Q99PW7 · FSTL3_RAT
- ProteinFollistatin-related protein 3
- GeneFstl3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids256 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
The secreted form is a binding and antagonizing protein for members of the TGF-beta family, such as activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. The nuclear form is probably involved in transcriptional regulation via interaction with MLLT10 (By similarity).
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
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFollistatin-related protein 3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ99PW7
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MRPGALWPLLWGALVWAVGSVGA | ||||||
Chain | PRO_0000010117 | 24-256 | Follistatin-related protein 3 | |||
Sequence: VMGSGDSVPGGVCWLQQGKEATCSLVLKTQVSREECCASGNINTAWSNFTHPGNKISLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPHCECVSNCEGVPAGFQVCGSDGATYRDECELRTARCRGHPDLRVMYRGRCQKSCAQVVCPRPQSCLVDQTGSAHCVVCRAAPCPVPPNPGQELCGNNNVTYISSCHLRQATCFLGRSIGVRHPGICTGGPKVPAEEEENFV | ||||||
Disulfide bond | 36↔59 | |||||
Sequence: CWLQQGKEATCSLVLKTQVSREEC | ||||||
Disulfide bond | 46↔90 | |||||
Sequence: CSLVLKTQVSREECCASGNINTAWSNFTHPGNKISLLGFLGLVHC | ||||||
Disulfide bond | 60↔93 | |||||
Sequence: CASGNINTAWSNFTHPGNKISLLGFLGLVHCLPC | ||||||
Glycosylation | 71 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 97↔108 | |||||
Sequence: CDGVECGPGKAC | ||||||
Disulfide bond | 102↔117 | |||||
Sequence: CGPGKACRMLGGRPHC | ||||||
Disulfide bond | 119↔151 | |||||
Sequence: CVSNCEGVPAGFQVCGSDGATYRDECELRTARC | ||||||
Disulfide bond | 123↔144 | |||||
Sequence: CEGVPAGFQVCGSDGATYRDEC | ||||||
Disulfide bond | 133↔165 | |||||
Sequence: CGSDGATYRDECELRTARCRGHPDLRVMYRGRC | ||||||
Disulfide bond | 193↔227 | |||||
Sequence: CRAAPCPVPPNPGQELCGNNNVTYISSCHLRQATC | ||||||
Disulfide bond | 198↔220 | |||||
Sequence: CPVPPNPGQELCGNNNVTYISSC | ||||||
Disulfide bond | 209↔241 | |||||
Sequence: CGNNNVTYISSCHLRQATCFLGRSIGVRHPGIC | ||||||
Glycosylation | 213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with INHBA and INHBB. Interacts with FN1. Interacts with ADAM12. Interacts with MLLT10; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with MSTN (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-105 | TB | ||||
Sequence: GVCWLQQGKEATCSLVLKTQVSREECCASGNINTAWSNFTHPGNKISLLGFLGLVHCLPCKDSCDGVECGPG | ||||||
Domain | 97-117 | Follistatin-like 1 | ||||
Sequence: CDGVECGPGKACRMLGGRPHC | ||||||
Domain | 111-167 | Kazal-like 1 | ||||
Sequence: LGGRPHCECVSNCEGVPAGFQVCGSDGATYRDECELRTARCRGHPDLRVMYRGRCQK | ||||||
Domain | 168-191 | Follistatin-like 2 | ||||
Sequence: SCAQVVCPRPQSCLVDQTGSAHCV | ||||||
Domain | 187-243 | Kazal-like 2 | ||||
Sequence: SAHCVVCRAAPCPVPPNPGQELCGNNNVTYISSCHLRQATCFLGRSIGVRHPGICTG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length256
- Mass (Da)27,109
- Last updated2001-06-01 v1
- ChecksumC8464166C0A1D56F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AEC7 | A0A8I6AEC7_RAT | Fstl3 | 332 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB021295 EMBL· GenBank· DDBJ | BAB32664.1 EMBL· GenBank· DDBJ | mRNA | ||
AB071603 EMBL· GenBank· DDBJ | BAC16229.1 EMBL· GenBank· DDBJ | mRNA |