Reviewed, UniProtKB/Swiss-Prot P02677 (FIBB_CANFA)

Names and origin

Protein names

Recommended name:
    Fibrinogen beta chain
Cleaved into the following chain:
    1- Recommended name:
            Fibrinopeptide B

Gene names

Name:

FGB

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	31 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Subunit structure	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.
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.
Post-translational modification	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.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	Coiled coil
PTM	Disulfide bond Sulfation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	platelet activation Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	fibrinogen complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding, bridging Inferred from electronic annotation. Source: InterPro receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 19	19	Fibrinopeptide B		PRO_0000009059
	Chain	20 – ›31	›12	Fibrinogen beta chain		PRO_0000009060
Amino acid modifications
	Modified residue	2	1	Sulfotyrosine; partial
	Modified residue	3	1	Sulfotyrosine
Experimental info
	Non-terminal residue	31	1

Sequences

	Sequence		Length	Mass (Da)
	P02677-1 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: A043727257698156	FASTA	31	3,731
	10 20 30 HYYDDTDEEE RIVSTVDARG HRPLDKKREE A

References

[1]	"Studies of the structure of canine fibrinogen." Birken S., Wilner G.D., Canfield R.E. Thromb. Res. 7:599-610(1975) [PubMed: 1198547] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Studies on fibrinopeptides from mammals." Blombaeck B., Blombaeck M., Grondahl N.J. Acta Chem. Scand. 19:1789-1791(1965) Cited for: PROTEIN SEQUENCE OF 1-19.
[3]	"The location of tyrosine-O-sulphate in fibrinopeptides." Krajewski T., Blombaeck B. Acta Chem. Scand. 22:1339-1346(1968) [PubMed: 5727635] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19.

Cross-references

Sequence databases
PIR	A05297. B94308.
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFG00000008424. Canis familiaris. [Contig view]
Phylogenomic databases
HOVERGEN	P02677.
Family and domain databases
InterPro	IPR002181. Fibrinogen_a/b/g_C. IPR018986. Fibrinogen_bsu_coiled-coil_N. [Graphical view]
Pfam	PF09389. Fib_beta. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FIBB_CANFA

Accession

Primary (citable) accession number: P02677

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)