Skip Header

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

Patatin-like phospholipase domain-containing protein 2

Gene

Pnpla2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Pathwayi: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1482883. Acyl chain remodeling of DAG and TAG.
UniPathwayiUPA00256.

Names & Taxonomyi

Protein namesi
Recommended name:
Patatin-like phospholipase domain-containing protein 2 (EC:3.1.1.3)
Alternative name(s):
Adipose triglyceride lipase
Gene namesi
Name:Pnpla2
Synonyms:Atgl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1309044. Pnpla2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 478449LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Patatin-like phospholipase domain-containing protein 2PRO_0000292529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence analysis
Modified residuei366 – 3661Phosphoserine; in vitroBy similarity
Modified residuei388 – 3881Phosphoserine; by PKABy similarity
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources
Modified residuei460 – 4601Phosphoserine; in vitroBy similarity

Post-translational modificationi

May be phosphorylated.By similarity
Phosphorylation at Ser-398 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP0C548.
PRIDEiP0C548.

PTM databases

iPTMnetiP0C548.

Expressioni

Inductioni

Increased by rosiglitazone in subcutaneous and visceral white adipose tissue.1 Publication

Gene expression databases

GenevisibleiP0C548. RN.

Interactioni

Subunit structurei

Interacts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity (By similarity). Interacts with SERPINF1; interacts at one site of interaction (By similarity). Despite a colocalization in lipid droplets, it probably does not interact with PLIN (By similarity). Interacts with PLIN5; prevents interaction with ABHD5 (PubMed:23408028, PubMed:24303154). Interacts with FAF2 (By similarity).By similarity2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025826.

Structurei

3D structure databases

ProteinModelPortaliP0C548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 179170PatatinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 495GXSXG

Sequence similaritiesi

Contains 1 patatin domain.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3773. Eukaryota.
ENOG410XSQS. LUCA.
GeneTreeiENSGT00390000005295.
HOGENOMiHOG000007467.
HOVERGENiHBG007046.
InParanoidiP0C548.
KOiK16816.
OMAiDSHEHAS.
OrthoDBiEOG7J9VQR.
PhylomeDBiP0C548.
TreeFamiTF314272.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
IPR033562. PLPL.
[Graphical view]
PANTHERiPTHR12406. PTHR12406. 1 hit.
PfamiPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C548-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA
60 70 80 90 100
LTATALVTGA CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK
110 120 130 140 150
TLPADCHTRA SGRLGISLTR VSDGENVIIS HFSSKDELIQ ANVCSTFIPV
160 170 180 190 200
YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN TITVSPFSGE SDICPQDSST
210 220 230 240 250
NIHELRITNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ GYRDGLRFLR
260 270 280 290 300
RNGLLNQPNP LLALPPVVPQ EEDAEEAAVT EERTGGEDRI LEHLPARLNE
310 320 330 340 350
ALLEACVEPK DLMTTLSNML PVRLATAMMV PYTLPLESAV SFTIRLLEWL
360 370 380 390 400
PDVPEDIRWM KEQTGSICQY LVMRAKRKLG DHLPSRLSEQ VELRRAQSLP
410 420 430 440 450
SVPLSCATYS EALPNWVRNN LSLGDALAKW EECQRQLLLG LFCTNVAFPP
460 470
DALRMRAPAS PTATDPATPQ DPSGLPPC
Length:478
Mass (Da):52,567
Last modified:June 26, 2007 - v1
Checksum:iE6B8294E47631410
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109542 Genomic DNA. No translation available.
RefSeqiNP_001101979.2. NM_001108509.2.
XP_003749062.1. XM_003749014.3.
UniGeneiRn.19196.

Genome annotation databases

EnsembliENSRNOT00000025319; ENSRNOP00000025319; ENSRNOG00000018736.
ENSRNOT00000025826; ENSRNOP00000025826; ENSRNOG00000047551.
GeneIDi100911615.
361676.
KEGGirno:100911615.
rno:361676.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109542 Genomic DNA. No translation available.
RefSeqiNP_001101979.2. NM_001108509.2.
XP_003749062.1. XM_003749014.3.
UniGeneiRn.19196.

3D structure databases

ProteinModelPortaliP0C548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025826.

PTM databases

iPTMnetiP0C548.

Proteomic databases

PaxDbiP0C548.
PRIDEiP0C548.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025319; ENSRNOP00000025319; ENSRNOG00000018736.
ENSRNOT00000025826; ENSRNOP00000025826; ENSRNOG00000047551.
GeneIDi100911615.
361676.
KEGGirno:100911615.
rno:361676.

Organism-specific databases

CTDi57104.
RGDi1309044. Pnpla2.

Phylogenomic databases

eggNOGiKOG3773. Eukaryota.
ENOG410XSQS. LUCA.
GeneTreeiENSGT00390000005295.
HOGENOMiHOG000007467.
HOVERGENiHBG007046.
InParanoidiP0C548.
KOiK16816.
OMAiDSHEHAS.
OrthoDBiEOG7J9VQR.
PhylomeDBiP0C548.
TreeFamiTF314272.

Enzyme and pathway databases

UniPathwayiUPA00256.
ReactomeiR-RNO-1482883. Acyl chain remodeling of DAG and TAG.

Miscellaneous databases

PROiP0C548.

Gene expression databases

GenevisibleiP0C548. RN.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
IPR033562. PLPL.
[Graphical view]
PANTHERiPTHR12406. PTHR12406. 1 hit.
PfamiPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "PPARgamma agonism increases rat adipose tissue lipolysis, expression of glyceride lipases, and the response of lipolysis to hormonal control."
    Festuccia W.T., Laplante M., Berthiaume M., Gelinas Y., Deshaies Y.
    Diabetologia 49:2427-2436(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and following stimulated contraction."
    MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.
    Am. J. Physiol. 304:R644-R650(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5.
  5. "Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and following lipolysis during adrenergic or contractile stimulation."
    Macpherson R.E., Vandenboom R., Roy B.D., Peters S.J.
    Physiol. Rep. 1:E00084-E00084(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5.

Entry informationi

Entry nameiPLPL2_RAT
AccessioniPrimary (citable) accession number: P0C548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: July 6, 2016
This is version 70 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.