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Leptin (Obese protein) (Obesity factor)

 LEP_HUMAN               Reviewed;         167 AA.
P41159; O15158; Q56A88;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
30-AUG-2017, entry version 172.
RecName: Full=Leptin {ECO:0000312|HGNC:HGNC:6553};
AltName: Full=Obese protein;
AltName: Full=Obesity factor;
Flags: Precursor;
Name=LEP {ECO:0000312|HGNC:HGNC:6553};
Synonyms=OB {ECO:0000312|HGNC:HGNC:6553},
OBS {ECO:0000312|HGNC:HGNC:6553};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7984236; DOI=10.1038/372425a0;
Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
"Positional cloning of the mouse obese gene and its human homologue.";
Nature 372:425-432(1994).
[2]
ERRATUM.
Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
Nature 374:479-479(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=7789654; DOI=10.2337/diab.44.7.855;
Masuzaki H., Ogawa Y., Isse N., Satoh N., Okazaki T., Shigemoto M.,
Mori K., Tamura N., Hosoda K., Yoshimasa Y., Jingami H., Kawada T.,
Nakao K.;
"Human obese gene expression. Adipocyte-specific expression and
regional differences in the adipose tissue.";
Diabetes 44:855-858(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8626726; DOI=10.1074/jbc.271.8.3971;
Gong D.W., Bi S., Pratley R.E., Weintraub B.D.;
"Genomic structure and promoter analysis of the human obese gene.";
J. Biol. Chem. 271:3971-3974(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chehab F.F., Lim M.E.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7499240; DOI=10.1074/jbc.270.46.27728;
Isse N., Ogawa Y., Tamura N., Masuzaki H., Mori K., Okazaki T.,
Satoh N., Shigemoto M., Yoshimasa Y., Nishi S., Hosada K., Inazawa J.,
Nakao K.;
"Structural organization and chromosomal assignment of the human obese
gene.";
J. Biol. Chem. 270:27728-27733(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8621021; DOI=10.2337/diab.45.5.675;
Niki T., Mori H., Tamori Y., Kishimoto-Hashiramoto M., Ueno H.,
Araki S., Masugi J., Sawant N., Majithia H.R., Rais N.,
Hashiramoto M., Taniguchi H., Kasuga M.;
"Human obese gene: molecular screening in Japanese and Asian Indian
NIDDM patients associated with obesity.";
Diabetes 45:675-678(1996).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
Lu L., Fu Z., Xu M., Fu Y., Hu Z.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-94.
SeattleSNPs variation discovery resource;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[11]
FUNCTION.
PubMed=8589726; DOI=10.1038/ng0396-318;
Chehab F.F., Lim M.E., Lu R.;
"Correction of the sterility defect in homozygous obese female mice by
treatment with the human recombinant leptin.";
Nat. Genet. 12:318-320(1996).
[12]
INTERACTION WITH SIGLEC6.
PubMed=10428856; DOI=10.1074/jbc.274.32.22729;
Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
Varki A., Kastelein R.A.;
"OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the
immunoglobulin superfamily.";
J. Biol. Chem. 274:22729-22738(1999).
[13]
ERRATUM.
Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
Varki A., Kastelein R.A.;
J. Biol. Chem. 274:28058-28058(1999).
[14]
TISSUE SPECIFICITY, AND INDUCTION BY SECRETIN.
PubMed=10896907; DOI=10.1136/gut.47.2.178;
Sobhani I., Bado A., Vissuzaine C., Buyse M., Kermorgant S.,
Laigneau J.P., Attoub S., Lehy T., Henin D., Mignon M., Lewin M.J.;
"Leptin secretion and leptin receptor in the human stomach.";
Gut 47:178-183(2000).
[15]
FUNCTION.
PubMed=11460888; DOI=10.1038/emm.2001.17;
Park H.Y., Kwon H.M., Lim H.J., Hong B.K., Lee J.Y., Park B.E.,
Jang Y., Cho S.Y., Kim H.S.;
"Potential role of leptin in angiogenesis: leptin induces endothelial
cell proliferation and expression of matrix metalloproteinases in vivo
and in vitro.";
Exp. Mol. Med. 33:95-102(2001).
[16]
TISSUE SPECIFICITY.
PubMed=12448771; DOI=10.1046/j.0021-8782.2002.00106.x;
De Matteis R., Puxeddu R., Riva A., Cinti S.;
"Intralobular ducts of human major salivary glands contain leptin and
its receptor.";
J. Anat. 201:363-370(2002).
[17]
FUNCTION.
