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Protein

HRAS-like suppressor 3

Gene

Pla2g16

Organism
Mus musculus (Mouse)
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) (By similarity). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue. N- and O-acylation activity is hardly detectable (By similarity). Also has weak lysophospholipase activity.By similarity1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=16 µM for 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PC)1 Publication
  1. Vmax=7.8 µmol/min/mg enzyme with 1-palmitoyl-2-linoleoyl-PC as substrate (in the presence of 2 mM calcium)1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei23 – 231By similarity
Active sitei35 – 351By similarity
Active sitei113 – 1131Acyl-thioester intermediateBy 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-MMU-1482788. Acyl chain remodelling of PC.
R-MMU-1482801. Acyl chain remodelling of PS.
R-MMU-1482839. Acyl chain remodelling of PE.
R-MMU-1482922. Acyl chain remodelling of PI.

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):
Group XVI phospholipase A1/A2
H-rev 107 protein
Gene namesi
Name:Pla2g16
Synonyms:H-rev107, Hrasls3, Hrev107
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2179715. 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

  • endoplasmic reticulum Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231H → A or Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi112 – 1121N → A or Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi113 – 1131C → A or S: Abolishes enzyme activity. 1 Publication
Mutagenesisi129 – 1291Q → A: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162HRAS-like suppressor 3PRO_0000152485Add
BLAST

Proteomic databases

EPDiQ8R3U1.
MaxQBiQ8R3U1.
PaxDbiQ8R3U1.
PRIDEiQ8R3U1.

PTM databases

iPTMnetiQ8R3U1.
PhosphoSiteiQ8R3U1.

Expressioni

Tissue specificityi

Ubiquitously expressed in normal tissues but down-regulated in primary carcinomas or in many cell lines derived from tumors. Highly expressed in white adipose tissue and in adipocytes. Expressed at lower levels in brown adipose tissue.2 Publications

Gene expression databases

BgeeiQ8R3U1.
ExpressionAtlasiQ8R3U1. baseline and differential.
GenevisibleiQ8R3U1. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025925.

Structurei

3D structure databases

ProteinModelPortaliQ8R3U1.
SMRiQ8R3U1. Positions 1-124.
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.
InParanoidiQ8R3U1.
KOiK16817.
OMAiHVNNKHD.
OrthoDBiEOG7B8S59.
PhylomeDBiQ8R3U1.
TreeFamiTF330836.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R3U1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLAPIPEPKP GDLIEIFRPM YRHWAIYVGD GYVIHLAPPS EIAGAGAASI
60 70 80 90 100
MSALTDKAIV KKELLCHVAG KDKYQVNNKH DEEYTPLPLS KIIQRAERLV
110 120 130 140 150
GQEVLYRLTS ENCEHFVNEL RYGVPRSDQV RDAVKAVGIA GVGLAALGLV
160
GVMLSRNKKQ KQ
Length:162
Mass (Da):17,872
Last modified:April 26, 2005 - v2
Checksum:iE688128CF00AADAB
GO
Isoform 2 (identifier: Q8R3U1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-162: RDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ → CHRPCTLTLGVRSFSQLPVAGPECGWRQNYKQDDNSLM

Note: No experimental confirmation available.
Show »
Length:168
Mass (Da):18,932
Checksum:i73F410B77F832256
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421I → V in AAH24581 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei131 – 16232RDAVK…KKQKQ → CHRPCTLTLGVRSFSQLPVA GPECGWRQNYKQDDNSLM in isoform 2. 1 PublicationVSP_013542Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB298806 mRNA. Translation: BAH08635.1.
AK039703 mRNA. Translation: BAE20550.1.
AK042007 mRNA. Translation: BAE20615.1.
AK052657 mRNA. Translation: BAC35085.1.
AK163505 mRNA. Translation: BAE37375.1.
CH466612 Genomic DNA. Translation: EDL33312.1.
CH466612 Genomic DNA. Translation: EDL33314.1.
BC024581 mRNA. Translation: AAH24581.1.
CCDSiCCDS29528.1. [Q8R3U1-1]
RefSeqiNP_644675.2. NM_139269.2. [Q8R3U1-1]
XP_006526984.1. XM_006526921.1. [Q8R3U1-1]
UniGeneiMm.274810.

