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HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HREV107-3) (Renal carcinoma antigen NY-REN-65)

 PA216_HUMAN             Reviewed;         162 AA.
P53816; B2R7Q4; B7XAK5; Q3SYI3; Q9HDD1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 2.
25-OCT-2017, entry version 145.
RecName: Full=HRAS-like suppressor 3 {ECO:0000303|PubMed:17374643};
Short=HRSL3 {ECO:0000303|PubMed:17374643};
EC=3.1.1.32 {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22923616};
EC=3.1.1.4 {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22923616};
AltName: Full=Adipose-specific phospholipase A2 {ECO:0000250|UniProtKB:Q8R3U1};
Short=AdPLA {ECO:0000250|UniProtKB:Q8R3U1};
AltName: Full=Group XVI phospholipase A1/A2 {ECO:0000312|HGNC:HGNC:17825};
AltName: Full=H-rev 107 protein homolog {ECO:0000303|PubMed:9771974};
Short=H-REV107 {ECO:0000303|PubMed:9771974};
Short=HREV107-1 {ECO:0000303|PubMed:9771974};
AltName: Full=HRAS-like suppressor 1;
AltName: Full=HREV107-3;
AltName: Full=Renal carcinoma antigen NY-REN-65 {ECO:0000303|PubMed:10508479};
Name=PLA2G16 {ECO:0000312|HGNC:HGNC:17825};
Synonyms=HRASLS3 {ECO:0000303|PubMed:22605381},
HREV107 {ECO:0000303|PubMed:9771974};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9771974; DOI=10.1038/sj.onc.1202060;
Husmann K., Sers C., Fietze E., Mincheva A., Lichter P., Schafer R.;
"Transcriptional and translational downregulation of H-REV107, a class
II tumour suppressor gene located on human chromosome 11q11-12.";
Oncogene 17:1305-1312(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Kato S.;
"Human cDNA encoding H-REV107 protein homolog.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=11526504; DOI=10.1038/sj.onc.1204658;
Siegrist S., Feral C., Chami M., Solhonne B., Mattei M.G.,
Rajpert-De Meyts E., Guellaen G., Bulle F.;
"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.";
Oncogene 20:5155-5163(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, CATALYTIC
ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Testis;
PubMed=19615464; DOI=10.1016/j.bbalip.2009.07.001;
Uyama T., Jin X.H., Tsuboi K., Tonai T., Ueda N.;
"Characterization of the human tumor suppressors TIG3 and HRASLS2 as
phospholipid-metabolizing enzymes.";
Biochim. Biophys. Acta 1791:1114-1124(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11973642; DOI=10.1038/sj.onc.1205377;
Sers C., Husmann K., Nazarenko I., Reich S., Wiechen K.,
Zhumabayeva B., Adhikari P., Schroder K., Gontarewicz A., Schafer R.;
"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.";
Oncogene 21:2829-2839(2002).
[10]
FUNCTION, INTERACTION WITH PPP2R1A, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF HIS-23 AND CYS-113.
PubMed=17374643; DOI=10.1242/jcs.000018;
Nazarenko I., Schafer R., Sers C.;
"Mechanisms of the HRSL3 tumor suppressor function in ovarian
carcinoma cells.";
J. Cell Sci. 120:1393-1404(2007).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19047760; DOI=10.1194/jlr.M800453-JLR200;
Uyama T., Morishita J., Jin X.H., Okamoto Y., Tsuboi K., Ueda N.;
"The tumor suppressor gene H-Rev107 functions as a novel Ca2+-
independent cytosolic phospholipase A1/2 of the thiol hydrolase
type.";
J. Lipid Res. 50:685-693(2009).
[12]
TISSUE SPECIFICITY.
PubMed=19136964; DOI=10.1038/nm.1904;
Jaworski K., Ahmadian M., Duncan R.E., Sarkadi-Nagy E., Varady K.A.,
Hellerstein M.K., Lee H.Y., Samuel V.T., Shulman G.I., Kim K.H.,
de Val S., Kang C., Sul H.S.;
"AdPLA ablation increases lipolysis and prevents obesity induced by
high-fat feeding or leptin deficiency.";
Nat. Med. 15:159-168(2009).
