SLYPGSWSEG 430 440 450 460 470 480 APFRTGILNA LTPQFKRIAA IFTDLLFQSP RRVMLNATKD VNRWTYLATQ LHNLVPFLGT 490 500 510 520 530 540 FHGSDLLFQY YVDLGPSSAY RRYFISFANH HDPNVGTNLK QWDMYTDSGK EMLQIHMIGN 550 560 SMRTDDFRIE GISNFESDVT LFG

References

[1]	"cDNA molecular cloning of Geotrichum candidum lipase." Shimada Y., Sugihara A., Tominaga Y., Iizumi T., Tsunasawa S. J. Biochem. 106:383-388(1989) [PubMed: 2481674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE. Strain: ATCC 34614.
[2]	"Polymorphism in the lipase genes of Geotrichum candidum strains." Bertolini M.C., Laramee L., Thomas D.Y., Cygler M., Schrag J.D., Vernet T. Eur. J. Biochem. 219:119-125(1994) [PubMed: 8306978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 20-563. Strain: ATCC 34614, ATCC 74169 / NRRL Y-552 / ED00652, ATCC 90287 / NRRL Y-553 and NRCC 205002.
[3]	"Cloning and sequencing of two chromosomal lipase genes from Geotrichum candidum." Nagao T., Shimada Y., Sugihara A., Tominaga Y. J. Biochem. 113:776-780(1993) [PubMed: 8370674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-30 AND 551-563. Strain: ATCC 34614.
[4]	"Does sequence similarity of human choline esterase, Torpedo acetylcholine esterase and Geotrichum candidum lipase reveal the active site serine residue?" Slabas A.R., Windust J., Sidebottom C.M. Biochem. J. 269:279-280(1990) [PubMed: 2115773] [Abstract] Cited for: SIMILARITY TO CARBOXYLESTERASES.
[5]	"Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II." Bertolini M.C., Schrag J.D., Cygler M., Ziomek E., Thomas D.Y., Vernet T. Eur. J. Biochem. 228:863-869(1995) [PubMed: 7737187] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U02622 Unassigned DNA. Translation: AAA03435.1. U02387 Unassigned DNA. Translation: AAA03425.1. U02524 Unassigned DNA. Translation: AAA03428.1. U02525 Unassigned DNA. Translation: AAA03429.1. S65081 Genomic DNA. Translation: AAB28106.1. S65082 Genomic DNA. Translation: AAB28107.1.
PIR	ACGUGC. PN0492. S41090. S41091. S41092. S41093.
3D structure databases
ProteinModelPortal	P17573.
SMR	P17573. Positions 20-563.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIP1_GEOCN

Accession

Primary (citable) accession number: P17573
Secondary accession number(s): Q00882 , Q00883, Q00884, Q00886, Q02176, Q96WW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 16, 2004
Last modified:	May 31, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program