Genome annotation databases

EnsembliENSMUST00000025925; ENSMUSP00000025925; ENSMUSG00000060675. [Q8R3U1-1]
ENSMUST00000136465; ENSMUSP00000119403; ENSMUSG00000060675. [Q8R3U1-2]
ENSMUST00000136756; ENSMUSP00000115151; ENSMUSG00000060675. [Q8R3U1-1]
GeneIDi225845.
KEGGimmu:225845.
UCSCiuc008glh.1. mouse. [Q8R3U1-2]
uc008gli.1. mouse. [Q8R3U1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB298806 mRNA. Translation: BAH08635.1.
AK039703 mRNA. Translation: BAE20550.1.
AK042007 mRNA. Translation: BAE20615.1.
AK052657 mRNA. Translation: BAC35085.1.
AK163505 mRNA. Translation: BAE37375.1.
CH466612 Genomic DNA. Translation: EDL33312.1.
CH466612 Genomic DNA. Translation: EDL33314.1.
BC024581 mRNA. Translation: AAH24581.1.
CCDSiCCDS29528.1. [Q8R3U1-1]
RefSeqiNP_644675.2. NM_139269.2. [Q8R3U1-1]
XP_006526984.1. XM_006526921.1. [Q8R3U1-1]
UniGeneiMm.274810.

3D structure databases

ProteinModelPortaliQ8R3U1.
SMRiQ8R3U1. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025925.

PTM databases

iPTMnetiQ8R3U1.
PhosphoSiteiQ8R3U1.

Proteomic databases

EPDiQ8R3U1.
MaxQBiQ8R3U1.
PaxDbiQ8R3U1.
PRIDEiQ8R3U1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025925; ENSMUSP00000025925; ENSMUSG00000060675. [Q8R3U1-1]
ENSMUST00000136465; ENSMUSP00000119403; ENSMUSG00000060675. [Q8R3U1-2]
ENSMUST00000136756; ENSMUSP00000115151; ENSMUSG00000060675. [Q8R3U1-1]
GeneIDi225845.
KEGGimmu:225845.
UCSCiuc008glh.1. mouse. [Q8R3U1-2]
uc008gli.1. mouse. [Q8R3U1-1]

Organism-specific databases

CTDi11145.
MGIiMGI:2179715. Pla2g16.

Phylogenomic databases

eggNOGiENOG410IW0Y. Eukaryota.
ENOG4111TDD. LUCA.
GeneTreeiENSGT00390000013327.
HOGENOMiHOG000293227.
InParanoidiQ8R3U1.
KOiK16817.
OMAiHVNNKHD.
OrthoDBiEOG7B8S59.
PhylomeDBiQ8R3U1.
TreeFamiTF330836.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8R3U1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R3U1.
ExpressionAtlasiQ8R3U1. baseline and differential.
GenevisibleiQ8R3U1. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Purification and characterization of LRAT-like protein 3."
    Morishita J., Okamoto Y., Jin X.H., Tsuboi K., Ueda N.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Kidney, Spinal cord and Thymus.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Silencing of the mouse H-rev107 gene encoding a class II tumor suppressor by CpG methylation."
    Roder K., Latasa M.-J., Sul H.S.
    J. Biol. Chem. 277:30543-30550(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Identification and functional characterization of adipose-specific phospholipase A2 (AdPLA)."
    Duncan R.E., Sarkadi-Nagy E., Jaworski K., Ahmadian M., Sul H.S.
    J. Biol. Chem. 283:25428-25436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-23; ASN-112; CYS-113 AND GLN-129.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Liver, Pancreas and Spleen.

Entry informationi

Entry nameiHRSL3_MOUSE
AccessioniPrimary (citable) accession number: Q8R3U1
Secondary accession number(s): B7X6T3, Q3V3C3, Q8BWF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: June 8, 2016
This is version 96 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.