Glycoprotein hormones, alpha polypeptide

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Glycoprotein hormones, alpha polypeptide - Wikipedia

From Wikipedia, the free encyclopedia

(Redirected from Chorionic gonadotropin alpha)

CGA

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1DZ7, 1E9J, 1FL7, 1HCN, 1HD4, 1HRP, 1QFW, 1XWD, 4AY9, 4MQW

Identifiers

Aliases

CGA, CG-ALPHA, FSHA, GPHA1, GPHa, HCG, LHA, TSHA, Chorionic gonadotropin alpha, glycoprotein hormones, alpha polypeptide, Alpha subunit of glycoprotein hormones, GPA1

External IDs

OMIM: 118850; MGI: 88390; HomoloGene: 587; GeneCards: CGA; OMA:CGA - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6q14.3	Start	87,085,498 bp^[1]
Band	6q14.3	End	87,095,106 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 A5\|4 16.86 cM	Start	34,893,779 bp^[2]
Band	4 A5\|4 16.86 cM	End	34,907,370 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

anterior pituitary

placenta

buccal mucosa cell

testicle

tail of epididymis

gonad

amniotic fluid

decidua

islet of Langerhans

hair follicle

Top expressed in

pituitary gland

median eminence

anterior pituitary

pars tuberalis

arcuate nucleus

pars distalis of adenohypophysis

morula

embryo

outer nuclear layer

blastocyst

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding hormone activity follicle-stimulating hormone activity
Cellular component	Golgi lumen extracellular region extracellular space follicle-stimulating hormone complex
Biological process	cell-cell signaling peptide hormone processing positive regulation of cell population proliferation positive regulation of transcription by RNA polymerase II signal transduction positive regulation of cell migration regulation of transcription by RNA polymerase II regulation of signaling receptor activity G protein-coupled receptor signaling pathway positive regulation of steroid biosynthetic process thyroid hormone generation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


1081


12640

Ensembl


ENSG00000135346


ENSMUSG00000028298

UniProt


P01215


P01216

RefSeq (mRNA)


NM_001252383 NM_000735


NM_009889

RefSeq (protein)


NP_000726 NP_001239312


NP_034019

Location (UCSC)

Chr 6: 87.09 – 87.1 Mb

Chr 4: 34.89 – 34.91 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Glycoprotein hormones, alpha polypeptide is a protein that in humans is encoded by the CGA gene.^[5]

The gonadotropin hormones, human chorionic gonadotropin (hCG), luteinizing hormone (LH), follicle-stimulating hormone (FSH), and thyroid-stimulating hormone (TSH) are heterodimers consisting of alpha and beta subunits (also called chains) that are associated non-covalently. The alpha subunits of these four human glycoprotein hormones are identical; however, their beta chains are unique and confer biological specificity. The protein encoded by this gene is the alpha subunit and belongs to the glycoprotein hormones alpha chain family.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135346 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028298 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Fiddes JC, Goodman HM (Oct 1982). "The gene encoding the common alpha subunit of the four human glycoprotein hormones". Journal of Molecular and Applied Genetics. 1 (1): 3–18. PMID 6286817.
^ "Entrez Gene: CGA glycoprotein hormones, alpha polypeptide".

