Relaxin
Sign in to saveAlso known as IPR022421
Relaxin is a protein hormone of about 6000 Da, first described in 1926 by Frederick Hisaw.
In the Vinony graph
Within Vinony's link graph, Relaxin is referenced by 223 other articles, and connects out to human pregnancy, matrix metalloproteinases and RXFP1.
It sits within the topics Genes on human chromosome 19, Genes on human chromosome 9 and Hormones of the ovary.
Its subject is documented across 24 Wikipedia language editions.
Key facts
- Protein.Name
- Relaxin 3
- Protein.image
- relaxin.png
- Protein.HGNCid
- 17135
- Protein.Symbol
- RLN3
- Protein.AltSymbols
- ZINS4, RXN3, H3
- Protein.EntrezGene
- 117579
- Protein.OMIM
- 606855
- Protein.RefSeq
- NM_080864
- Protein.UniProt
- Q8WXF3
- Protein.Chromosome
- 19
- Protein.Arm
- p
- Protein.Band
- 13.3
- Protein.LocusSupplementaryData
- -q12
- Protein.PDB
- 6RLX
via Wikipedia infobox
Research
3,955 papers- Relaxin suppresses atrial fibrillation, reverses fibrosis and reduces inflammation in aged hearts.Biochemical pharmacology · 2024
- Relaxin.Annual review of physiology · 1984
- Understanding relaxin signalling at the cellular level.Molecular and cellular endocrinology · 2019
- Relaxin--a review.The Australian & New Zealand journal of obstetrics & gynaecology · 1981
- Cardioprotective actions of relaxin.Molecular and cellular endocrinology · 2019
via PubMed
Wikidata facts
- Instance of
- protein family
- Subclass of
- peptide hormone
- Image
- Relaxin.png
Show 1 more fact
- Commons category
- Relaxin
via Wikidata · CC0
~9 min read
Encyclopedic overview
16 sectionsContents
- Synthesis
- Structure
- Function in humans
- Reproduction
- Cardiovascular function
- Function in other animals
- Reproduction
- Cardiovascular function
- Receptors
- Disorders
- Pregnancy
- Pharmacological targets
- Evolution
- See also
- References
- External links
Relaxin is a protein hormone of about 6000 Da, first described in 1926 by Frederick Hisaw.
The relaxin family peptide hormones belong to the insulin superfamily and consists of seven peptides of high structural but low sequence similarity; relaxin-1 (RLN1), 2 (RLN2) and 3 (RLN3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, and INSL6 remain uncharacterised.
Excerpted from Wikipedia’s “Relaxin” article, available under the CC BY-SA 4.0 licence.