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Reviewed, UniProtKB/Swiss-Prot P16233 (LIPP_HUMAN)

Last modified June 16, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

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

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Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriacylglycerol lipase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Chain17 – 465449Pancreatic triacylglycerol lipase
PRO_0000017785

Regions

Domain355 – 465111PLAT

Sites

Active site1691Nucleophile
Active site1931Charge relay system
Active site2801Charge relay system

Amino acid modifications

Glycosylation1831N-linked (GlcNAc...)
Disulfide bond20 ↔ 26
Disulfide bond107 ↔ 118
Disulfide bond254 ↔ 278
Disulfide bond302 ↔ 313
Disulfide bond316 ↔ 321
Disulfide bond449 ↔ 465

Secondary structure

1 .................................................................................... 465
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P16233-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 2BC49CC7F0E2DF52

FASTA46551,157
        10         20         30         40         50         60 
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN 

        70         80         90        100        110        120 
ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC 

       130        140        150        160        170        180 
VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR 

       190        200        210        220        230        240 
RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH 

       250        260        270        280        290        300 
LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF 

       310        320        330        340        350        360 
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS 

       370        380        390        400        410        420 
VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY 

       430        440        450        460 
NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of human pancreatic lipase cDNA."
Lowe M.E., Rosenblum J.L., Strauss A.W.
J. Biol. Chem. 264:20042-20048(1989) [PubMed: 2479644] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity."
Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.
J. Biol. Chem. 267:16509-16516(1992) [PubMed: 1379598] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[3]"The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family."
Sims H.F., Jennens M.L., Lowe M.E.
Gene 131:281-285(1993) [PubMed: 8406023] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
Tissue: Lung.
[5]"Structure of human pancreatic lipase."
Winkler F.K., D'Arcy A., Hunziker W.
Nature 343:771-774(1990) [PubMed: 2106079] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[6]"Structure of the pancreatic lipase-procolipase complex."
van Tilbeurgh H., Sarda L., Verger R., Cambillau C.
Nature 359:159-162(1992) [PubMed: 1522902] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[7]"Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography."
van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C.
Nature 362:814-820(1993) [PubMed: 8479519] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[8]"Structure-function relationships in naturally occurring mutants of pancreatic lipase."
Carriere F., Thirstrup K., Boel E., Verger R., Thim L.
Protein Eng. 7:563-569(1994) [PubMed: 8029213] [Abstract]
Cited for: STRUCTURE BY NMR OF 354-465.
+Additional computationally mapped references.

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Web resources

Wikipedia

Pancreatic lipase entry

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Cross-references

Sequence databases

J05125 mRNA. Translation: AAA36740.1.
M93285 mRNA. Translation: AAA60129.1.
L24529 expand/collapse EMBL AC list , L11242, L24502, L24522, L24523, L24525, L24526, L24527, L24528 Genomic DNA. Translation: AAA99053.1.
BC014309 mRNA. Translation: AAH14309.1.
IPIIPI00027720.
PIRC43357.
RefSeqNP_000927.1.
UniGeneHs.501135

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GPLX-ray2.01A18-465[»]
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ModBaseSearch...

Proteomic databases

PRIDEP16233.

Genome annotation databases

EnsemblENSG00000175535. Homo sapiens. [Contig view]
GeneID5406.
KEGGhsa:5406.

Organism-specific databases

GeneCardsGC10P118295.
H-InvDBHIX0009235.
HGNCHGNC:9155. PNLIP.
MIM246600. gene+phenotype.
PharmGKBPA33478.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP16233.
HOVERGENP16233.
OMAP16233. YEIFKGT.

Enzyme and pathway databases

BRENDA3.1.1.3. 247.
ReactomeREACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpressP16233.
BgeeP16233.
CleanExHS_PNLIP.
GermOnlineENSG00000175535. Homo sapiens.

Family and domain databases

InterProIPR000734. Lipase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHERPTHR11610. Lipase. 1 hit.
PTHR11610:SF8. Lipase_panc. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00522. Bentiromide.
DB01083. Orlistat.
NextBio20931.
SOURCESearch...

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Entry information

Entry nameLIPP_HUMAN
AccessionPrimary (citable) accession number: P16233
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 10

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

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents