P08476 · INHBA_HUMAN
- ProteinInhibin beta A chain
- GeneINHBA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids426 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInhibin beta A chain
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08476
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_072640 | 280 | found in a patient with early-onset epithelial ovarian tumor; uncertain significance | |||
Sequence: G → E | ||||||
Natural variant | VAR_052566 | 299 | in dbSNP:rs41294833 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_072641 | 386 | found in a patient with early-onset epithelial ovarian tumor; uncertain significance; alters the ratio of secreted activins and ihibins; dbSNP:rs1361491625 | |||
Sequence: N → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 655 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MPLLWLRGFLLASCWIIVRS | ||||||
Propeptide | PRO_0000033708 | 21-310 | ||||
Sequence: SPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRR | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000033709 | 311-426 | Inhibin beta A chain | |||
Sequence: GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS | ||||||
Disulfide bond | 314↔322 | |||||
Sequence: CDGKVNICC | ||||||
Disulfide bond | 321↔391 | |||||
Sequence: CCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCC | ||||||
Disulfide bond | 350↔423 | |||||
Sequence: CEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEEC | ||||||
Disulfide bond | 354↔425 | |||||
Sequence: CPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGC | ||||||
Disulfide bond | 390 | Interchain | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P08476 | Fst P21674 | 2 | EBI-8077140, EBI-5746973 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 259-288 | Disordered | ||||
Sequence: KKKKKEEEGEGKKKGGGEGGAGADEEKEQS |
Sequence similarities
Belongs to the TGF-beta family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length426
- Mass (Da)47,442
- Last updated1989-07-01 v2
- Checksum201CDEDF99CB6919
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 377-379 | in Ref. 7; CAA51163 | ||||
Sequence: RMR → AC |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M13436 EMBL· GenBank· DDBJ | AAA59168.1 EMBL· GenBank· DDBJ | mRNA | ||
X04447 EMBL· GenBank· DDBJ | CAA28041.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X57578 EMBL· GenBank· DDBJ | CAA40805.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X57579 EMBL· GenBank· DDBJ | CAA40805.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X57579 EMBL· GenBank· DDBJ | CAA40806.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC005027 EMBL· GenBank· DDBJ | AAQ96861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007858 EMBL· GenBank· DDBJ | AAH07858.1 EMBL· GenBank· DDBJ | mRNA | ||
J03634 EMBL· GenBank· DDBJ | AAA35787.1 EMBL· GenBank· DDBJ | mRNA | ||
X72498 EMBL· GenBank· DDBJ | CAA51163.1 EMBL· GenBank· DDBJ | mRNA |