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Protein

HRAS-like suppressor 3

Gene

PLA2G16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.By similarity2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=300 µM for dipalmitoyl-PC1 Publication
  1. Vmax=2.57 µmol/min/mg enzyme with dipalmitoyl-PC as substrate1 Publication
  2. Vmax=267 nmol/min/mg enzyme with dipalmitoyl-PE as substrate1 Publication

pH dependencei

Optimum pH is 9.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei23 – 231
Active sitei35 – 351
Active sitei113 – 1131Acyl-thioester intermediate

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-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.

Chemistry

SwissLipidsiSLP:000001077.

Names & Taxonomyi

Protein namesi
Recommended name:
HRAS-like suppressor 3 (EC:3.1.1.32, EC:3.1.1.4)
Short name:
HRSL3
Alternative name(s):
Adipose-specific phospholipase A2
Short name:
AdPLA
Group XVI phospholipase A1/A2
H-rev 107 protein homolog
HRAS-like suppressor 1
HREV107-1
HREV107-3
Renal carcinoma antigen NY-REN-65
Gene namesi
Name:PLA2G16
Synonyms:HRASLS3, HREV107
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:17825. PLA2G16.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 132132CytoplasmicSequence analysisAdd
BLAST
Transmembranei133 – 15523HelicalSequence analysisAdd
BLAST
Topological domaini156 – 1627LumenalSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231H → A: No effect on PPP2R1A-binding. 1 Publication
Mutagenesisi113 – 1131C → S: No effect on PPP2R1A-binding. 1 Publication

Organism-specific databases

PharmGKBiPA164724584.

Polymorphism and mutation databases

BioMutaiPLA2G16.
DMDMi20141767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162HRAS-like suppressor 3PRO_0000152484Add
BLAST

Proteomic databases

MaxQBiP53816.
PaxDbiP53816.
PRIDEiP53816.

PTM databases

iPTMnetiP53816.
PhosphoSiteiP53816.

Expressioni

Tissue specificityi

Widely expressed. low expression, if any, in hematopoietic cells and thymus. In testis, confined to round spermatids. Expressed in normal ovarian epithelial cells. Down-regulated in some ovarian carcinomas and testicular germ cell tumors.4 Publications

Inductioni

By IFNG and IRF1.1 Publication

Gene expression databases

BgeeiP53816.
CleanExiHS_PLA2G16.
ExpressionAtlasiP53816. baseline and differential.
GenevisibleiP53816. HS.

Organism-specific databases

HPAiHPA058997.

Interactioni

Subunit structurei

Interacts with PPP2R1A; this interaction might decrease PP2A activity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP2R1AP301537EBI-746318,EBI-302388
UBQLN1Q9UMX04EBI-746318,EBI-741480
UBQLN1Q9UMX0-23EBI-746318,EBI-10173939

Protein-protein interaction databases

BioGridi116317. 3 interactions.
IntActiP53816. 3 interactions.
MINTiMINT-1461468.
STRINGi9606.ENSP00000320337.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Beta strandi21 – 299Combined sources
Beta strandi32 – 376Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 484Combined sources
Helixi49 – 524Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 695Combined sources
Beta strandi72 – 765Combined sources
Helixi79 – 824Combined sources
Helixi89 – 9810Combined sources
Turni99 – 1013Combined sources
Beta strandi103 – 1097Combined sources
Helixi110 – 12213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KYTNMR-A1-125[»]
4DOTX-ray1.96A1-132[»]
4FA0X-ray2.65A1-134[»]
4Q95X-ray2.20A/B2-38[»]
A/B59-129[»]
ProteinModelPortaliP53816.
SMRiP53816. Positions 1-125.
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.
InParanoidiP53816.
KOiK16817.
OMAiHVNNKHD.
OrthoDBiEOG7B8S59.
PhylomeDBiP53816.
TreeFamiTF330836.

Family and domain databases

InterProiIPR007053. LRAT-like_dom.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAPIPEPKP GDLIEIFRPF YRHWAIYVGD GYVVHLAPPS EVAGAGAASV
60 70 80 90 100
MSALTDKAIV KKELLYDVAG SDKYQVNNKH DDKYSPLPCS KIIQRAEELV
110 120 130 140 150
GQEVLYKLTS ENCEHFVNEL RYGVARSDQV RDVIIAASVA GMGLAAMSLI
160
GVMFSRNKRQ KQ
Length:162
Mass (Da):17,937
Last modified:January 31, 2002 - v2
Checksum:i3565BFC756A6DA3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901S → T in CAA63423 (PubMed:9771974).Curated
Sequence conflicti90 – 901S → T in BAH08749 (PubMed:19615464).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92814 mRNA. Translation: CAA63423.1.
AB030814 mRNA. Translation: BAB08108.1.
AF317086 mRNA. Translation: AAL26892.1.
AB439591 mRNA. Translation: BAH08749.1.
AK313075 mRNA. Translation: BAG35901.1.
CH471076 Genomic DNA. Translation: EAW74158.1.
BC001387 mRNA. Translation: AAH01387.1.
BC103807 mRNA. Translation: AAI03808.1.
CCDSiCCDS8047.1.
RefSeqiNP_001121675.1. NM_001128203.1.
NP_009000.2. NM_007069.3.
XP_006718489.1. XM_006718426.1.
UniGeneiHs.502775.

