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P07098 (LIPG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Gastric triacylglycerol lipase
Short name=Gastric lipase
Short name=GL
EC=3.1.1.3
Gene names
Name:LIPF
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Sequence caution

The sequence CAA29414.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride metabolic process Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlipid binding Ref.4

Non-traceable author statement. Source: UniProtKB

triglyceride lipase activity Ref.1

Traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.4
Chain20 – 398379Gastric triacylglycerol lipase
PRO_0000017766

Sites

Active site1721Nucleophile
Active site3431Charge relay system
Active site3721Charge relay system

Amino acid modifications

Glycosylation341N-linked (GlcNAc...)
Glycosylation991N-linked (GlcNAc...)
Glycosylation2711N-linked (GlcNAc...)
Glycosylation3271N-linked (GlcNAc...)
Disulfide bond246 ↔ 255

Natural variations

Natural variant1611T → A. [dbSNP:rs814628] Ref.2 Ref.3
VAR_011947
Natural variant2241F → I. [dbSNP:rs6586145] Ref.2
VAR_020565
Natural variant3481P → T. [dbSNP:rs17333991] Ref.2
VAR_020566

Secondary structure

1 ........................................................................ 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07098-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: CD3EE1621C014F0F

FASTA39845,238
        10         20         30         40         50         60 
MWLLLTMASL ISVLGTTHGL FGKLHPGSPE VTMNISQMIT YWGYPNEEYE VVTEDGYILE 

        70         80         90        100        110        120 
VNRIPYGKKN SGNTGQRPVV FLQHGLLASA TNWISNLPNN SLAFILADAG YDVWLGNSRG 

       130        140        150        160        170        180 
NTWARRNLYY SPDSVEFWAF SFDEMAKYDL PATIDFIVKK TGQKQLHYVG HSQGTTIGFI 

       190        200        210        220        230        240 
AFSTNPSLAK RIKTFYALAP VATVKYTKSL INKLRFVPQS LFKFIFGDKI FYPHNFFDQF 

       250        260        270        280        290        300 
LATEVCSREM LNLLCSNALF IICGFDSKNF NTSRLDVYLS HNPAGTSVQN MFHWTQAVKS 

       310        320        330        340        350        360 
GKFQAYDWGS PVQNRMHYDQ SQPPYYNVTA MNVPIAVWNG GKDLLADPQD VGLLLPKLPN 

       370        380        390 
LIYHKEIPFY NHLDFIWAMD APQEVYNDIV SMISEDKK

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a human gastric lipase and expression of the enzyme in yeast."
Bodmer M.W., Angal S., Yarranton G.T., Harris T.J.R., Lyons A., King D.J., Pieroni G., Riviere C., Verger R., Lowe P.A.
Biochim. Biophys. Acta 909:237-244(1987) [PubMed: 3304425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-161; ILE-224 AND THR-348.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-161.
[4]"Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity."
Bernbaeck S., Blaeckberg L.
Eur. J. Biochem. 182:495-499(1989) [PubMed: 2753032] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-45.
[5]"Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest."
Roussel A., Canaan S., Egloff M.P., Riviere M., Dupuis L., Verger R., Cambillau C.
J. Biol. Chem. 274:16995-17002(1999) [PubMed: 10358049] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X05997 mRNA. Translation: CAA29413.1.
X05997 mRNA. Translation: CAA29414.1. Different initiation.
AY631869 Genomic DNA. Translation: AAT38115.1.
BC112272 mRNA. Translation: AAI12273.1.
BC113711 mRNA. Translation: AAI13712.1.
IPIIPI00009893.
PIRS07145.
RefSeqNP_004181.1.
UniGeneHs.523130.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLGX-ray3.00A/B28-398[»]
ProteinModelPortalP07098.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07098.

PTM databases

PhosphoSiteP07098.

Proteomic databases

PRIDEP07098.

Genome annotation databases

EnsemblENST00000238983; ENSP00000238983; ENSG00000182333; Homo sapiens. [Genome view]
GeneID8513.
KEGGhsa:8513.
UCSCuc001kfg.1. human.

Organism-specific databases

CTD8513.
GeneCardsGC10P090415.
H-InvDBHIX0009012.
HGNCHGNC:6622. LIPF.
MIM601980. gene.
PharmGKBPA30394.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14370.
HOVERGENHBG006265.
InParanoidP07098.
OMAFYNHLDF.
OrthoDBEOG980MGD.
PhylomeDBP07098.

Enzyme and pathway databases

BRENDA3.1.1.3. 247.

Gene expression databases

ArrayExpressP07098.
BgeeP07098.
CleanExHS_LIPF.
GenevestigatorP07098.
GermOnlineENSG00000182333. Homo sapiens.

Family and domain databases

InterProIPR006693. AB_hydro-assoc_lipase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamPF04083. Abhydro_lipase. 1 hit.
PF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio31864.
PMAP-CutDBP07098.
SOURCESearch...

Entry information

Entry nameLIPG_HUMAN
AccessionPrimary (citable) accession number: P07098
Secondary accession number(s): Q2M1P6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: August 10, 2010
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents