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Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A] (Fragment)

 FIBA_VULVU              Reviewed;          16 AA.
P68212; P02673; P14464;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
20-JAN-2016, entry version 31.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Flags: Fragment;
Name=FGA;
Vulpes vulpes (Red fox).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Vulpes.
NCBI_TaxID=9627;
[1]
PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-3.
Blombaeck B., Blombaeck M., Grondahl N.J.;
"Studies on fibrinopeptides from mammals.";
Acta Chem. Scand. 19:1789-1791(1965).
-!- 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. {ECO:0000250|UniProtKB:E9PV24}.
-!- 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). {ECO:0000250|UniProtKB:P02671}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- 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. {ECO:0000250|UniProtKB:P02671}.
-!- PTM: 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.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers.
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GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
1: Evidence at protein level;
Adaptive immunity; Blood coagulation; Coiled coil;
Direct protein sequencing; Disulfide bond; Hemostasis; Immunity;
Innate immunity; Phosphoprotein; Secreted.
PEPTIDE 1 16 Fibrinopeptide A.
/FTId=PRO_0000009044.
MOD_RES 3 3 Phosphoserine. {ECO:0000269|Ref.1}.
CONFLICT 2 2 N -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 4 7 KEGE -> EGKQ (in Ref. 1; AA sequence).
{ECO:0000305}.
NON_TER 16 16
SEQUENCE 16 AA; 1651 MW; 09598EB6319A9E66 CRC64;
TNSKEGEFIA EGGGVR


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