Genome annotation databases

EnsembliENST00000323646; ENSP00000320337; ENSG00000176485.
ENST00000415826; ENSP00000389124; ENSG00000176485.
GeneIDi11145.
KEGGihsa:11145.
UCSCiuc001nxh.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92814 mRNA. Translation: CAA63423.1.
AB030814 mRNA. Translation: BAB08108.1.
AF317086 mRNA. Translation: AAL26892.1.
AB439591 mRNA. Translation: BAH08749.1.
AK313075 mRNA. Translation: BAG35901.1.
CH471076 Genomic DNA. Translation: EAW74158.1.
BC001387 mRNA. Translation: AAH01387.1.
BC103807 mRNA. Translation: AAI03808.1.
CCDSiCCDS8047.1.
RefSeqiNP_001121675.1. NM_001128203.1.
NP_009000.2. NM_007069.3.
XP_006718489.1. XM_006718426.1.
UniGeneiHs.502775.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KYTNMR-A1-125[»]
4DOTX-ray1.96A1-132[»]
4FA0X-ray2.65A1-134[»]
4Q95X-ray2.20A/B2-38[»]
A/B59-129[»]
ProteinModelPortaliP53816.
SMRiP53816. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116317. 3 interactions.
IntActiP53816. 3 interactions.
MINTiMINT-1461468.
STRINGi9606.ENSP00000320337.

Chemistry

SwissLipidsiSLP:000001077.

PTM databases

iPTMnetiP53816.
PhosphoSiteiP53816.

Polymorphism and mutation databases

BioMutaiPLA2G16.
DMDMi20141767.

Proteomic databases

MaxQBiP53816.
PaxDbiP53816.
PRIDEiP53816.

Protocols and materials databases

DNASUi11145.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323646; ENSP00000320337; ENSG00000176485.
ENST00000415826; ENSP00000389124; ENSG00000176485.
GeneIDi11145.
KEGGihsa:11145.
UCSCiuc001nxh.4. human.

Organism-specific databases

CTDi11145.
GeneCardsiPLA2G16.
HGNCiHGNC:17825. PLA2G16.
HPAiHPA058997.
MIMi613867. gene.
neXtProtiNX_P53816.
PharmGKBiPA164724584.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IW0Y. Eukaryota.
ENOG4111TDD. LUCA.
GeneTreeiENSGT00390000013327.
HOGENOMiHOG000293227.
InParanoidiP53816.
KOiK16817.
OMAiHVNNKHD.
OrthoDBiEOG7B8S59.
PhylomeDBiP53816.
TreeFamiTF330836.

Enzyme and pathway databases

ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.

Miscellaneous databases

ChiTaRSiPLA2G16. human.
GeneWikiiHRASLS3.
GenomeRNAii11145.
NextBioi42368.
PROiP53816.
SOURCEiSearch...

Gene expression databases

BgeeiP53816.
CleanExiHS_PLA2G16.
ExpressionAtlasiP53816. baseline and differential.
GenevisibleiP53816. HS.

Family and domain databases

InterProiIPR007053. LRAT-like_dom.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional and translational downregulation of H-REV107, a class II tumour suppressor gene located on human chromosome 11q11-12."
    Husmann K., Sers C., Fietze E., Mincheva A., Lichter P., Schafer R.
    Oncogene 17:1305-1312(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Human cDNA encoding H-REV107 protein homolog."
    Kato S.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "hH-Rev107, a class II tumor suppressor gene, is expressed by post-meiotic testicular germ cells and CIS cells but not by human testicular germ cell tumors."
    Siegrist S., Feral C., Chami M., Solhonne B., Mattei M.G., Rajpert-De Meyts E., Guellaen G., Bulle F.
    Oncogene 20:5155-5163(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Testis.
  4. "Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes."
    Uyama T., Jin X.H., Tsuboi K., Tonai T., Ueda N.
    Biochim. Biophys. Acta 1791:1114-1124(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  8. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  9. "The class II tumour suppressor gene H-REV107-1 is a target of interferon-regulatory factor-1 and is involved in IFNgamma-induced cell death in human ovarian carcinoma cells."
    Sers C., Husmann K., Nazarenko I., Reich S., Wiechen K., Zhumabayeva B., Adhikari P., Schroder K., Gontarewicz A., Schafer R.
    Oncogene 21:2829-2839(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  10. "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells."
    Nazarenko I., Schafer R., Sers C.
    J. Cell Sci. 120:1393-1404(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP2R1A, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-23 AND CYS-113.
  11. "Solution structure of the N-terminal catalytic domain of human H-REV107 -- a novel circular permutated NlpC/P60 domain."
    Ren X., Lin J., Jin C., Xia B.
    FEBS Lett. 584:4222-4226(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-125, ACTIVE SITE.
  12. "Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins."
    Golczak M., Kiser P.D., Sears A.E., Lodowski D.T., Blaner W.S., Palczewski K.
    J. Biol. Chem. 287:23790-23807(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 1-132, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION.
  13. "Structure/Function relationships of adipose phospholipase A2 containing a cys-his-his catalytic triad."
    Pang X.Y., Cao J., Addington L., Lovell S., Battaile K.P., Zhang N., Rao J.L., Dennis E.A., Moise A.R.
    J. Biol. Chem. 287:35260-35274(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-134, CATALYTIC ACTIVITY, ACTIVE SITE.

Entry informationi

Entry nameiHRSL3_HUMAN
AccessioniPrimary (citable) accession number: P53816
Secondary accession number(s): B2R7Q4
, B7XAK5, Q3SYI3, Q9HDD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 31, 2002
Last modified: March 16, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.