| Primary information |
|---|
| ID | 13585 |
| Uniprot ID | P02671 |
| Description | Fibrinogen alpha chain [Cleaved into- Fibrinopeptide A; Fibrinogen alpha chain] |
| Organism | Homo sapiens |
| Txonomy | Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata (jawed vertebrates); Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini; Hominoidea (apes); Hominidae (great apes); Homininae; Homo; Homo sapiens (Human) |
| Subcellular Location | Secreted |
| Developmental Stage | NA |
| Similarity | NA |
| Tissue Specificity | Detected in blood plasma (at protein level). |
| Post Translational Modification | The alpha chain is normally not N-glycosylated (PubMed-23151259); even though glycosylation at Asn-686 was observed when a fragment of the protein was expressed in insect cells (PubMed-9689040). It is |
| Function | Cleaved by the protease thrombin to yield monomers which; together with fibrinogen beta (FGB) and fibrinogen gamma (FGG); polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition; functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. 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. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection; where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. |
| Length | 866 |
| Molecular Weight | 94 |
| Name | Fibrinogen alpha chain |
| Sequence | PRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ |
| Sequence map | 50-26 |
| PDB ID | 1BBR; 1DM4; 1FPH; 1FZA; 1FZB; 1FZC; 1FZD; 1FZE; 1FZF; 1FZG; 1LT9; 1LTJ; 1N86; 1N8E; 1RE3; 1RE4; 1RF0 |
| Drugpedia | DB04919;DB00009;DB05099;DB00029;DB13151;DB05675;DB |
| Receptor | P06756 |
| Domain | A long coiled coil structure formed by 3 polypepti |
| Pharmaceutical Use | NA
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