FIBB_VULVU
ID FIBB_VULVU Reviewed; 19 AA.
AC P14482;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Flags: Fragment;
GN Name=FGB;
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1]
RP PROTEIN SEQUENCE.
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; P14482; -.
DR STRING; 9627.ENSVVUP00000034637; -.
DR Proteomes; UP000286640; 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.
FT PEPTIDE 1..19
FT /note="Fibrinopeptide B"
FT /id="PRO_0000009091"
FT NON_TER 19
SQ SEQUENCE 19 AA; 2305 MW; 0B0D756C24A1F2C0 CRC64;
EYYDDTDEEE RIVSTVDAR