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P16233

- LIPP_HUMAN

UniProt

P16233 - LIPP_HUMAN

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Protein
Pancreatic triacylglycerol lipase
Gene
PNLIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691Nucleophile
Active sitei193 – 1931Charge relay system
Metal bindingi204 – 2041Calcium; via carbonyl oxygen
Metal bindingi207 – 2071Calcium; via carbonyl oxygen
Metal bindingi209 – 2091Calcium
Metal bindingi212 – 2121Calcium
Active sitei280 – 2801Charge relay system

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. triglyceride lipase activity Source: ProtInc

GO - Biological processi

  1. intestinal cholesterol absorption Source: Ensembl
  2. lipid catabolic process Source: UniProtKB-KW
  3. lipid digestion Source: Reactome
  4. phototransduction, visible light Source: Reactome
  5. retinoid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10947-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic triacylglycerol lipase (EC:3.1.1.3)
Short name:
PL
Short name:
PTL
Short name:
Pancreatic lipase
Gene namesi
Name:PNLIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9155. PNLIP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

MIMi246600. gene+phenotype.
PharmGKBiPA33478.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616
Add
BLAST
Chaini17 – 465449Pancreatic triacylglycerol lipase
PRO_0000017785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 26
Disulfide bondi107 ↔ 118
Glycosylationi183 – 1831N-linked (GlcNAc...)
Disulfide bondi254 ↔ 278
Disulfide bondi302 ↔ 313
Disulfide bondi316 ↔ 321
Disulfide bondi449 ↔ 465

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16233.
PRIDEiP16233.

PTM databases

PhosphoSiteiP16233.

Expressioni

Inductioni

By colipase/CLPS in the presence of bile salts.

Gene expression databases

BgeeiP16233.
CleanExiHS_PNLIP.
GenevestigatoriP16233.

Interactioni

Protein-protein interaction databases

BioGridi111407. 2 interactions.
IntActiP16233. 1 interaction.
MINTiMINT-1179407.
STRINGi9606.ENSP00000358223.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 214
Turni22 – 243
Beta strandi25 – 284
Turni31 – 333
Beta strandi34 – 385
Helixi48 – 514
Beta strandi54 – 585
Beta strandi60 – 656
Beta strandi67 – 693
Helixi73 – 786
Beta strandi87 – 915
Helixi101 – 11010
Turni111 – 1133
Beta strandi117 – 1226
Helixi124 – 1274
Helixi131 – 15626
Helixi160 – 1623
Beta strandi163 – 1686
Helixi170 – 18011
Turni181 – 1844
Beta strandi186 – 1938
Turni197 – 2015
Turni204 – 2063
Helixi210 – 2123
Beta strandi216 – 2194
Turni227 – 2293
Beta strandi239 – 2457
Beta strandi248 – 2503
Helixi258 – 2625
Helixi268 – 29124
Turni294 – 2974
Helixi305 – 3095
Beta strandi323 – 3253
Helixi328 – 3303
Turni332 – 3354
Beta strandi336 – 3449
Beta strandi348 – 3514
Beta strandi355 – 36511
Beta strandi368 – 37811
Beta strandi386 – 3938
Beta strandi398 – 40710
Beta strandi411 – 42010
Beta strandi431 – 44010
Beta strandi445 – 4495
Beta strandi460 – 4645

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ProteinModelPortaliP16233.
SMRiP16233. Positions 17-465.

Miscellaneous databases

EvolutionaryTraceiP16233.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 465111PLAT
Add
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP16233.
KOiK14073.
OMAiVKFIWYN.
OrthoDBiEOG7KSX8B.
PhylomeDBiP16233.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16233-1 [UniParc]FASTAAdd to Basket

« Hide

MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD    50
VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE 100
NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE 150
FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ 200
GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE 250
MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF 300
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS 350
NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS 400
NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS 450
PETVREEVLL TLTPC 465
Length:465
Mass (Da):51,157
Last modified:April 1, 1990 - v1
Checksum:i2BC49CC7F0E2DF52
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05125 mRNA. Translation: AAA36740.1.
M93285 mRNA. Translation: AAA60129.1.
L24529
, 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.
CCDSiCCDS7594.1.
PIRiC43357.
RefSeqiNP_000927.1. NM_000936.2.
UniGeneiHs.501135.

Genome annotation databases

EnsembliENST00000369221; ENSP00000358223; ENSG00000175535.
GeneIDi5406.
KEGGihsa:5406.
UCSCiuc001lcm.3. human.

Polymorphism databases

DMDMi126318.

Cross-referencesi

Web resourcesi

Wikipedia

Pancreatic lipase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05125 mRNA. Translation: AAA36740.1 .
M93285 mRNA. Translation: AAA60129.1 .
L24529
, 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 .
CCDSi CCDS7594.1.
PIRi C43357.
RefSeqi NP_000927.1. NM_000936.2.
UniGenei Hs.501135.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LPA X-ray 3.04 B 17-465 [» ]
1LPB X-ray 2.46 B 17-465 [» ]
1N8S X-ray 3.04 A 17-465 [» ]
ProteinModelPortali P16233.
SMRi P16233. Positions 17-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111407. 2 interactions.
IntActi P16233. 1 interaction.
MINTi MINT-1179407.
STRINGi 9606.ENSP00000358223.

Chemistry

BindingDBi P16233.
ChEMBLi CHEMBL1812.
DrugBanki DB00522. Bentiromide.
DB01083. Orlistat.
GuidetoPHARMACOLOGYi 2590.

PTM databases

PhosphoSitei P16233.

Polymorphism databases

DMDMi 126318.

Proteomic databases

PaxDbi P16233.
PRIDEi P16233.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369221 ; ENSP00000358223 ; ENSG00000175535 .
GeneIDi 5406.
KEGGi hsa:5406.
UCSCi uc001lcm.3. human.

Organism-specific databases

CTDi 5406.
GeneCardsi GC10P118305.
HGNCi HGNC:9155. PNLIP.
MIMi 246600. gene+phenotype.
neXtProti NX_P16233.
PharmGKBi PA33478.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40923.
HOGENOMi HOG000038552.
HOVERGENi HBG003243.
InParanoidi P16233.
KOi K14073.
OMAi VKFIWYN.
OrthoDBi EOG7KSX8B.
PhylomeDBi P16233.
TreeFami TF324997.

Enzyme and pathway databases

BioCyci MetaCyc:HS10947-MONOMER.
Reactomei REACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.

Miscellaneous databases

ChiTaRSi PNLIP. human.
EvolutionaryTracei P16233.
GeneWikii Pancreatic_lipase.
GenomeRNAii 5406.
NextBioi 20931.
PROi P16233.
SOURCEi Search...

Gene expression databases

Bgeei P16233.
CleanExi HS_PNLIP.
Genevestigatori P16233.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiLIPP_HUMAN
AccessioniPrimary (citable) accession number: P16233
Secondary accession number(s): Q5VSQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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