P02674 · FIBA1_PETMA
- ProteinFibrinogen alpha-1 chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids966 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 11-12 | Cleavage; by thrombin; to release fibrinopeptide A | ||||
Sequence: RG |
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 | fibrinogen complex | |
Molecular Function | signaling receptor binding | |
Biological Process | platelet activation | |
Biological Process | protein polymerization |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameFibrinogen alpha-1 chain
- Cleaved into 2 chains
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Cyclostomata > Hyperoartia > Petromyzontiformes > Petromyzontidae > Petromyzon
Accessions
- Primary accessionP02674
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-5 | |||||
Sequence: QVCIA | ||||||
Peptide | PRO_0000009049 | 6-11 | Fibrinopeptide A | |||
Sequence: DDISLR | ||||||
Chain | PRO_0000009050 | 12-966 | Fibrinogen alpha-1 chain | |||
Sequence: GPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGGMSSLDMLPALPDFGTWDMPDHSDIFSRRRVSTSSTTSSSSGGGHAGAAAGGGGDGASRFGSLFTTDFGPEFHEEFRSMLPGASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP | ||||||
Disulfide bond | 26 | Interchain (with alpha chain) | ||||
Sequence: C | ||||||
Disulfide bond | 34 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 43 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 47 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 159 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 163 | Interchain (with beta chain) | ||||
Sequence: C |
Post-translational modification
Not glycosylated.
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.
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
Keywords
- PTM
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 87-205 | |||||
Sequence: AVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNR | ||||||
Compositional bias | 208-246 | Polar residues | ||||
Sequence: ETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVP | ||||||
Region | 208-804 | Disordered | ||||
Sequence: ETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGG | ||||||
Compositional bias | 262-308 | Polar residues | ||||
Sequence: NEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFH | ||||||
Compositional bias | 318-352 | Polar residues | ||||
Sequence: RDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKD | ||||||
Compositional bias | 371-775 | Polar residues | ||||
Sequence: SLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQG | ||||||
Repeat | 391-408 | 1 | ||||
Sequence: FTGSAQGGSWSTGGSTAT | ||||||
Region | 391-786 | 22 X 18 AA approximate tandem repeats of [FN]-T-G-S-[AG]-[QK]-G-G-S-W-[SG]-T-G-G-[RS]-T-[AE]-[TP] | ||||
Sequence: FTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGA | ||||||
Repeat | 409-426 | 2 | ||||
Sequence: NTGSAQGGSWSTGGRTEP | ||||||
Repeat | 427-444 | 3 | ||||
Sequence: NTGSGQGGSWGTGGRTEP | ||||||
Repeat | 445-462 | 4 | ||||
Sequence: NTGSGQGGSWGTGGRTEP | ||||||
Repeat | 463-480 | 5 | ||||
Sequence: NTGSGQGGSWGTGGRTEP | ||||||
Repeat | 481-498 | 6 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 499-516 | 7 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 517-534 | 8 | ||||
Sequence: NTGSAQGGSWSTGGRTEP | ||||||
Repeat | 535-552 | 9 | ||||
Sequence: NTGSAKGGSWGTGGRTEP | ||||||
Repeat | 553-570 | 10 | ||||
Sequence: NTGSAKGGSWSTGGRTEP | ||||||
Repeat | 571-588 | 11 | ||||
Sequence: NTGSAKGGSWGTGGRTEP | ||||||
Repeat | 589-606 | 12 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 607-624 | 13 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 625-642 | 14 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 643-660 | 15 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 661-678 | 16 | ||||
Sequence: NTGSAQGGSWSTGGRTEP | ||||||
Repeat | 679-696 | 17 | ||||
Sequence: NTGSGQGGSWGTGGRTEP | ||||||
Repeat | 697-714 | 18 | ||||
Sequence: NTGSGQGGSWSTGGRTEP | ||||||
Repeat | 715-732 | 19 | ||||
Sequence: NTGSGQGGSWGTGGRTEP | ||||||
Repeat | 733-750 | 20 | ||||
Sequence: NTGSAQGGSWGTGGRTEP | ||||||
Repeat | 751-768 | 21 | ||||
Sequence: NTGSAQGGSWGTGGSTAT | ||||||
Repeat | 769-786 | 22; approximate | ||||
Sequence: NTGSAQGGGGYAAGGTGA | ||||||
Compositional bias | 785-804 | Polar residues | ||||
Sequence: GAQTGSGSTSTHSAHSASGG | ||||||
Region | 831-857 | Disordered | ||||
Sequence: RRRVSTSSTTSSSSGGGHAGAAAGGGG | ||||||
Compositional bias | 832-847 | Polar residues | ||||
Sequence: RRVSTSSTTSSSSGGG | ||||||
Compositional bias | 885-940 | Polar residues | ||||
Sequence: GASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAA | ||||||
Region | 885-966 | Disordered | ||||
Sequence: GASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP |
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
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length966
- Mass (Da)97,314
- Last updated1991-02-01 v2
- Checksum410520898AA799EE
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: Q | ||||||
Compositional bias | 208-246 | Polar residues | ||||
Sequence: ETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVP | ||||||
Compositional bias | 262-308 | Polar residues | ||||
Sequence: NEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFH | ||||||
Compositional bias | 318-352 | Polar residues | ||||
Sequence: RDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKD | ||||||
Compositional bias | 371-775 | Polar residues | ||||
Sequence: SLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQG | ||||||
Compositional bias | 785-804 | Polar residues | ||||
Sequence: GAQTGSGSTSTHSAHSASGG | ||||||
Compositional bias | 832-847 | Polar residues | ||||
Sequence: RRVSTSSTTSSSSGGG | ||||||
Compositional bias | 885-940 | Polar residues | ||||
Sequence: GASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAA |
Keywords
- Technical term