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Fibrinogen beta chain [Cleaved into: Fibrinopeptide B] (Fragment)

 FIBB_CEREN              Reviewed;          21 AA.
P68119; P14468;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
10-MAY-2017, entry version 31.
RecName: Full=Fibrinogen beta chain;
Contains:
RecName: Full=Fibrinopeptide B;
Flags: Fragment;
Name=FGB;
Cervus elaphus nelsoni (Rocky Mountain elk) (Cervus canadensis
nelsoni).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Cervidae; Cervinae; Cervus.
NCBI_TaxID=9864;
[1]
PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND SULFATION AT
TYR-6.
Mross G.A., Doolittle R.F.;
"Amino acid sequence studies on artiodacty fibrinopeptides.";
Arch. Biochem. Biophys. 122:674-684(1967).
-!- FUNCTION: Cleaved by the protease thrombin to yield monomers
which, together with fibrinogen alpha (FGA) and fibrinogen gamma
(FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a
major function in hemostasis as one of the primary components of
blood clots. In addition, functions during the early stages of
wound repair to stabilize the lesion and guide cell migration
during re-epithelialization. Was originally thought to be
essential for platelet aggregation, based on in vitro studies
using anticoagulated blood. However subsequent studies have shown
that it is not absolutely required for thrombus formation in vivo.
Enhances expression of SELP in activated platelets. Maternal
fibrinogen is essential for successful pregnancy. Fibrin
deposition is also associated with infection, where it protects
against IFNG-mediated hemorrhage. May also facilitate the
antibacterial immune response via both innate and T-cell mediated
pathways. {ECO:0000250|UniProtKB:E9PV24}.
-!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3
non-identical chains (alpha, beta and gamma). The 2 heterotrimers
are in head to head conformation with the N-termini in a small
central domain (By similarity). {ECO:0000250|UniProtKB:P02675}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DOMAIN: A long coiled coil structure formed by 3 polypeptide
chains connects the central nodule to the C-terminal domains
(distal nodules). The long C-terminal ends of the alpha chains
fold back, contributing a fourth strand to the coiled coil
structure. {ECO:0000250|UniProtKB:P02675}.
-!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin,
which cleaves fibrinopeptides A and B from alpha and beta chains,
and thus exposes the N-terminal polymerization sites responsible
for the formation of the soft clot.
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GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
1: Evidence at protein level;
Adaptive immunity; Blood coagulation; Coiled coil;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
Immunity; Innate immunity; Pyrrolidone carboxylic acid; Secreted;
Sulfation.
PEPTIDE 1 21 Fibrinopeptide B.
/FTId=PRO_0000009063.
MOD_RES 1 1 Pyrrolidone carboxylic acid.
{ECO:0000269|Ref.1}.
MOD_RES 6 6 Sulfotyrosine. {ECO:0000269|Ref.1}.
CARBOHYD 4 4 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P02676}.
NON_TER 21 21
SEQUENCE 21 AA; 2558 MW; FCEE745D98931627 CRC64;
QHSTDYDEEE EDRAKLHLDA R


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