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Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei169Nucleophile1
Active sitei193Charge relay system1
Metal bindingi204Calcium; via carbonyl oxygen1
Metal bindingi207Calcium; via carbonyl oxygen1
Metal bindingi209Calcium1
Metal bindingi212Calcium1
Active sitei280Charge relay system1

GO - Molecular functioni

  • lipase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  • intestinal cholesterol absorption Source: Ensembl
  • lipid catabolic process Source: UniProtKB-KW
  • lipid metabolic process Source: UniProtKB
  • positive regulation of triglyceride lipase activity Source: CACAO

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10947-MONOMER
ReactomeiR-HSA-192456 Digestion of dietary lipid
R-HSA-975634 Retinoid metabolism and transport
SABIO-RKiP16233

Protein family/group databases

ESTHERihuman-PNLIP Pancreatic_lipase

Chemistry databases

SwissLipidsiSLP:000000529

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000175535.6
HGNCiHGNC:9155 PNLIP
MIMi246600 gene
neXtProtiNX_P16233

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Pancreatic lipase deficiency (PNLIPD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by exocrine pancreatic failure. Clinical findings include oily/greasy stools from infancy or early childhood, absence of discernible pancreatic disease, and significantly decreased pancreatic lipolytic activity.
See also OMIM:614338
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078977221T → M in PNLIPD; loss of function in lipid catabolic process; the mutant is not secreted. 2 PublicationsCorresponds to variant dbSNP:rs746000327EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5406
MalaCardsiPNLIP
MIMi614338 phenotype
OpenTargetsiENSG00000175535
PharmGKBiPA33478

Chemistry databases

ChEMBLiCHEMBL1812
DrugBankiDB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane
DB08909 Glycerol Phenylbutyrate
DB08222 METHOXYUNDECYLPHOSPHINIC ACID
DB01083 Orlistat
GuidetoPHARMACOLOGYi2590

Polymorphism and mutation databases

BioMutaiPNLIP
DMDMi126318

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Add BLAST16
ChainiPRO_000001778517 – 465Pancreatic triacylglycerol lipaseAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 26
Disulfide bondi107 ↔ 118
Glycosylationi183N-linked (GlcNAc...) asparagine1
Disulfide bondi254 ↔ 278
Disulfide bondi302 ↔ 313
Disulfide bondi316 ↔ 321
Disulfide bondi449 ↔ 465

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16233
PeptideAtlasiP16233
PRIDEiP16233
ProteomicsDBi53327

PTM databases

iPTMnetiP16233
PhosphoSitePlusiP16233

Expressioni

Inductioni

By colipase/CLPS in the presence of bile salts.

Gene expression databases

BgeeiENSG00000175535
CleanExiHS_PNLIP
GenevisibleiP16233 HS

Organism-specific databases

HPAiHPA062430
HPA062494

Interactioni

Protein-protein interaction databases

BioGridi111407, 10 interactors
IntActiP16233, 1 interactor
MINTiP16233
STRINGi9606.ENSP00000358223

Chemistry databases

BindingDBiP16233

Structurei

Secondary structure

1465
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 21Combined sources4
Turni22 – 24Combined sources3
Beta strandi25 – 28Combined sources4
Turni31 – 33Combined sources3
Beta strandi34 – 38Combined sources5
Helixi48 – 51Combined sources4
Beta strandi54 – 58Combined sources5
Beta strandi60 – 65Combined sources6
Beta strandi67 – 69Combined sources3
Helixi73 – 78Combined sources6
Beta strandi87 – 91Combined sources5
Helixi101 – 110Combined sources10
Turni111 – 113Combined sources3
Beta strandi117 – 122Combined sources6
Helixi124 – 127Combined sources4
Helixi131 – 156Combined sources26
Helixi160 – 162Combined sources3
Beta strandi163 – 168Combined sources6
Helixi170 – 180Combined sources11
Turni181 – 184Combined sources4
Beta strandi186 – 193Combined sources8
Turni197 – 201Combined sources5
Turni204 – 206Combined sources3
Helixi210 – 212Combined sources3
Beta strandi216 – 219Combined sources4
Turni227 – 229Combined sources3
Beta strandi239 – 245Combined sources7
Beta strandi248 – 250Combined sources3
Helixi258 – 262Combined sources5
Helixi268 – 291Combined sources24
Turni294 – 297Combined sources4
Helixi305 – 309Combined sources5
Beta strandi323 – 325Combined sources3
Helixi328 – 330Combined sources3
Turni332 – 335Combined sources4
Beta strandi336 – 344Combined sources9
Beta strandi348 – 351Combined sources4
Beta strandi355 – 365Combined sources11
Beta strandi368 – 378Combined sources11
Beta strandi386 – 393Combined sources8
Beta strandi398 – 407Combined sources10
Beta strandi411 – 420Combined sources10
Beta strandi431 – 440Combined sources10
Beta strandi445 – 449Combined sources5
Beta strandi460 – 464Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ProteinModelPortaliP16233
SMRiP16233
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16233

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini355 – 465PLATPROSITE-ProRule annotationAdd BLAST111

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHRX Eukaryota
ENOG410Y92X LUCA
GeneTreeiENSGT00760000119069
HOGENOMiHOG000038552
HOVERGENiHBG003243
InParanoidiP16233
KOiK14073
OMAiMSQVVGH
OrthoDBiEOG091G0DJ5
PhylomeDBiP16233
TreeFamiTF324997

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR002331 Lipase_panc
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00823 PANCLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

Sequencei

Sequence statusi: Complete.

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

P16233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD
60 70 80 90 100
VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE
110 120 130 140 150
NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE
160 170 180 190 200
FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ
210 220 230 240 250
GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE
260 270 280 290 300
MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
310 320 330 340 350
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS
360 370 380 390 400
NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS
410 420 430 440 450
NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS
460
PETVREEVLL TLTPC
Length:465
Mass (Da):51,157
Last modified:April 1, 1990 - v1
Checksum:i2BC49CC7F0E2DF52
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078977221T → M in PNLIPD; loss of function in lipid catabolic process; the mutant is not secreted. 2 PublicationsCorresponds to variant dbSNP:rs746000327EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
CH471066 Genomic DNA Translation: EAW49451.1
BC014309 mRNA Translation: AAH14309.1
CCDSiCCDS7594.1
PIRiC43357
RefSeqiNP_000927.1, NM_000936.3
UniGeneiHs.501135

Genome annotation databases

EnsembliENST00000369221; ENSP00000358223; ENSG00000175535
GeneIDi5406
KEGGihsa:5406
UCSCiuc001lcm.4 human

Similar proteinsi

Entry informationi

Entry nameiLIPP_HUMAN
AccessioniPrimary (citable) accession number: P16233
Secondary accession number(s): Q5VSQ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 20, 2018
This is version 187 of the entry and version 1 of the sequence. See 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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