ID   FIBG_CANLF              Reviewed;          24 AA.
AC   P12800;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Fibrinogen gamma chain;
DE   Flags: Fragment;
GN   Name=FGG;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=1198547; DOI=10.1016/0049-3848(75)90106-1;
RA   Birken S., Wilner G.D., Canfield R.E.;
RT   "Studies of the structure of canine fibrinogen.";
RL   Thromb. Res. 7:599-610(1975).
CC   -!- FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta
CC       (FGB), polymerizes to form an insoluble fibrin matrix. Has a major
CC       function in hemostasis as one of the primary components of blood clots.
CC       In addition, functions during the early stages of wound repair to
CC       stabilize the lesion and guide cell migration during re-
CC       epithelialization. Was originally thought to be essential for platelet
CC       aggregation, based on in vitro studies using anticoagulated blood.
CC       However, subsequent studies have shown that it is not absolutely
CC       required for thrombus formation in vivo. Enhances expression of SELP in
CC       activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen
CC       is essential for successful pregnancy. Fibrin deposition is also
CC       associated with infection, where it protects against IFNG-mediated
CC       hemorrhage. May also facilitate the antibacterial immune response via
CC       both innate and T-cell mediated pathways.
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:P02679}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1198547}.
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:P02679}.
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.
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DR   PIR; A05298; A05298.
DR   AlphaFoldDB; P12800; -.
DR   STRING; 9615.ENSCAFP00000012417; -.
DR   PaxDb; P12800; -.
DR   PRIDE; P12800; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR   Pfam; PF08702; Fib_alpha; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Coiled coil; Direct protein sequencing; Disulfide bond;
KW   Hemostasis; Reference proteome; Secreted.
FT   CHAIN           1..>24
FT                   /note="Fibrinogen gamma chain"
FT                   /id="PRO_0000099062"
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2690 MW;  D427050783F52628 CRC64;
     YTATRDNCCI LDERFGSYCP TTCG