Reviewed, UniProtKB/Swiss-Prot O88354 (LIPP_SPETR)

Names and origin

Protein names

Recommended name:
    Pancreatic triacylglycerol lipase
      Short name=Pancreatic lipase
      Short name=PL
    EC=3.1.1.3
Alternative name(s):
    Heart pancreatic lipase
    PL-h

Gene names

Name:	PNLIP
Synonyms:	PTL

Organism

Spermophilus tridecemlineatus (Thirteen-lined ground squirrel)

Taxonomic identifier

43179 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Sciuridae › Xerinae › Marmotini › Spermophilus

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Play 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.
Catalytic activity	Triacylglycerol + H(2)O = diacylglycerol + a carboxylate.
Subcellular location	SecretedBy similarity.
Tissue specificity	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.
Induction	Up-regulated during hibernation.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Hibernation Lipid degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	hibernation Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	triacylglycerol lipase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	By similarity
	Chain	17 – 465	449	Pancreatic triacylglycerol lipase		PRO_0000250516
Regions
	Domain	355 – 465	111	PLAT
Sites
	Active site	169	1	Charge relay system By similarity
	Active site	193	1	Charge relay system By similarity
	Active site	280	1	Charge relay system By similarity
Amino acid modifications
	Disulfide bond	20 ↔ 26		By similarity
	Disulfide bond	107 ↔ 118		By similarity
	Disulfide bond	254 ↔ 278		By similarity
	Disulfide bond	302 ↔ 313		By similarity
	Disulfide bond	316 ↔ 321		By similarity
	Disulfide bond	449 ↔ 465		By similarity
Experimental info
	Sequence conflict	133	1	Q → H in AAD51123. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O88354-1 [UniParc]. Last modified May 1, 2000. Version 2. Checksum: A152FB00CD01169B	FASTA	465	51,227
	10 20 30 40 50 60 MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD VNTRFLLYTN 70 80 90 100 110 120 ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE SWLANMCKKM FQVESVNCIC 130 140 150 160 170 180 VDWKGGSRTG YTQASQNIRI VGAEVAYFVD FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR 190 200 210 220 230 240 RTNGAIGRIT GLDPAEPCFE GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH 250 260 270 280 290 300 LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF 310 320 330 340 350 360 SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS NFSRWRYKVS 370 380 390 400 410 420 VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS NEFDSDVDVG DLQRVKFIWY 430 440 450 460 NNVINPSLPR VGASSISVER NDGRVFKFCS AETVREDVLL TLNAC

References

[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: 9653197] [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: 14583598] [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: 14583599] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF027293 mRNA. Translation: AAC40162.2. AF395870 mRNA. Translation: AAK72259.1. AF177402 mRNA. Translation: AAD51123.2. AF177403 mRNA. Translation: AAD51124.1.
3D structure databases
HSSP	HSSP built from PDB template 1LPB based on UniProtKB P16233.
ModBase	Search...
Genome annotation databases
Ensembl	ENSSTOG00000002279. Spermophilus tridecemlineatus. [Contig view]
Phylogenomic databases
HOVERGEN	O88354.
Family and domain databases
InterPro	IPR000734. Lipase. IPR008262. Lipase_AS. IPR013818. Lipase_N. IPR002331. Lipase_panc. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHER	PTHR11610. Lipase. 1 hit. PTHR11610:SF8. Lipase_panc. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00823. PANCLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIPP_SPETR

Accession

Primary (citable) accession number: O88354
Secondary accession number(s): Q9QWF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	May 1, 2000
Last modified:	November 25, 2008
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)