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Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

Organism
Spermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones (By similarity). Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius.By similarity1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691NucleophileBy similarity
Active sitei193 – 1931Charge relay systemPROSITE-ProRule annotation
Metal bindingi204 – 2041Calcium; via carbonyl oxygenBy similarity
Metal bindingi207 – 2071Calcium; via carbonyl oxygenBy similarity
Metal bindingi209 – 2091CalciumBy similarity
Metal bindingi212 – 2121CalciumBy similarity
Active sitei280 – 2801Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. hibernation Source: UniProtKB-KW
  2. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hibernation, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic triacylglycerol lipase (EC:3.1.1.3)
Short name:
PL
Short name:
PTL
Short name:
Pancreatic lipase
Alternative name(s):
Heart pancreatic lipase
PL-h
Gene namesi
Name:PNLIP
Synonyms:PTL
OrganismiSpermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
Taxonomic identifieri43179 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniIctidomys
ProteomesiUP000005215: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000250516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 26PROSITE-ProRule annotation
Disulfide bondi107 ↔ 118PROSITE-ProRule annotation
Disulfide bondi254 ↔ 278PROSITE-ProRule annotation
Disulfide bondi302 ↔ 313PROSITE-ProRule annotation
Disulfide bondi316 ↔ 321PROSITE-ProRule annotation
Disulfide bondi449 ↔ 465PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in many tissues with highest expression in liver. During hibernation there is a significant increases in expression in heart, white adipose tissue (WAT), and testis; but not in pancreas.1 Publication

Inductioni

By colipase/CLPS in the presence of bile salts. Up-regulated during hibernation.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO88354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 465111PLATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiO88354.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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.

O88354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD
60 70 80 90 100
VNTRFLLYTN ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE
110 120 130 140 150
SWLANMCKKM FQVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVD
160 170 180 190 200
FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR RTNGAIGRIT GLDPAEPCFE
210 220 230 240 250
GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH LDFFPNGGIE
260 270 280 290 300
MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF
310 320 330 340 350
SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS
360 370 380 390 400
NFSRWRYKVS VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS
410 420 430 440 450
NEFDSDVDVG DLQRVKFIWY NNVINPSLPR VGASSISVER NDGRVFKFCS
460
AETVREDVLL TLNAC
Length:465
Mass (Da):51,227
Last modified:May 1, 2000 - v2
Checksum:iA152FB00CD01169B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331Q → H in AAD51123 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027293 mRNA. Translation: AAC40162.2.
AF395870 mRNA. Translation: AAK72259.1.
AF177402 mRNA. Translation: AAD51123.2.
AF177403 mRNA. Translation: AAD51124.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027293 mRNA. Translation: AAC40162.2.
AF395870 mRNA. Translation: AAK72259.1.
AF177402 mRNA. Translation: AAD51123.2.
AF177403 mRNA. Translation: AAD51124.1.

3D structure databases

ProteinModelPortaliO88354.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiO88354.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[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]
ProtoNetiSearch...

Publicationsi

  1. "Low-temperature carbon utilization is regulated by novel gene activity in the heart of a hibernating mammal."
    Andrews M.T., Squire T.L., Bowen C.M., Rollins M.B.
    Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION IN HIBERNATION.
    Tissue: Heart.
  2. "Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel genomic organization."
    Squire T.L., Andrews M.T.
    Physiol. Genomics 16:119-130(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  3. Bauer V.W., Andrews M.T.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: White adipose tissue.
  4. "Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-adapted function and differential expression."
    Squire T.L., Lowe M.E., Bauer V.W., Andrews M.T.
    Physiol. Genomics 16:131-140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiLIPP_SPETR
AccessioniPrimary (citable) accession number: O88354
Secondary accession number(s): Q9QWF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.