Q8VCM7 · FIBG_MOUSE
- ProteinFibrinogen gamma chain
- GeneFgg
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids436 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix (By similarity).
Fibrin has a major function in hemostasis as one of the primary components of blood clots (By similarity).
In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (By similarity).
Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (By similarity).
Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769).
Maternal fibrinogen is essential for successful pregnancy (By similarity).
Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (By similarity).
May also facilitate the immune response via both innate and T-cell mediated pathways (By similarity).
Fibrin has a major function in hemostasis as one of the primary components of blood clots (By similarity).
In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (By similarity).
Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (By similarity).
Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769).
Maternal fibrinogen is essential for successful pregnancy (By similarity).
Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (By similarity).
May also facilitate the immune response via both innate and T-cell mediated pathways (By similarity).
Features
Showing features for binding site.
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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Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | cell cortex | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | fibrinogen complex | |
Cellular Component | synapse | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | signaling receptor binding | |
Biological Process | adaptive immune response | |
Biological Process | cell-matrix adhesion | |
Biological Process | innate immune response | |
Biological Process | platelet aggregation | |
Biological Process | protein polymerization |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFibrinogen gamma chain
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VCM7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 432-436 | Impairs induction of SELP in activated platelets. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MSWSLQPPSFLLCCLLLLFSPTGLA | ||||||
Chain | PRO_0000009100 | 26-436 | Fibrinogen gamma chain | |||
Sequence: YVATRDNCCILDERFGSFCPTTCGIADFLSSYQTDVDNDLRTLEDILFRAENRTTEAKELIKAIQVYYNPDQPPKPGMIDSATQKSKKMVEEIVKYEALLLTHETSIRYLQEIYNSNNQKITNLKQKVAQLEAQCQEPCKDSVQIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFNRLSIGEGQQHHMGGSKQAGDV | ||||||
Disulfide bond | 33 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 34 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 44 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 48 | Interchain (with alpha chain) | ||||
Sequence: C | ||||||
Glycosylation | 77 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 160 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 164 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 178↔207 | |||||
Sequence: CQEIANKGAKESGLYFIRPLKAKQQFLVYC | ||||||
Disulfide bond | 351↔364 | |||||
Sequence: CAEQDGSGWWMNKC | ||||||
Cross-link | 423 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-431) | ||||
Sequence: Q | ||||||
Modified residue | 430 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 431 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-423) | ||||
Sequence: K |
Post-translational modification
Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers (By similarity).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 169-415 | Fibrinogen C-terminal | ||||
Sequence: QIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFN |
Domain
A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length436
- Mass (Da)49,391
- Last updated2002-03-01 v1
- ChecksumFF45A34B6C92143E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q3UER8 | Q3UER8_MOUSE | Fgg | 443 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC019506 EMBL· GenBank· DDBJ | AAH19506.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019828 EMBL· GenBank· DDBJ | AAH19828.1 EMBL· GenBank· DDBJ | mRNA | ||
AF413206 EMBL· GenBank· DDBJ | AAL02226.1 EMBL· GenBank· DDBJ | mRNA |