General Information

  • ID:  hor003951
  • Uniprot ID:  P01189
  • Protein name:  Potential peptide
  • Gene name:  pomc
  • Organism:  Homo sapiens (Human)
  • Family:  POMC family
  • Source:  Human
  • Expression:  ACTH and MSH are produced by the pituitary gland.
  • Disease:  NA
  • Comments:  NA
  • Taxonomy:  Homo (genus), Homininae (subfamily), Hominidae (family), Hominoidea (superfamily), Catarrhini (parvorder), Simiiformes (infraorder), Haplorrhini (suborder), Primates (order), Euarchontoglires (superorder), Boreoeutheria, Eutheria, Theria, Mammalia (class), Amniota, Tetrapoda, Dipnotetrapodomorpha, Sarcopterygii (superclass), Euteleostomi, Teleostomi, Gnathostomata, Vertebrata, Craniata (subphylum), Chordata (phylum), Deuterostomia, Bilateria, Eumetazoa, Metazoa (kingdom), Opisthokonta, Eukaryota (superkingdom), cellular organisms
  • GO MF:  GO:0001664 G protein-coupled receptor binding; GO:0005102 signaling receptor binding; GO:0005179 hormone activity; GO:0005515 protein binding; GO:0031781 type 3 melanocortin receptor binding; GO:0031782 type 4 melanocortin receptor binding; GO:0070996 type 1 melanocortin receptor binding
  • GO BP:  GO:0006091 generation of precursor metabolites and energy; GO:0007165 signal transduction; GO:0007218 neuropeptide signaling pathway; GO:0007267 cell-cell signaling; GO:0008217 regulation of blood pressure; GO:0019722 calcium-mediated signaling; GO:0032098 regulation of appetite; GO:0032720 negative regulation of tumor necrosis factor production; GO:0033059 cellular pigmentation; GO:0042593 glucose homeostasis; GO:0043950 positive regulation of cAMP-mediated signaling; GO:0045944 positive regulation of transcription by RNA polymerase II; GO:0070873 regulation of glycogen metabolic process; GO:0140668 positive regulation of oxytocin production; GO:1990680 response to melanocyte-stimulating hormone; GO:2000852 regulation of corticosterone secretion
  • GO CC:  GO:0005576 extracellular region; GO:0005615 extracellular space; GO:0005737 cytoplasm; GO:0030141 secretory granule; GO:0034774 secretory granule lumen

Sequence Information

  • Sequence:  EDVSAGEDCGPLPEGGPEPRSDGAKPGPRE
  • Length:  30
  • Propeptide:  MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
  • Signal peptide:  MPRSCCSRSGALLLALLLQASMEVRG
  • Modification:  T30 Glutamic acid 1-amide
  • Glycosylation:  NA
  • Mutagenesis:  NA

Activity

  • Function:  [Corticotropin]: Stimulates the adrenal glands to release cortisol.; [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; [Beta-endorphin]: Endogenous orexigenic opiate.; [Met-enkephalin]: Endogenous opiate.
  • Mechanism:  NA
  • Cross BBB:  NA
  • Target:  MC4R, MC2R
  • Target Unid:  P32245, Q01718
  • IC50: NA
  • EC50: NA
  • ED50: NA
  • kd: NA
  • Half life: NA

Structure

  • Disulfide bond:  NA
  • Structure ID:  AF-P01189-F1(AlphaFold_DB_ID)
  • Structure: (PDB_ID-from https://www.rcsb.org/; AlphaFold_DB_ID-from https://alphafold.ebi.ac.uk/; hordbxxxxxx_AF2.pdb was predicted structure by AlphaFold2; hordbxxxxxx_ESM.pdb was predicted structure by ESMFold)
  •    hor003951_AF2.pdbhor003951_ESM.pdb

Physical Information

Mass: 352360 Formula: C123H193N37O49S
Absent amino acids: FHIMNQTWY Common amino acids: GP
pI: 3.88 Basic residues: 3
Polar residues: 9 Hydrophobic residues: 4
Hydrophobicity: -134.67 Boman Index: -8290
Half-Life: 1 hour Half-Life Yeast: 30 min
Half-Life E.Coli: >10 hour Aliphatic Index 29.33
Instability Index: 5281 Extinction Coefficient cystines: 0
Absorbance 280nm: 0

Literature

  • PubMed ID:  6272808
  • Title:  The Missing Fragment of the Pro-Sequence of Human Pro-Opiomelanocortin: Sequence and Evidence for C-terminal Amidation