INHBA

Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene.[5] INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

INHBA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1NYS, 1NYU, 1S4Y, 2ARP, 2ARV, 2B0U, 2P6A, 3B4V, 4MID, 5HLY, 5HLZ
Identifiers
Aliases	INHBA, EDF, FRP, inhibin beta A, inhibin beta A subunit, inhibin subunit beta A
External IDs	OMIM: 147290 MGI: 96570 HomoloGene: 1653 GeneCards: INHBA
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7p14.1 Start 41,667,168 bp[1] End 41,705,834 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 A1|13 5.85 cM Start 16,011,851 bp[2] End 16,031,621 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transforming growth factor beta receptor binding • receptor binding • hormone activity • identical protein binding • growth factor activity • cytokine activity • protein heterodimerization activity • type II activin receptor binding • peptide hormone binding • GO:0001948 protein binding • inhibin binding Cellular component • inhibin A complex • activin A complex • perinuclear region of cytoplasm • extracellular region • extracellular Biological process • negative regulation of cell proliferation • eyelid development in camera-type eye • endodermal cell differentiation • negative regulation of follicle-stimulating hormone secretion • GABAergic neuron differentiation • cell-cell signaling • progesterone secretion • mesodermal cell differentiation • negative regulation of macrophage differentiation • odontogenesis • hair follicle development • hematopoietic progenitor cell differentiation • regulation of transcription from RNA polymerase II promoter • negative regulation of phosphorylation • SMAD protein signal transduction • extrinsic apoptotic signaling pathway • cell cycle arrest • positive regulation of follicle-stimulating hormone secretion • cell surface receptor signaling pathway • positive regulation of pathway-restricted SMAD protein phosphorylation • nervous system development • positive regulation of ovulation • positive regulation of gene expression • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand • cellular response to cholesterol • mesoderm formation • activin receptor signaling pathway • negative regulation of B cell differentiation • ovarian follicle development • striatal medium spiny neuron differentiation • positive regulation of cellular protein metabolic process • positive regulation of transcription, DNA-templated • hemoglobin biosynthetic process • palate development • positive regulation of erythrocyte differentiation • cellular response to follicle-stimulating hormone stimulus • regulation of MAPK cascade • cell development • positive regulation of transcription from RNA polymerase II promoter • negative regulation of cell cycle • negative regulation of cell growth • response to drug • cell differentiation • defense response • erythrocyte differentiation • male gonad development • regulation of follicle-stimulating hormone secretion • regulation of receptor activity • G1/S transition of mitotic cell cycle • response to wounding • regulation of apoptotic process • negative regulation of hair follicle development • signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3624	16323
Ensembl	ENSG00000122641	ENSMUSG00000041324
UniProt	P08476	Q04998
RefSeq (mRNA)	NM_002192	NM_008380
RefSeq (protein)	NP_002183 NP_002183.1	NP_032406
Location (UCSC)	Chr 7: 41.67 – 41.71 Mb	Chr 13: 16.01 – 16.03 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.[6]

Interactions

INHBA has been shown to interact with ACVR2A.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000122641 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000041324 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Burger HG, Igarashi M (April 1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
6. "Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)".
7. Lewis, K A; Gray P C; Blount A L; MacConell L A; Wiater E; Bilezikjian L M; Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. ENGLAND. 404 (6776): 411–4. doi:10.1038/35006129. ISSN 0028-0836. PMID 10746731. S2CID 4393629.
8. Martens, J W; de Winter J P; Timmerman M A; McLuskey A; van Schaik R H; Themmen A P; de Jong F H (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells" (PDF). Endocrinology. UNITED STATES. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. ISSN 0013-7227. PMID 9202237.

