B6A8S2 · B6A8S2_OCHDA

Function

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. 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. 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. 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. 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. May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. 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). 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. 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. In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses. Increases CD4+CD25- T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation.

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionhormone activity
Molecular Functionpeptide hormone receptor binding
Biological Processenergy reserve metabolic process
Biological Processlipid metabolic process
Biological Processnegative regulation of appetite by leptin-mediated signaling pathway
Biological Processpositive regulation of p38MAPK cascade
Biological Processpositive regulation of receptor signaling pathway via JAK-STAT
Biological Processpositive regulation of TOR signaling
Biological Processresponse to insulin

Names & Taxonomy

Protein names

  • Recommended name
    Leptin
  • Alternative names
    • Obesity factor

Gene names

    • Name
      OB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Ochotonidae > Ochotona

Accessions

  • Primary accession
    B6A8S2

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_500284223022-167Leptin
Disulfide bond117↔167

Keywords

Family & Domains

Sequence similarities

Belongs to the leptin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    167
  • Mass (Da)
    18,516
  • Last updated
    2008-11-25 v1
  • Checksum
    C9218A2D8CD92F7F
MRCGPLCQLLWLWPCLLCVQAVSIWKVRDDTKTLIKTIVTRISDISHTHAVSSKQRITGLDFIPALHPNLSLSKMDQTLVLYKHILTSLPSRNVVQIANDLENLRDLLHLLAASQGCPPPRASDLESLNSLESILEASLYSTEVVALSRLQGSLHEMLQQLDIGPGC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ983185
EMBL· GenBank· DDBJ
ABL74882.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp