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P16233 (LIPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pancreatic triacylglycerol lipase

Short name=PL
Short name=PTL
Short name=Pancreatic lipase
EC=3.1.1.3
Gene names
Name:PNLIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 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. Ref.8

Subcellular location

Secreted.

Induction

By colipase/CLPS in the presence of bile salts.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

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
Metal binding2041Calcium; via carbonyl oxygen
Metal binding2071Calcium; via carbonyl oxygen
Metal binding2091Calcium
Metal binding2121Calcium

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P16233 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]"Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[9]"Structure of human pancreatic lipase."
Winkler F.K., D'Arcy A., Hunziker W.
Nature 343:771-774(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[10]"Structure of the pancreatic lipase-procolipase complex."
van Tilbeurgh H., Sarda L., Verger R., Cambillau C.
Nature 359:159-162(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[11]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[12]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 354-465.
+Additional computationally mapped references.

Web resources

Wikipedia

Pancreatic lipase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AK313941 mRNA. Translation: BAG36659.1.
AL731653 Genomic DNA. Translation: CAH72667.1.
CH471066 Genomic DNA. Translation: EAW49451.1.
BC014309 mRNA. Translation: AAH14309.1.
CCDSCCDS7594.1.
PIRC43357.
RefSeqNP_000927.1. NM_000936.2.
UniGeneHs.501135.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ProteinModelPortalP16233.
SMRP16233. Positions 17-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111407. 2 interactions.
IntActP16233. 1 interaction.
MINTMINT-1179407.
STRING9606.ENSP00000358223.

Chemistry

BindingDBP16233.
ChEMBLCHEMBL1812.
DrugBankDB00522. Bentiromide.
DB01083. Orlistat.
GuidetoPHARMACOLOGY2590.

PTM databases

PhosphoSiteP16233.

Polymorphism databases

DMDM126318.

Proteomic databases

PaxDbP16233.
PRIDEP16233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369221; ENSP00000358223; ENSG00000175535.
GeneID5406.
KEGGhsa:5406.
UCSCuc001lcm.3. human.

Organism-specific databases

CTD5406.
GeneCardsGC10P118305.
HGNCHGNC:9155. PNLIP.
MIM246600. gene+phenotype.
neXtProtNX_P16233.
PharmGKBPA33478.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038552.
HOVERGENHBG003243.
InParanoidP16233.
KOK14073.
OMAVKFIWYN.
OrthoDBEOG7KSX8B.
PhylomeDBP16233.
TreeFamTF324997.

Enzyme and pathway databases

BioCycMetaCyc:HS10947-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP16233.
CleanExHS_PNLIP.
GenevestigatorP16233.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 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]
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPNLIP. human.
EvolutionaryTraceP16233.
GeneWikiPancreatic_lipase.
GenomeRNAi5406.
NextBio20931.
PROP16233.
SOURCESearch...

Entry information

Entry nameLIPP_HUMAN
AccessionPrimary (citable) accession number: P16233
Secondary accession number(s): Q5VSQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 10

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