PubMed=12504075; DOI=10.1016/S0006-291X(02)02838-3;
Zhao Y., Sun R., You L., Gao C., Tian Z.;
"Expression of leptin receptors and response to leptin stimulation of
human natural killer cell lines.";
Biochem. Biophys. Res. Commun. 300:247-252(2003).
[18]
REVIEW OF FUNCTION IN IMMUNITY.
PubMed=15122202; DOI=10.1038/nri1350;
La Cava A., Matarese G.;
"The weight of leptin in immunity.";
Nat. Rev. Immunol. 4:371-379(2004).
[19]
FUNCTION.
PubMed=15899045; DOI=10.1186/ar1708;
Otero M., Lago R., Lago F., Reino J.J., Gualillo O.;
"signaling pathway involved in nitric oxide synthase type II
activation in chondrocytes: synergistic effect of leptin with
interleukin-1.";
Arthritis Res. Ther. 7:R581-R591(2005).
[20]
TISSUE SPECIFICITY.
PubMed=16052473; DOI=10.1002/jcb.20521;
Solberg R., Aas V., Thoresen G.H., Kase E.T., Drevon C.A.,
Rustan A.C., Reseland J.E.;
"Leptin expression in human primary skeletal muscle cells is reduced
during differentiation.";
J. Cell. Biochem. 96:89-96(2005).
[21]
FUNCTION.
PubMed=17344214; DOI=10.1074/jbc.M609798200;
Saxena N.K., Vertino P.M., Anania F.A., Sharma D.;
"leptin-induced growth stimulation of breast cancer cells involves
recruitment of histone acetyltransferases and mediator complex to
CYCLIN D1 promoter via activation of Stat3.";
J. Biol. Chem. 282:13316-13325(2007).
[22]
FUNCTION.
PubMed=18242580; DOI=10.1016/j.bbrc.2007.04.004;
Jiang H., Yu J., Guo H., Song H., Chen S.;
"up-regulation of survivin by leptin/STAT3 signaling in MCF-7 cells.";
Biochem. Biophys. Res. Commun. 368:1-5(2008).
[23]
FUNCTION.
PubMed=19688109; DOI=10.1155/2009/345838;
Vuolteenaho K., Koskinen A., Kukkonen M., Nieminen R.,
Paeivaerinta U., Moilanen T., Moilanen E.;
"Leptin enhances synthesis of proinflammatory mediators in human
osteoarthritic cartilage--mediator role of NO in leptin-induced PGE2,
IL-6, and IL-8 production.";
Mediators Inflamm. 2009:345838-345838(2009).
[24]
FUNCTION.
PubMed=24340098; DOI=10.1371/journal.pone.0083360;
El-Zein O., Kreydiyyeh S.I.;
"Leptin inhibits glucose intestinal absorption via PKC, p38MAPK, PI3K
and MEK/ERK.";
PLoS ONE 8:E83360-E83360(2013).
[25]
REVIEW OF FUNCTION.
PubMed=25232147; DOI=10.1530/JOE-14-0404;
Allison M.B., Myers M.G. Jr.;
"20 years of leptin: connecting leptin signaling to biological
function.";
J. Endocrinol. 223:T25-T35(2014).
[26]
FUNCTION.
PubMed=25060689; DOI=10.1016/j.metabol.2014.06.010;
Cassano S., Pucino V., La Rocca C., Procaccini C., De Rosa V.,
Marone G., Matarese G.;
"Leptin modulates autophagy in human CD4+CD25- conventional T cells.";
Metabolism 63:1272-1279(2014).
[27]
STRUCTURE BY NMR.
PubMed=9166907; DOI=10.1016/S0014-5793(97)00353-0;
Kline A.D., Becker G.W., Churgay L.M., Landen B.E., Martin D.K.,
Muth W.L., Rathnachalam R., Richardson J.M., Schoner B., Ulmer M.,
Hale J.E.;
"Leptin is a four-helix bundle: secondary structure by NMR.";
FEBS Lett. 407:239-242(1997).
[28]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=9144295; DOI=10.1038/387206a0;
Zhang F., Basinski M.B., Beals J.M., Briggs S.L., Churgay L.M.,
Clawson D.K., Dimarchi R.D., Furman T.C., Hale J.E., Hsiung H.M.,
Schoner B.E., Smith D.P., Zhang X.Y., Wery J.P., Schevitz R.W.;
"Crystal structure of the obese protein leptin-E100.";
Nature 387:206-209(1997).