[13]
FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF CYS-113.
PubMed=28077878; DOI=10.1038/nature21032;
Staring J., von Castelmur E., Blomen V.A., van den Hengel L.G.,
Brockmann M., Baggen J., Thibaut H.J., Nieuwenhuis J., Janssen H.,
van Kuppeveld F.J., Perrakis A., Carette J.E., Brummelkamp T.R.;
"PLA2G16 represents a switch between entry and clearance of
Picornaviridae.";
Nature 541:412-416(2017).
[14]
STRUCTURE BY NMR OF 1-125, AND ACTIVE SITE.
PubMed=20837014; DOI=10.1016/j.febslet.2010.09.015;
Ren X., Lin J., Jin C., Xia B.;
"Solution structure of the N-terminal catalytic domain of human H-
REV107 -- a novel circular permutated NlpC/P60 domain.";
FEBS Lett. 584:4222-4226(2010).
[15]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 1-132, CATALYTIC ACTIVITY,
ACTIVE SITE, AND SUBCELLULAR LOCATION.
PubMed=22605381; DOI=10.1074/jbc.M112.361550;
Golczak M., Kiser P.D., Sears A.E., Lodowski D.T., Blaner W.S.,
Palczewski K.;
"Structural basis for the acyltransferase activity of lecithin:retinol
acyltransferase-like proteins.";
J. Biol. Chem. 287:23790-23807(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-134, CATALYTIC ACTIVITY,
AND ACTIVE SITE.
PubMed=22923616; DOI=10.1074/jbc.M112.398859;
Pang X.Y., Cao J., Addington L., Lovell S., Battaile K.P., Zhang N.,
Rao J.L., Dennis E.A., Moise A.R.;
"Structure/Function relationships of adipose phospholipase A2
containing a cys-his-his catalytic triad.";
J. Biol. Chem. 287:35260-35274(2012).
[17]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-38 AND 59-129, AND
MUTAGENESIS OF 39-PRO--LYS-57.
PubMed=25383759; DOI=10.1038/nchembio.1687;
Golczak M., Sears A.E., Kiser P.D., Palczewski K.;
"LRAT-specific domain facilitates vitamin A metabolism by domain
swapping in HRASLS3.";
Nat. Chem. Biol. 11:26-32(2015).
-!- FUNCTION: Lipid-modifying enzyme that acts as major regulator of
adipocyte lipolysis by catalyzing the release of fatty acids from
phospholipids in adipose tissue (PubMed:19615464, PubMed:19047760,
PubMed:20837014, PubMed:22605381, PubMed:22923616). Shows
phospholipase A1 and A2 activity, catalyzing the calcium-
independent hydrolysis of acyl groups in various
phosphatidylcholines (PC) and phosphatidylethanolamine (PE)
(PubMed:19615464, PubMed:19047760, PubMed:20837014,
PubMed:22605381, PubMed:22923616). 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 (PubMed:22605381, PubMed:25383759). The
relevance of acyltransferase activity in vivo is however unclear
and would require additional evidences (PubMed:22605381,
PubMed:25383759). Also has weak lysophospholipase activity (By
similarity). {ECO:0000250|UniProtKB:Q8R3U1,
ECO:0000269|PubMed:17374643, ECO:0000269|PubMed:19047760,
ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:20837014,
ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22923616,
ECO:0000269|PubMed:25383759}.
-!- FUNCTION: (Microbial infection) Acts as a host factor for
picornaviruses: required during early infection to promote viral
genome release into the cytoplasm (PubMed:28077878). May act as a
cellular sensor of membrane damage at sites of virus entry, which
relocalizes to sites of membrane rupture upon virus unfection
(PubMed:28077878). Facilitates safe passage of the RNA away from
LGALS8, enabling viral genome translation by host ribosome
(PubMed:28077878). May also be involved in initiating pore
formation, increasing pore size or in maintaining pores for genome
delivery (PubMed:28077878). The lipid-modifying enzyme activity is
required for this process (PubMed:28077878).