Further reading

• Munz B, Hübner G, Tretter Y, et al. (1999). "A novel role of activin in inflammation and repair". J. Endocrinol. 161 (2): 187–93. doi:10.1677/joe.0.1610187. PMID 10320815.
• Welt C, Sidis Y, Keutmann H, Schneyer A (2002). "Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium". Exp. Biol. Med. (Maywood). 227 (9): 724–52. doi:10.1177/153537020222700905. PMID 12324653. S2CID 19795772.
• Shav-Tal Y, Zipori D (2003). "The role of activin a in regulation of hemopoiesis". Stem Cells. 20 (6): 493–500. doi:10.1634/stemcells.20-6-493. PMID 12456957. S2CID 36242096.
• Reis FM, Luisi S, Carneiro MM, et al. (2005). "Activin, inhibin and the human breast". Mol. Cell. Endocrinol. 225 (1–2): 77–82. doi:10.1016/j.mce.2004.02.016. PMID 15451571. S2CID 24201803.
• Shao L, Frigon NL, Young AL, et al. (1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773–81. doi:10.1182/blood.V79.3.773.bloodjournal793773. PMID 1310063.
• Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6): 973–82. doi:10.1016/0092-8674(91)90549-E. PMID 1646080. S2CID 36407277.
• Tanimoto K, Handa S, Ueno N, et al. (1992). "Structure and sequence analysis of the human activin beta A subunit gene". DNA Seq. 2 (2): 103–10. doi:10.3109/10425179109039678. PMID 1777673.
• Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH (1990). "Activin B: precursor sequences, genomic structure and in vitro activities". Mol. Endocrinol. 3 (9): 1352–8. doi:10.1210/mend-3-9-1352. PMID 2575216.
• Barton DE, Yang-Feng TL, Mason AJ, et al. (1989). "Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice". Genomics. 5 (1): 91–9. doi:10.1016/0888-7543(89)90091-8. PMID 2767687.
• Murata M, Eto Y, Shibai H, et al. (1988). "Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain". Proc. Natl. Acad. Sci. U.S.A. 85 (8): 2434–8. Bibcode:1988PNAS...85.2434M. doi:10.1073/pnas.85.8.2434. PMC 280011. PMID 3267209.
• Burger HG, Igarashi M (1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
• Mason AJ, Niall HD, Seeburg PH (1986). "Structure of two human ovarian inhibins". Biochem. Biophys. Res. Commun. 135 (3): 957–64. doi:10.1016/0006-291X(86)91021-1. PMID 3754442.
• Stewart AG, Milborrow HM, Ring JM, et al. (1986). "Human inhibin genes. Genomic characterisation and sequencing". FEBS Lett. 206 (2): 329–34. doi:10.1016/0014-5793(86)81006-7. PMID 3758355. S2CID 21261385.
• Sumitomo S, Inouye S, Liu XJ, et al. (1995). "The heparin binding site of follistatin is involved in its interaction with activin". Biochem. Biophys. Res. Commun. 208 (1): 1–9. doi:10.1006/bbrc.1995.1297. PMID 7887917.
• Xu J, McKeehan K, Matsuzaki K, McKeehan WL (1995). "Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism". J. Biol. Chem. 270 (11): 6308–6313. doi:10.1074/jbc.270.11.6308. PMID 7890768.
• Mason AJ (1994). "Functional analysis of the cysteine residues of activin A". Mol. Endocrinol. 8 (3): 325–32. doi:10.1210/me.8.3.325. PMID 8015550.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Nishihara T, Okahashi N, Ueda N (1994). "Activin A induces apoptotic cell death". Biochem. Biophys. Res. Commun. 197 (2): 985–91. doi:10.1006/bbrc.1993.2576. PMID 8267637.
• ten Dijke P, Ichijo H, Franzén P, et al. (1993). "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". Oncogene. 8 (10): 2879–87. PMID 8397373.
• Tanimoto K, Yoshida E, Mita S, et al. (1997). "Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers". J. Biol. Chem. 271 (51): 32760–9. doi:10.1074/jbc.271.51.32760. PMID 8955111.