ID   FIBB_SHEEP              Reviewed;          20 AA.
AC   P68116; P14470;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Fibrinogen beta chain;
DE   Contains:
DE     RecName: Full=Fibrinopeptide B;
DE   Flags: Fragment;
GN   Name=FGB;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE, AND SULFATION AT TYR-5.
RA   Blombaeck B., Blombaeck M., Grondahl N.J.;
RT   "Studies on fibrinopeptides from mammals.";
RL   Acta Chem. Scand. 19:1789-1791(1965).
CC   -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC       together with fibrinogen alpha (FGA) 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       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. Maternal fibrinogen is essential for successful
CC       pregnancy. Fibrin deposition is also associated with infection, where
CC       it protects against IFNG-mediated hemorrhage. May also facilitate the
CC       antibacterial immune response via both innate and T-cell mediated
CC       pathways. {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:P02675}.
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:P02675}.
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.
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DR   AlphaFoldDB; P68116; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Blood coagulation; Coiled coil;
KW   Direct protein sequencing; Disulfide bond; Hemostasis; Immunity;
KW   Innate immunity; Reference proteome; Secreted; Sulfation.
FT   PEPTIDE         1..20
FT                   /note="Fibrinopeptide B"
FT                   /id="PRO_0000009087"
FT   MOD_RES         5
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|Ref.1"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2339 MW;  FCF5B6FF0DEC6627 CRC64;
     GYLDYDEVDD NRAKLPLDAR