{ECO:0000269|PubMed:28077878}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464,
ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
ECO:0000269|PubMed:22923616}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 2-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464,
ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
ECO:0000269|PubMed:22923616}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=300 uM for dipalmitoyl-PC {ECO:0000269|PubMed:19615464};
Vmax=2.57 umol/min/mg enzyme with dipalmitoyl-PC as substrate
{ECO:0000269|PubMed:19615464};
Vmax=267 nmol/min/mg enzyme with dipalmitoyl-PE as substrate
{ECO:0000269|PubMed:19615464};
pH dependence:
Optimum pH is 9. {ECO:0000269|PubMed:19615464};
-!- SUBUNIT: Interacts with PPP2R1A; this interaction might decrease
PP2A activity. {ECO:0000269|PubMed:17374643}.
-!- INTERACTION:
P30153:PPP2R1A; NbExp=7; IntAct=EBI-746318, EBI-302388;
Q9UMX0:UBQLN1; NbExp=6; IntAct=EBI-746318, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-746318, EBI-10173939;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:22605381};
Single-pass membrane protein {ECO:0000255}. Cytoplasm
{ECO:0000269|PubMed:17374643}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane
{ECO:0000250|UniProtKB:Q8R3U1}.
-!- TISSUE SPECIFICITY: 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. Highly expressed in white adipose tissue
(PubMed:19136964). {ECO:0000269|PubMed:11526504,
ECO:0000269|PubMed:11973642, ECO:0000269|PubMed:19136964,
ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:9771974}.
-!- INDUCTION: By IFNG and IRF1. {ECO:0000269|PubMed:11973642}.
-!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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EMBL; X92814; CAA63423.1; -; mRNA.
EMBL; AB030814; BAB08108.1; -; mRNA.
EMBL; AF317086; AAL26892.1; -; mRNA.
EMBL; AB439591; BAH08749.1; -; mRNA.
EMBL; AK313075; BAG35901.1; -; mRNA.
EMBL; CH471076; EAW74158.1; -; Genomic_DNA.
EMBL; BC001387; AAH01387.1; -; mRNA.
EMBL; BC103807; AAI03808.1; -; mRNA.
CCDS; CCDS8047.1; -.
RefSeq; NP_001121675.1; NM_001128203.1.
RefSeq; NP_009000.2; NM_007069.3.
RefSeq; XP_006718489.1; XM_006718426.1.
UniGene; Hs.502775; -.
PDB; 2KYT; NMR; -; A=1-125.
PDB; 4DOT; X-ray; 1.96 A; A=1-132.
PDB; 4FA0; X-ray; 2.65 A; A=1-134.
PDB; 4Q95; X-ray; 2.20 A; A/B=2-38, A/B=59-129.
PDBsum; 2KYT; -.
PDBsum; 4DOT; -.
PDBsum; 4FA0; -.
PDBsum; 4Q95; -.
ProteinModelPortal; P53816; -.
SMR; P53816; -.
BioGrid; 116317; 6.
IntAct; P53816; 4.
MINT; MINT-1461468; -.
STRING; 9606.ENSP00000320337; -.
SwissLipids; SLP:000001077; -.
iPTMnet; P53816; -.
PhosphoSitePlus; P53816; -.
BioMuta; PLA2G16; -.
DMDM; 20141767; -.
EPD; P53816; -.
MaxQB; P53816; -.
PaxDb; P53816; -.
PeptideAtlas; P53816; -.
PRIDE; P53816; -.
DNASU; 11145; -.
Ensembl; ENST00000323646; ENSP00000320337; ENSG00000176485.
Ensembl; ENST00000415826; ENSP00000389124; ENSG00000176485.
GeneID; 11145; -.
KEGG; hsa:11145; -.
UCSC; uc001nxh.4; human.
CTD; 11145; -.
DisGeNET; 11145; -.
EuPathDB; HostDB:ENSG00000176485.10; -.
GeneCards; PLA2G16; -.
HGNC; HGNC:17825; PLA2G16.
HPA; HPA058997; -.
MIM; 613867; gene.
neXtProt; NX_P53816; -.
OpenTargets; ENSG00000176485; -.
PharmGKB; PA164724584; -.
eggNOG; ENOG410IW0Y; Eukaryota.
eggNOG; ENOG4111TDD; LUCA.
GeneTree; ENSGT00390000013327; -.
