General Information

  • ID:  hor006707
  • Uniprot ID:  P01217
  • Protein name:  Glycoprotein hormones alpha chain
  • Gene name:  CGA
  • Organism:  Bos taurus (Bovine)
  • Family:  Glycoprotein hormones subunit alpha family
  • Source:  animal
  • Expression:  NA
  • Disease:  NA
  • Comments:  NA
  • Taxonomy:   Bos (genus), Bovinae (subfamily), Bovidae (family), Pecora (infraorder), Ruminantia (suborder), Artiodactyla (order), Laurasiatheria (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:0005179 hormone activity; GO:0016913 follicle-stimulating hormone activity
  • GO BP:  GO:0006590 thyroid hormone generation; GO:0007186 G protein-coupled receptor signaling pathway; GO:0010469 regulation of signaling receptor activity; GO:0010893 positive regulation of steroid biosynthetic process
  • GO CC:  GO:0005576 extracellular region; GO:0005615 extracellular space; GO:0016914 follicle-stimulating hormone complex; GO:0061696 pituitary gonadotropin complex

Sequence Information

  • Sequence:  FPDGEFTMQGCPECKLKENKYFSKPDAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNVRVENHTECHCSTCYYHKS
  • Length:  96
  • Propeptide:  MDYYRKYAAVILAILSLFLQILHSFPDGEFTMQGCPECKLKENKYFSKPDAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNVRVENHTECHCSTCYYHKS
  • Signal peptide:  MDYYRKYAAVILAILSLFLQILHS
  • Modification:  NA
  • Glycosylation:  T43 O-linked (GalNAc...) threonine;T56 N-linked (GlcNAc...) asparagine;T82 N-linked (GlcNAc...) asparagine
  • Mutagenesis:  NA

Activity

  • Function:  Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
  • Mechanism:  NA
  • Cross BBB:  NA
  • Target:  NA
  • Target Unid:  NA
  • IC50: NA
  • EC50: NA
  • ED50: NA
  • kd: NA
  • Half life: NA

Structure

  • Disulfide bond:  11-35; 14-64; 32-86; 36-88; 63-91
  • Structure ID:  AF-P01217-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)
  •    hor006707_AF2.pdbhor006707_ESM.pdb

Physical Information

Mass: 1248616 Formula: C467H725N127O139S14
Absent amino acids: W Common amino acids: CKT
pI: 8.41 Basic residues: 16
Polar residues: 38 Hydrophobic residues: 21
Hydrophobicity: -46.56 Boman Index: -16100
Half-Life: 1.1 hour Half-Life Yeast: 3 min
Half-Life E.Coli: 2 min Aliphatic Index 38.65
Instability Index: 5270.94 Extinction Coefficient cystines: 8075
Absorbance 280nm: 85

Literature

  • PubMed ID:  6314263
  • Title:  Characterization and nucleotide sequence of the gene for the common alpha subunit of the bovine pituitary glycoprotein hormones.
  • PubMed ID:  6688736
  • Title:  Nucleotide sequence of cloned complementary deoxyribonucleic acid for the alpha subunit of bovine pituitary glycoprotein hormones.
  • PubMed ID:  6187740
  • Title:  Nucleotide sequence of a cDNA for the common alpha subunit of the bovine pituitary glycoprotein hormones. Conservation of nucleotides in the 3'-untranslated region of bovine and human pre-alpha subunit mRNAs.
  • PubMed ID:  5101174
  • Title:  The primary structure of bovine thyrotropin. II. The amino acid sequences of the reduced, S-carboxymethyl alpha and beta chains.
  • PubMed ID:  5101175
  • Title:  Comparisons between the alpha chain of bovine thyrotropin and the CI chain of luteinizing hormone. Compositions of tryptic peptides, cyanogen bromide fragments, and carbohydrate moieties.
  • PubMed ID:  5107231
  • Title:  Bovine luteinizing hormone. Study of the primary structure around the carbohydrate attachment sites of the luteinizing hormone alpha-subunit.
  • PubMed ID:  4854483
  • Title:  Studies on the disulfide bonds of glycoprotein hormones. Locations in the alpha chain based on partial reductions and formation of 14C-labeled S-carboxymethyl derivatives.