Compound monograph
SHLP3
SHLP3 is a 38-residue peptide from the same mitochondrial region as humanin, characterised principally through the study that named the series.
01
Identity & nomenclature
SHLP3 is a 38-residue peptide from the same mitochondrial region as humanin, characterised principally through the study that named the series.
The number denotes a distinct peptide, not an activity rank and not a shortened humanin. Mature endogenous termini and intact endogenous sequence confirmation are UNKNOWN; a synthetic peptide showing activity does not demonstrate that the same mature molecule is produced physiologically.
Canonical name: Small humanin-like peptide 3.
Declared aliases and development codes: SHLP-3.
02
Molecular properties
| Molecular formula | C214H301N47O49S2 |
|---|---|
| Molecular mass | 4380.2 Da |
| One-letter sequence | MLGYNFSSFPCGTISIAPGFNFYRLYFIWVNGLAKVVW |
Thirty-eight residues with free termini and a cysteine at position 11. The recorded sequence has valine at position 29; substitution with tryptophan would change both formula and mass.
03
Structural characteristics
The discovery study identified small open reading frames in the mitochondrial 16S rRNA region and found different cellular responses among the SHLP peptides. SHLP3 induced ERK phosphorylation without detectable STAT3 phosphorylation in the reported comparison. No direct receptor assignment is established here. The conservation analysis found no significant synonymous codon bias and poor conservation for SHLP3, arguing against amino-acid sequence constraint despite the reported cellular observations.
Terminal features: Free N-terminus, Free C-terminal carboxyl.
04
Molecular targets & mechanisms
05
Analytical considerations
Sequence confirmation should distinguish valine from tryptophan at position 29 and establish both termini. One cysteine permits intermolecular disulfide formation, and methionine oxidation changes mass. A matching retention time or nominal mass does not establish residue order or leucine/isoleucine assignments.
06
Verified bibliography
- Naturally occurring mitochondrial-derived peptides are age-dependent regulators of apoptosis, insulin sensitivity, and inflammatory markers.current
Cobb LJ, Lee C, Xiao J, Yen K, Wong RG, Nakamura HK, Mehta HH, Gao Q, Ashur C, Huffman DM, Wan J, Muzumdar R, Barzilai N, Cohen P
Aging · 2016-04 · Journal Article
- Evidence of natural selection in the mitochondrial-derived peptides humanin and SHLP6.current
Gruschus JM, Morris DL, Tjandra N
Scientific reports · 2023-08-29 · Journal Article
- The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance.current
Lee C, Zeng J, Drew BG, Sallam T, Martin-Montalvo A, Wan J, Kim SJ, Mehta H, Hevener AL, de Cabo R, Cohen P
Cell metabolism · 2015-03-03 · Journal Article
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Methodology & citation verification
Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.
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