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Protein

HRAS-like suppressor 3

Gene

Pla2g16

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

Functioni

Lipid-modifying enzyme that acts as major regulator of adipocyte lipolysis by catalyzing the release of fatty acids from phospholipids in adipose tissue (PubMed:19047760). Shows phospholipase A1 and A2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE) (PubMed:19047760). For most substrates, phospholipase A1 activity is much higher than phospholipase A2 activity (PubMed:19047760). Phospholipase activity causes decreased intracellular levels of ether-type lipids, affecting peroxisome metabolism (By similarity). May also have acyltransferase activity: catalyzes both N-acylation of phosphatidylethanolamine to form N-acyl-phosphatidylethanolamine and O-acylation of lyso-phosphatidylcholines to form phosphatidylcholines (By similarity). The relevance of acyltransferase activity in vivo is however unclear and would require additional evidences (By similarity). Also has weak lysophospholipase activity (By similarity).By similarity1 Publication

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.1 Publication
Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei211 Publication1
Active sitei33By similarity1
Active sitei111Acyl-thioester intermediate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.32 5301
ReactomeiR-RNO-1482788 Acyl chain remodelling of PC
R-RNO-1482801 Acyl chain remodelling of PS
R-RNO-1482839 Acyl chain remodelling of PE
R-RNO-1482922 Acyl chain remodelling of PI

Chemistry databases

SwissLipidsiSLP:000001906

Names & Taxonomyi

Protein namesi
Recommended name:
HRAS-like suppressor 3By similarity (EC:3.1.1.321 Publication, EC:3.1.1.41 Publication)
Short name:
HRSL3By similarity
Alternative name(s):
Group XVI phospholipase A2Imported
H-rev 107 protein homologBy similarity
Gene namesi
Name:Pla2g16Imported
Synonyms:H-rev107By similarity, Hrasls3By similarity, Hrev107By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2829 Pla2g16

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 130CytoplasmicSequence analysisAdd BLAST130
Transmembranei131 – 153HelicalSequence analysisAdd BLAST23
Topological domaini154 – 160LumenalSequence analysis7

Keywords - Cellular componenti

Cytoplasm, Membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21H → L: Abolishes enzyme activity. 1 Publication1
Mutagenesisi111C → S: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524871 – 160HRAS-like suppressor 3Add BLAST160

Proteomic databases

PaxDbiP53817

Expressioni

Tissue specificityi

Specifically expressed in H-ras resistant fibroblasts.2 Publications

Inductioni

Induced during preadipocyte differentiation into adipocytes.1 Publication

Gene expression databases

BgeeiENSRNOG00000021206
ExpressionAtlasiP53817 baseline and differential
GenevisibleiP53817 RN

Interactioni

Subunit structurei

Interacts with PPP2R1A; this interaction might decrease PP2A activity.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038045

Structurei

3D structure databases

SMRiP53817
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the H-rev107 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IW0Y Eukaryota
ENOG4111TDD LUCA
GeneTreeiENSGT00390000013327
HOGENOMiHOG000293227
InParanoidiP53817
KOiK16817
OMAiHVNNKHD
PhylomeDBiP53817
TreeFamiTF330836

Family and domain databases

InterProiView protein in InterPro
IPR007053 LRAT-like_dom
PfamiView protein in Pfam
PF04970 LRAT, 1 hit

Sequencei

Sequence statusi: Complete.

P53817-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIPEPKPGD LIEIFRPMYS HWAIYVGDGY VIHLAPPSEI PGAGAASIMS
60 70 80 90 100
ALTDKAIVKK ELLRDVAGKD KYQVNNKHDK EYTPLPLNKI IQRAEELVGQ
110 120 130 140 150
EVLYRLTSEN CEHFVNELRY GVPRSDQVRD AVKVATVTGV GLAALGLIGV
160
MLSRNKKQKQ
Length:160
Mass (Da):17,749
Last modified:September 1, 2009 - v2
Checksum:iA0B32D6FA0A943A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131A → T in CAA53991 (PubMed:8290259).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76453 mRNA Translation: CAA53991.1
AB298805 mRNA Translation: BAH08634.1
CH473953 Genomic DNA Translation: EDM12684.1
CH473953 Genomic DNA Translation: EDM12685.1
PIRiS42794
RefSeqiNP_058756.2, NM_017060.2
UniGeneiRn.11377

Genome annotation databases

EnsembliENSRNOT00000032879; ENSRNOP00000038045; ENSRNOG00000021206
GeneIDi24913
KEGGirno:24913
UCSCiRGD:2829 rat

Similar proteinsi

Entry informationi

Entry nameiPA216_RAT
AccessioniPrimary (citable) accession number: P53817
Secondary accession number(s): B7X6T2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: May 23, 2018
This is version 105 of the entry and version 2 of the sequence. See 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

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