ID   FIBA_ANAPL              Reviewed;          15 AA.
AC   P12801;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Fibrinogen alpha chain;
DE   Contains:
DE     RecName: Full=Fibrinopeptide A;
DE   Flags: Fragment;
GN   Name=FGA;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RX   PubMed=3983613;
RA   Min Y., Ping Z., Yaoshi Z.;
RT   "Purification and primary structures of duck fibrinopeptides A and B.";
RL   Sci. Sin., Ser. B Chem. Biol. Agric. Med. Earth Sci. 28:31-35(1985).
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.
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; JP0101; JP0101.
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; Pyrrolidone carboxylic acid; Secreted.
FT   PEPTIDE         1..15
FT                   /note="Fibrinopeptide A"
FT                   /id="PRO_0000009045"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3983613"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1580 MW;  D78A51FF88B40373 CRC64;
     QDGKSSFQKE GGGVR