INHBA

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) [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 16,186,436 bp [2] End 16,206,206 bp [2]
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 [3] [4]
Wikidata
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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.

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. ^[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 KA, 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 . 404 (6776). ENGLAND: 411–4. Bibcode:2000Natur.404..411L. doi:10.1038/35006129. ISSN   0028-0836. PMID   10746731. S2CID   4393629.
8. Martens JW, 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 . 138 (7). UNITED STATES: 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/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.