[29]
VARIANT MET-94.
Bartholomew D.W., McClellan J.M.;
"A novel polymorphism in the leptin gene.";
Hum. Mutat. 12:220-220(1998).
[30]
VARIANT LEPD TRP-105.
PubMed=9500540; DOI=10.1038/ng0398-213;
Strobel A., Issad T., Camoin L., Ozata M., Strosberg A.D.;
"A leptin missense mutation associated with hypogonadism and morbid
obesity.";
Nat. Genet. 18:213-215(1998).
[31]
VARIANT LEPD TYR-100, AND CHARACTERIZATION OF VARIANT LEPD TYR-100.
PubMed=25551525; DOI=10.1056/NEJMoa1406653;
Wabitsch M., Funcke J.B., Lennerz B., Kuhnle-Krahl U., Lahr G.,
Debatin K.M., Vatter P., Gierschik P., Moepps B.,
Fischer-Posovszky P.;
"Biologically inactive leptin and early-onset extreme obesity.";
N. Engl. J. Med. 372:48-54(2015).
-!- FUNCTION: Key player in the regulation of energy balance and body
weight control. Once released into the circulation, has central
and peripheral effects by binding LEPR, found in many tissues,
which results in the activation of several major signaling
pathways (PubMed:17344214, PubMed:15899045, PubMed:19688109). In
the hypothalamus, acts as an appetite-regulating factor that
induces a decrease in food intake and an increase in energy
consumption by inducing anorexinogenic factors and suppressing
orexigenic neuropeptides, also regulates bone mass and secretion
of hypothalamo-pituitary-adrenal hormones. In the periphery,
increases basal metabolism, influences reproductive function,
regulates pancreatic beta-cell function and insulin secretion, is
pro-angiogenic for endothelial cell and affects innate and
adaptive immunity (By similarity) (PubMed:8589726,
PubMed:11460888, PubMed:19688109, PubMed:24340098,
PubMed:25060689). In the arcuate nucleus of the hypothalamus,
activates by depolarization POMC neurons inducing FOS and SOCS3
expression to release anorexigenic peptides and inhibits by
hyperpolarization NPY neurons inducing SOCS3 with a consequent
reduction on release of orexigenic peptides (By similarity). In
addition to its known satiety inducing effect, has a modulatory
role in nutrient absorption. In the intestine, reduces glucose
absorption by enterocytes by activating PKC and leading to a
sequential activation of p38, PI3K and ERK signaling pathways
which exerts an inhibitory effect on glucose absorption
(PubMed:24340098). Acts as a growth factor on certain tissues,
through the activation of different signaling pathways increases
expression of genes involved in cell cycle regulation such as
CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1
pathways (By similarity) (PubMed:17344214). May also play an
apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5
expression (PubMed:18242580). Pro-angiogenic, has mitogenic
activity on vascular endothelial cells and plays a role in matrix
remodeling by regulating the expression of matrix
metalloproteinases (MMPs) and tissue inhibitors of
metalloproteinases (TIMPs) (PubMed:11460888). In innate immunity,
modulates the activity and function of neutrophils by increasing
chemotaxis and the secretion of oxygen radicals. Increases
phagocytosis by macrophages and enhances secretion of pro-
inflammatory mediators. Increases cytotoxic ability of NK cells
(PubMed:12504075). Plays a pro-inflammatory role, in synergy with
IL1B, by inducing NOS2 wich promotes the production of IL6, IL8
and Prostaglandin E2, through a signaling pathway that involves
JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045,
PubMed:19688109). In adaptive immunity, promotes the switch of
memory T-cells towards T helper-1 cell immune responses (By
similarity). Increases CD4(+)CD25(-) T-cell proliferation and
reduces autophagy during TCR (T-cell receptor) stimulation,
through MTOR signaling pathway activation and BCL2 up-regulation
(PubMed:25060689). {ECO:0000250|UniProtKB:P41160,
ECO:0000250|UniProtKB:P50596, ECO:0000269|PubMed:11460888,
ECO:0000269|PubMed:12504075, ECO:0000269|PubMed:15899045,
ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580,
ECO:0000269|PubMed:19688109, ECO:0000269|PubMed:24340098,
ECO:0000269|PubMed:25060689, ECO:0000269|PubMed:8589726,
ECO:0000305|PubMed:15122202, ECO:0000305|PubMed:25232147}.
