ID   FIBA_TILRU              Reviewed;          14 AA.
AC   Q7LZT3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 27.
DE   RecName: Full=Fibrinogen alpha chain;
DE   Contains:
DE     RecName: Full=Fibrinopeptide A;
DE   Flags: Fragment;
GN   Name=FGA {ECO:0000250|UniProtKB:P02671};
OS   Tiliqua rugosa (Shingleback lizard) (Trachydosaurus rugosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Scinciformata; Scincidae;
OC   Egerniinae; Tiliqua.
OX   NCBI_TaxID=8527;
RN   [1] {ECO:0000305, ECO:0000312|PIR:A32654}
RP   PROTEIN SEQUENCE.
RA   Blombaeck B., Blombaeck M.;
RL   (In) Hawkes J.G. (eds.);
RL   Chemotaxonomy and serotaxonomy, pp.3-20, Academic Press, London and New
RL   York (1968).
CC   -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC       together with fibrinogen beta (FGB) and fibrinogen gamma (FGG),
CC       polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC       function in hemostasis as one of the primary components of blood clots.
CC       {ECO:0000250|UniProtKB:E9PV24}.
CC   -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC       identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC       head to head conformation with the N-termini in a small central domain
CC       (By similarity). {ECO:0000250|UniProtKB:P02671}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}.
CC   -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC       connects the central nodule to the C-terminal domains (distal nodules).
CC       The long C-terminal ends of the alpha chains fold back, contributing a
CC       fourth strand to the coiled coil structure.
CC       {ECO:0000250|UniProtKB:P02671}.
CC   -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC       cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC       exposes the N-terminal polymerization sites responsible for the
CC       formation of the soft clot. The soft clot is converted into the hard
CC       clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC       cross-linking between gamma chains (stronger) and between alpha chains
CC       (weaker) of different monomers.
CC   -!- PTM: Forms F13A-mediated cross-links between a glutamine and the
CC       epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen
CC       heteropolymers.
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DR   PIR; A32654; A32654.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation; Coiled coil; Direct protein sequencing; Disulfide bond;
KW   Hemostasis; Secreted.
FT   PEPTIDE         1..14
FT                   /note="Fibrinopeptide A"
FT                   /id="PRO_0000252047"
FT   NON_TER         14
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   14 AA;  1491 MW;  638C9BA321E96A1B CRC64;
     EDTGTFEEGH GGVR