Roger M, Lahlou N, Couzinet B, Chaussain JL, Scholler R (Oct 1989). "[Free alpha-subunit glycoprotein hormones: physiological and pathological data]". Journal of Steroid Biochemistry. 33 (4B): 763–9. doi:10.1016/0022-4731(89)90489-5. PMID 2481154.
Pierce JG (Dec 1971). "Eli Lilly lecture. The subunits of pituitary thyrotropin--their relationship to other glycoprotein hormones". Endocrinology. 89 (6): 1331–44. doi:10.1210/endo-89-6-1331. PMID 5002675.
Kourides IA, Gurr JA, Wolf O (1984). "The regulation and organization of thyroid stimulating hormone genes". Recent Progress in Hormone Research. 40: 79–120. doi:10.1016/b978-0-12-571140-1.50007-4. ISBN 9780125711401. PMID 6207569.
Miyoshi I, Kasai N, Hayashizaki Y (Apr 1994). "[Structure and regulation of human thyroid-stimulating hormone (TSH) gene]". Nihon Rinsho. Japanese Journal of Clinical Medicine. 52 (4): 940–7. PMID 8196184.
Barrios-De-Tomasi J, Timossi C, Merchant H, Quintanar A, Avalos JM, Andersen CY, Ulloa-Aguirre A (Jan 2002). "Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones". Molecular and Cellular Endocrinology. 186 (2): 189–98. doi:10.1016/S0303-7207(01)00657-8. PMID 11900895. S2CID 27824657.
Moyle WR, Bahl OP, März L (Dec 1975). "Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action". The Journal of Biological Chemistry. 250 (23): 9163–9. doi:10.1016/S0021-9258(19)40704-7. PMID 172504.
Fiddes JC, Goodman HM (Oct 1979). "Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit of human chorionic gonadotropin". Nature. 281 (5730): 351–6. Bibcode:1979Natur.281..351F. doi:10.1038/281351a0. PMID 481597. S2CID 4349804.
Sairam MR, Li CH (Jul 1977). "Human pituitary thyrotropin. The primary structure of the alpha and beta subunits". Canadian Journal of Biochemistry. 55 (7): 755–60. doi:10.1139/o77-108. PMID 890569.
Morgan FJ, Birken S, Canfield RE (Jul 1975). "The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit". The Journal of Biological Chemistry. 250 (13): 5247–58. doi:10.1016/S0021-9258(19)41303-3. PMID 1150658.
Rathnam P, Saxena BB (Sep 1975). "Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit". The Journal of Biological Chemistry. 250 (17): 6735–46. doi:10.1016/S0021-9258(19)40994-0. PMID 1158880.
Weisshaar G, Hiyama J, Renwick AG, Nimtz M (Jan 1991). "NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin". European Journal of Biochemistry. 195 (1): 257–68. doi:10.1111/j.1432-1033.1991.tb15702.x. PMID 1991473.
Sakakibara R, Yokoo Y, Yoshikoshi K, Tominaga N, Eida K, Ishiguro M (Nov 1987). "Subcellular localization of intracellular forms of human chorionic gonadotropin in first trimester placenta". Journal of Biochemistry. 102 (5): 993–1001. doi:10.1093/oxfordjournals.jbchem.a122176. PMID 2449427.
Matzuk MM, Keene JL, Boime I (Feb 1989). "Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction". The Journal of Biological Chemistry. 264 (5): 2409–14. doi:10.1016/S0021-9258(19)81628-9. PMID 2536708.
Lustbader JW, Birken S, Pileggi NF, Kolks MA, Pollak S, Cuff ME, Yang W, Hendrickson WA, Canfield RE (Nov 1989). "Crystallization and characterization of human chorionic gonadotropin in chemically deglycosylated and enzymatically desialylated states". Biochemistry. 28 (24): 9239–43. doi:10.1021/bi00450a001. PMID 2611225.
Harris DC, Machin KJ, Evin GM, Morgan FJ, Isaacs NW (Apr 1989). "Preliminary X-ray diffraction analysis of human chorionic gonadotropin". The Journal of Biological Chemistry. 264 (12): 6705–6. doi:10.1016/S0021-9258(18)83485-8. PMID 2708337.
Hayashizaki Y, Miyai K, Kato K, Matsubara K (Sep 1985). "Molecular cloning of the human thyrotropin-beta subunit gene". FEBS Letters. 188 (2): 394–400. doi:10.1016/0014-5793(85)80409-9. PMID 3839756. S2CID 85070974.
Bellisario R, Carlsen RB, Bahl OP (Oct 1973). "Human chorionic gonadotropin. Linear amino acid sequence of the alpha subunit". The Journal of Biological Chemistry. 248 (19): 6796–809. doi:10.1016/S0021-9258(19)43424-8. PMID 4745444.
Shome B, Parlow AF (Jul 1974). "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)". The Journal of Clinical Endocrinology and Metabolism. 39 (1): 199–202. doi:10.1210/jcem-39-1-199. PMID 4835135.

PDB gallery

1dz7: SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN [MODELED WITHOUT CARBOHYDRATE RESIDUES]
1e9j: SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN [INCLUDING A SINGLE GLCNAC RESIDUE AT ASN52 AND ASN78]
1fl7: HUMAN FOLLICLE STIMULATING HORMONE
1hcn: STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
1hd4: SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN [MODELED WITH DIANTENNARY GLYCAN AT ASN78]
1hrp: CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN
1qfw: TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT
1xwd: Crystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor

Hormones

Endocrine
glands

Hypothalamic–
pituitary

Hypothalamus	GnRH TRH Dopamine CRH GHRH Somatostatin (GHIH) MCH
Posterior pituitary	Oxytocin Vasopressin
Anterior pituitary	FSH LH TSH Prolactin POMC CLIP ACTH MSH Endorphins Lipotropin GH

Testis	Testosterone AMH Inhibin
Ovary	Estradiol Progesterone Activin Inhibin Relaxin GnSAF
Placenta	hCG HPL Estrogen Progesterone

Other

Stomach	Gastrin Ghrelin
Duodenum	CCK GIP Secretin Motilin VIP
Ileum	Enteroglucagon Peptide YY GLP-1
Liver/other	Insulin-like growth factor IGF-1 IGF-2

Adipose tissue

Skeleton

Osteocalcin

Kidney

Heart

Natriuretic peptide
- ANP
- BNP

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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References

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