-!- SUBUNIT: Interacts with SIGLEC6. {ECO:0000269|PubMed:10428856}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25232147}.
-!- TISSUE SPECIFICITY: Adipose tissue is the main source of leptin it
is also produced by other peripheral tissues such as the skeletal
muscle (PubMed:7789654, PubMed:16052473, PubMed:12448771).
Expressed by intercalated and striated tracts of submandibular and
parotid salivary gland intralobular ducts (PubMed:12448771).
Detected by fundic epithelium of the gastric mucosa
(PubMed:10896907). Secreted into blood and gastric juice
(PubMed:10896907). {ECO:0000269|PubMed:10896907,
ECO:0000269|PubMed:12448771, ECO:0000269|PubMed:16052473,
ECO:0000269|PubMed:7789654}.
-!- INDUCTION: Induced by secretin. {ECO:0000269|PubMed:10896907}.
-!- DISEASE: Leptin deficiency (LEPD) [MIM:614962]: A rare disease
characterized by low levels of serum leptin, severe hyperphagia
and intractable obesity from an early age.
{ECO:0000269|PubMed:25551525, ECO:0000269|PubMed:9500540}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the leptin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Leptin entry;
URL="https://en.wikipedia.org/wiki/Leptin";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/lep/";
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EMBL; U18915; AAA60470.1; -; mRNA.
EMBL; D49487; BAA08448.1; -; mRNA.
EMBL; U43653; AAC50400.1; -; mRNA.
EMBL; U43415; AAC31660.1; -; Genomic_DNA.
EMBL; D63710; BAA09839.1; -; Genomic_DNA.
EMBL; D63519; BAA09787.1; -; Genomic_DNA.
EMBL; AF008123; AAB63507.1; -; mRNA.
EMBL; AY996373; AAX81413.1; -; Genomic_DNA.
EMBL; BC060830; AAH60830.1; -; mRNA.
EMBL; BC069452; AAH69452.1; -; mRNA.
EMBL; BC069527; AAH69527.1; -; mRNA.
CCDS; CCDS5800.1; -.
PIR; A38952; LTHU.
PIR; I53166; I53166.
RefSeq; NP_000221.1; NM_000230.2.
RefSeq; XP_005250397.1; XM_005250340.4.
UniGene; Hs.194236; -.
PDB; 1AX8; X-ray; 2.40 A; A=22-167.
PDBsum; 1AX8; -.
ProteinModelPortal; P41159; -.
SMR; P41159; -.
BioGrid; 110143; 5.
DIP; DIP-6116N; -.
IntAct; P41159; 1.
STRING; 9606.ENSP00000312652; -.
iPTMnet; P41159; -.
PhosphoSitePlus; P41159; -.
BioMuta; LEP; -.
PaxDb; P41159; -.
PeptideAtlas; P41159; -.
PRIDE; P41159; -.
DNASU; 3952; -.
Ensembl; ENST00000308868; ENSP00000312652; ENSG00000174697.
GeneID; 3952; -.
KEGG; hsa:3952; -.
UCSC; uc003vml.3; human.
CTD; 3952; -.
DisGeNET; 3952; -.
GeneCards; LEP; -.
HGNC; HGNC:6553; LEP.
HPA; CAB010490; -.
MalaCards; LEP; -.
MIM; 164160; gene.
MIM; 614962; phenotype.
neXtProt; NX_P41159; -.
OpenTargets; ENSG00000174697; -.
Orphanet; 66628; Obesity due to congenital leptin deficiency.
PharmGKB; PA228; -.
eggNOG; ENOG410IVT0; Eukaryota.
eggNOG; ENOG410Y7NT; LUCA.
GeneTree; ENSGT00390000011772; -.
HOGENOM; HOG000252923; -.
HOVERGEN; HBG007860; -.
InParanoid; P41159; -.
KO; K05424; -.
OMA; QISNDLE; -.
OrthoDB; EOG091G0Y82; -.
PhylomeDB; P41159; -.
TreeFam; TF105086; -.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
SignaLink; P41159; -.
SIGNOR; P41159; -.
EvolutionaryTrace; P41159; -.
GeneWiki; Leptin; -.
GenomeRNAi; 3952; -.
PRO; PR:P41159; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000174697; -.
CleanEx; HS_LEP; -.
ExpressionAtlas; P41159; baseline and differential.
Genevisible; P41159; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:HGNC.
