HORDB

General Information

ID: hor006705
Uniprot ID: P01215
Protein name: Glycoprotein hormones alpha chain
Gene name: CGA
Organism: Homo sapiens (Human)
Family: Glycoprotein hormones subunit alpha family
Source: Human
Expression: NA
Disease: Diseases associated with CGA include Ectopic Pregnancy and Ovarian Hyperstimulation Syndrome.
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:0005179 hormone activity; GO:0005515 protein binding; GO:0016913 follicle-stimulating hormone activity
GO BP: GO:0006590 thyroid hormone generation; GO:0007186 G protein-coupled receptor signaling pathway; GO:0008284 positive regulation of cell population proliferation; GO:0008406 gonad development; GO:0009755 hormone-mediated signaling pathway; GO:0010469 regulation of signaling receptor activity; GO:0010893 positive regulation of steroid biosynthetic process; GO:0030335 positive regulation of cell migration; GO:0030878 thyroid gland development; GO:0032275 luteinizing hormone secretion; GO:0032870 cellular response to hormone stimulus; GO:0035265 organ growth; GO:0042699 follicle-stimulating hormone signaling pathway; GO:0045944 positive regulation of transcription by RNA polymerase II; GO:0046621 negative regulation of organ growth; GO:0046884 follicle-stimulating hormone secretion; GO:0048589 developmental growth
GO CC: GO:0005576 extracellular region; GO:0005615 extracellular space; GO:0005796 Golgi lumen; GO:0016914 follicle-stimulating hormone complex; GO:0061696 pituitary gonadotropin complex

Sequence Information

Sequence: APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
Length: 92
Propeptide: MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
Signal peptide: MDYYRKYAAIFLVTLSVFLHVLHS
Modification: NA
Glycosylation: T52 N-linked (GlcNAc...) asparagine;T78 N-linked (GlcNAc...) asparagine
Mutagenesis: 52-52N->D: Increases from 1 to 3 the number of FSH binding a single FSHR receptor.

Activity

Function: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. 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: 7-31; 10-60; 28-82; 32-84; 59-87
Structure ID: AF-P01215-F1(AlphaFold_DB_ID)/1DZ7(PDB_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)

1dz7.pdb

hor006705_AF2.pdb

hor006705_ESM.pdb

Physical Information

Mass:	1182906	Formula:	C437H682N122O134S13
Absent amino acids:	W	Common amino acids:	C
pI:	8.09	Basic residues:	12
Polar residues:	38	Hydrophobic residues:	21
Hydrophobicity:	-31.52	Boman Index:	-14184
Half-Life:	4.4 hour	Half-Life Yeast:	>20 hour
Half-Life E.Coli:	>10 hour	Aliphatic Index	48.7
Instability Index:	7006.41	Extinction Coefficient cystines:	6585
Absorbance 280nm:	72.36

Literature

PubMed ID: 481597
Title: Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit of human chorionic gonadotropin.
PubMed ID: 8196184
Title: [Structure and regulation of human thyroid-stimulating hormone (TSH) gene].
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 6286817
Title: The gene encoding the common alpha subunit of the four human glycoprotein hormones.
PubMed ID: 7462224
Title: The amino acid sequences of the prepeptides contained in the alpha and beta subunits of human choriogonadotropin.
PubMed ID: 890569
Title: Human pituitary thyrotropin. The primary structure of the alpha and beta subunits.
PubMed ID: 5065401
Title: Human pituitary interstitial cell stimulating hormone: primary structure of the subunit.
PubMed ID: 1158880
Title: Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit.
PubMed ID: 4835135
Title: Human follicle stimulating hormone (hFSH): first proposal for the amino acid sequence of the alpha-subunit (hFSHa) and first demonstration of its identity with the alpha-subunit of human luteinizing hormone (hLHa).
PubMed ID: 1150658
Title: The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit.
PubMed ID: 4745444
Title: Human chorionic gonadotropin. Linear amino acid sequence of the alpha subunit.
PubMed ID: 6774759
Title: Studies on the disulfide bonds in human pituitary follicle-stimulating hormone.
PubMed ID: 7410374
Title: Assignment of disulfide bonds in the alpha subunit of human chorionic gonadotropin.
PubMed ID: 1991473
Title: NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
PubMed ID: 2494176
Title: Expression of biologically active human follitropin in Chinese hamster ovary cells.
PubMed ID: 8202136
Title: Crystal structure of human chorionic gonadotropin.
PubMed ID: 8898911
Title: NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
PubMed ID: 15662415
Title: Structure of human follicle-stimulating hormone in complex with its receptor.
PubMed ID: 24692546
Title: Evidence for Follicle-stimulating Hormone Receptor as a Functional Trimer.