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O88354

- LIPP_SPETR

UniProt

O88354 - LIPP_SPETR

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Protein
Pancreatic triacylglycerol lipase
Gene
PNLIP, PTL
Organism
Spermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
Status
Reviewed - 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.1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

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

GO - Molecular functioni

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

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 – 1616 By similarity
Add
BLAST
Chaini17 – 465449Pancreatic triacylglycerol lipase
PRO_0000250516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 26 By similarity
Disulfide bondi107 ↔ 118 By similarity
Disulfide bondi254 ↔ 278 By similarity
Disulfide bondi302 ↔ 313 By similarity
Disulfide bondi316 ↔ 321 By similarity
Disulfide bondi449 ↔ 465 By similarity

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.

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

HOGENOMiHOG000038552.
HOVERGENiHBG003243.

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.

O88354-1 [UniParc]FASTAAdd to Basket

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MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD    50
VNTRFLLYTN ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE 100
SWLANMCKKM FQVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVD 150
FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR RTNGAIGRIT GLDPAEPCFE 200
GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH LDFFPNGGIE 250
MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF 300
SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS 350
NFSRWRYKVS VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS 400
NEFDSDVDVG DLQRVKFIWY NNVINPSLPR VGASSISVER NDGRVFKFCS 450
AETVREDVLL TLNAC 465
Length:465
Mass (Da):51,227
Last modified:May 1, 2000 - v2
Checksum:iA152FB00CD01169B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331Q → H in AAD51123. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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

ProteinModelPortali O88354.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000038552.
HOVERGENi HBG003243.

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

  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: June 11, 2014
This is version 87 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

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