HOGENOM; HOG000293227; -.
InParanoid; P53816; -.
KO; K16817; -.
OMA; HVNNKHD; -.
OrthoDB; EOG091G08MK; -.
PhylomeDB; P53816; -.
TreeFam; TF330836; -.
Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
SIGNOR; P53816; -.
ChiTaRS; PLA2G16; human.
GeneWiki; HRASLS3; -.
GenomeRNAi; 11145; -.
PRO; PR:P53816; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000176485; -.
CleanEx; HS_PLA2G16; -.
ExpressionAtlas; P53816; baseline and differential.
Genevisible; P53816; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008970; F:phosphatidylcholine 1-acylhydrolase activity; IDA:UniProtKB.
GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:Reactome.
GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
GO; GO:1904177; P:regulation of adipose tissue development; ISS:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
InterPro; IPR007053; LRAT-like_dom.
Pfam; PF04970; LRAT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase;
Lipid degradation; Lipid metabolism; Membrane; Peroxisome;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 162 HRAS-like suppressor 3.
/FTId=PRO_0000152484.
TOPO_DOM 1 132 Cytoplasmic. {ECO:0000255}.
TRANSMEM 133 155 Helical. {ECO:0000255}.
TOPO_DOM 156 162 Lumenal. {ECO:0000255}.
ACT_SITE 23 23 {ECO:0000269|PubMed:20837014,
ECO:0000269|PubMed:22605381,
ECO:0000269|PubMed:22923616}.
ACT_SITE 35 35 {ECO:0000269|PubMed:20837014,
ECO:0000269|PubMed:22605381,
ECO:0000269|PubMed:22923616}.
ACT_SITE 113 113 Acyl-thioester intermediate.
{ECO:0000269|PubMed:20837014,
ECO:0000269|PubMed:22605381,
ECO:0000269|PubMed:22923616}.
MUTAGEN 23 23 H->A: No effect on PPP2R1A-binding.
{ECO:0000269|PubMed:17374643}.
MUTAGEN 39 57 PSEVAGAGAASVMSALTDK->DILLALTDDMGRTQKVVSNK
RLILGVIVKV: Induces a major structural
rearrangement accompanied by domain-
swapping dimerization and changes in
substrate-specificity.
{ECO:0000269|PubMed:25383759}.
MUTAGEN 113 113 C->S: No effect on PPP2R1A-binding.
Impaired ability to act as a host factor
for picornaviruses.
{ECO:0000269|PubMed:17374643,
ECO:0000269|PubMed:28077878}.
CONFLICT 90 90 S -> T (in Ref. 1; CAA63423 and 4;
BAH08749). {ECO:0000305}.
STRAND 13 18 {ECO:0000244|PDB:4DOT}.
STRAND 21 29 {ECO:0000244|PDB:4DOT}.
STRAND 32 37 {ECO:0000244|PDB:4DOT}.
STRAND 41 43 {ECO:0000244|PDB:2KYT}.
STRAND 45 48 {ECO:0000244|PDB:2KYT}.
HELIX 49 52 {ECO:0000244|PDB:2KYT}.
STRAND 59 64 {ECO:0000244|PDB:4DOT}.
HELIX 65 69 {ECO:0000244|PDB:4DOT}.
STRAND 72 76 {ECO:0000244|PDB:4DOT}.
HELIX 79 82 {ECO:0000244|PDB:4DOT}.
HELIX 89 98 {ECO:0000244|PDB:4DOT}.
TURN 99 101 {ECO:0000244|PDB:4DOT}.
STRAND 103 109 {ECO:0000244|PDB:4Q95}.
HELIX 110 122 {ECO:0000244|PDB:4DOT}.
SEQUENCE 162 AA; 17937 MW; 3565BFC756A6DA3C CRC64;
MRAPIPEPKP GDLIEIFRPF YRHWAIYVGD GYVVHLAPPS EVAGAGAASV MSALTDKAIV
KKELLYDVAG SDKYQVNNKH DDKYSPLPCS KIIQRAEELV GQEVLYKLTS ENCEHFVNEL
RYGVARSDQV RDVIIAASVA GMGLAAMSLI GVMFSRNKRQ KQ


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