INHBA

Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene. 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; OMA:INHBA - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p14.1 Start 41,667,168 bp End 41,705,834 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 A1|13 5.85 cM Start 16,186,436 bp End 16,206,206 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue saphenous vein vena cava visceral pleura stromal cell of endometrium buccal mucosa cell beta cell placenta caput epididymis lower lobe of lung Top expressed in cumulus cell epithelium of lens incisor nasopharynx ascending aorta dental follicle rib efferent ductule aortic valve barrel cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transforming growth factor beta receptor binding signaling receptor binding hormone activity identical protein binding growth factor activity cytokine activity protein heterodimerization activity type II activin receptor binding peptide hormone binding protein binding inhibin binding Cellular component inhibin A complex activin A complex perinuclear region of cytoplasm extracellular region extracellular space Biological process negative regulation of cell population 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 by RNA polymerase II negative regulation of phosphorylation SMAD protein signal transduction extrinsic apoptotic signaling pathway 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 protein metabolic process positive regulation of transcription, DNA-templated hemoglobin biosynthetic process roof of mouth development positive regulation of erythrocyte differentiation cellular response to follicle-stimulating hormone stimulus regulation of MAPK cascade cell development positive regulation of transcription by RNA polymerase II negative regulation of cell cycle negative regulation of cell growth cell differentiation defense response erythrocyte differentiation male gonad development regulation of follicle-stimulating hormone secretion regulation of signaling 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: 16.19 – 16.21 Mb PubMed search
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 several fold 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.

Interactions

INHBA has been shown to interact with ACVR2A.

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/mend.8.3.8015550. PMID 8015550. S2CID 7615672.
• 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.