GO; GO:0008083; F:growth factor activity; IEA:Ensembl.
GO; GO:0005179; F:hormone activity; IBA:GO_Central.
GO; GO:0051428; F:peptide hormone receptor binding; IBA:GO_Central.
GO; GO:1990051; P:activation of protein kinase C activity; IDA:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0008343; P:adult feeding behavior; ISS:HGNC.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
GO; GO:0098868; P:bone growth; ISS:UniProtKB.
GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:0071298; P:cellular response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; IDA:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:0006112; P:energy reserve metabolic process; IBA:GO_Central.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0006114; P:glycerol biosynthetic process; IEA:Ensembl.
GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0032615; P:interleukin-12 production; IEA:Ensembl.
GO; GO:0072604; P:interleukin-6 secretion; IDA:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB.
GO; GO:0050892; P:intestinal absorption; IDA:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032099; P:negative regulation of appetite; ISS:HGNC.
GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
GO; GO:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
GO; GO:0070093; P:negative regulation of glucagon secretion; IEA:Ensembl.
GO; GO:0046325; P:negative regulation of glucose import; IDA:UniProtKB.
GO; GO:2000486; P:negative regulation of glutamine transport; IEA:Ensembl.
GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045906; P:negative regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IDA:DFLAT.
GO; GO:0048639; P:positive regulation of developmental growth; IDA:DFLAT.
GO; GO:1904651; P:positive regulation of fat cell apoptotic process; IEA:Ensembl.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IEA:Ensembl.
GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IDA:UniProtKB.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IEA:Ensembl.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:2000366; P:positive regulation of STAT protein import into nucleus; IBA:GO_Central.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:0032310; P:prostaglandin secretion; IDA:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
GO; GO:0090335; P:regulation of brown fat cell differentiation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
GO; GO:0001936; P:regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
GO; GO:0060587; P:regulation of lipoprotein lipid oxidation; IEA:Ensembl.
GO; GO:0032814; P:regulation of natural killer cell activation; IDA:UniProtKB.
GO; GO:0042269; P:regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0032817; P:regulation of natural killer cell proliferation; IDA:UniProtKB.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IBA:GO_Central.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000065; Leptin.
PANTHER; PTHR11724; PTHR11724; 1.
Pfam; PF02024; Leptin; 1.
PIRSF; PIRSF001837; Leptin; 1.
PRINTS; PR00495; LEPTIN.
ProDom; PD005698; Leptin; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Diabetes mellitus; Disease mutation;
Disulfide bond; Obesity; Polymorphism; Reference proteome; Secreted;
Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 167 Leptin.
/FTId=PRO_0000017685.
DISULFID 117 167
VARIANT 49 49 Missing.
/FTId=VAR_004196.
VARIANT 94 94 V -> M (in dbSNP:rs17151919).
{ECO:0000269|PubMed:9144295,
ECO:0000269|Ref.9}.
/FTId=VAR_004197.
VARIANT 100 100 D -> Y (in LEPD; no effect on secretion;
does not bind or activate LEPR;
dbSNP:rs724159998).
{ECO:0000269|PubMed:25551525}.
/FTId=VAR_075144.
VARIANT 105 105 R -> W (in LEPD; dbSNP:rs104894023).
{ECO:0000269|PubMed:9500540}.
/FTId=VAR_008094.
VARIANT 110 110 V -> M (in dbSNP:rs1800564).
/FTId=VAR_011955.
CONFLICT 96 96 Q -> R (in Ref. 8; AAB63507).
{ECO:0000305}.
HELIX 25 44 {ECO:0000244|PDB:1AX8}.
HELIX 72 87 {ECO:0000244|PDB:1AX8}.
HELIX 92 114 {ECO:0000244|PDB:1AX8}.
HELIX 128 131 {ECO:0000244|PDB:1AX8}.
HELIX 132 135 {ECO:0000244|PDB:1AX8}.
HELIX 142 160 {ECO:0000244|PDB:1AX8}.
HELIX 161 163 {ECO:0000244|PDB:1AX8}.
SEQUENCE 167 AA; 18641 MW; C91A121E92D37B69 CRC64;
MHWGTLCGFL WLWPYLFYVQ AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSSKQKVTGL
DFIPGLHPIL TLSKMDQTLA VYQQILTSMP SRNVIQISND LENLRDLLHV LAFSKSCHLP
WASGLETLDS LGGVLEASGY STEVVALSRL QGSLQDMLWQ LDLSPGC


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