Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27657

- LIPP_RAT

UniProt

P27657 - LIPP_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pancreatic triacylglycerol lipase

Gene

Pnlip

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

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. lipase activity Source: RGD
  2. metal ion binding Source: UniProtKB-KW
  3. triglyceride lipase activity Source: RGD

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. lipid metabolic process Source: RGD
  3. post-embryonic development Source: RGD
  4. response to lipid Source: RGD
  5. response to peptide hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

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:
Pancreatic lipase
Gene namesi
Name:Pnlip
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3360. Pnlip.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000017788Add
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

Proteomic databases

PaxDbiP27657.
PRIDEiP27657.

Expressioni

Tissue specificityi

Pancreatic secretory (zymogen) granule.

Inductioni

By colipase/CLPS in the presence of bile salts.

Gene expression databases

GenevestigatoriP27657.

Structurei

3D structure databases

ProteinModelPortaliP27657.
SMRiP27657. Positions 18-465.
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

eggNOGiNOG40923.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP27657.
KOiK14073.
PhylomeDBiP27657.

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.

P27657-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLMLWTFAVL LGAVAGKEVC FDKLGCFSDD APWSGTIDRP LKALPWSPAQ
60 70 80 90 100
INTRFLLYTN ENQDNYQKIT SDASSIRNSN FKTNRKTRII IHGFIDKGEE
110 120 130 140 150
NWLSDMCKNM FKVESVNCIC VDWKGGSRAT YTQATQNVRV VGAEVALLVN
160 170 180 190 200
VLKSDLGHPP DNVHLIGHSL GSHVAGEAGK RTFGAIGRIT GLDAAEPYFQ
210 220 230 240 250
GTPEEVRLDP TDAQFVDAIH TDAAPIIPNL GFGMSQTVGH LDFFPNGGME
260 270 280 290 300
MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFSGF
310 320 330 340 350
SCSSYNVFSA NKCFPCGSEG CPQMGHYADK YPGKTKELYQ KFYLNTGDKS
360 370 380 390 400
NFARWRYQVT VTLSGQKVTG HILVSLFGNG GNSKQYEVFK GSLHPGDTHV
410 420 430 440 450
KEFDSDMDVG DLQKVKFIWY NNVINPTLPK VGASRISVER NDGRVFNFCS
460
QDTVREDVLL TLSAC
Length:465
Mass (Da):51,440
Last modified:August 1, 1992 - v1
Checksum:iCF014D58AA09A6A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58369 mRNA. Translation: AAA79888.1.
RefSeqiNP_037293.1. NM_013161.2.
UniGeneiRn.10130.

Genome annotation databases

GeneIDi25702.
KEGGirno:25702.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58369 mRNA. Translation: AAA79888.1 .
RefSeqi NP_037293.1. NM_013161.2.
UniGenei Rn.10130.

3D structure databases

ProteinModelPortali P27657.
SMRi P27657. Positions 18-465.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P27657.
PRIDEi P27657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25702.
KEGGi rno:25702.

Organism-specific databases

CTDi 5406.
RGDi 3360. Pnlip.

Phylogenomic databases

eggNOGi NOG40923.
HOGENOMi HOG000038552.
HOVERGENi HBG003243.
InParanoidi P27657.
KOi K14073.
PhylomeDBi P27657.

Miscellaneous databases

NextBioi 607735.
PROi P27657.

Gene expression databases

Genevestigatori P27657.

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. "Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development."
    Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.
    Am. J. Physiol. 266:G914-G921(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification and cloning of GP-3 from rat pancreatic acinar zymogen granules as a glycosylated membrane-associated lipase."
    Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D., Williams J.A.
    J. Biol. Chem. 268:10303-10311(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-37.
    Strain: Sprague-Dawley.
    Tissue: Pancreas.
  3. "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.

Entry informationi

Entry nameiLIPP_RAT
AccessioniPrimary (citable) accession number: P27657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 1, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3