P14475 (FIBB_MUNMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibrinogen beta chain

Cleaved into the following chain:

1. Fibrinopeptide B

Gene names

Name:

FGB

Organism

Muntiacus muntjak (Barking deer) (Indian muntjac)

Taxonomic identifier

9888 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Cervidae › Muntiacinae › Muntiacus

Protein attributes

Sequence length	21 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 Pyrrolidone carboxylic acid Sulfation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 21	21	Fibrinopeptide B		PRO_0000009079
Amino acid modifications
	Modified residue	1	1	Pyrrolidone carboxylic acid
	Modified residue	6	1	Sulfotyrosine
Experimental info
	Non-terminal residue	21	1

Sequences

	Sequence		Length	Mass (Da)
	P14475 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: FCEE75188F0C1627	FASTA	21	2,514
	10 20 QHSTDYDEVE DDRAKLHLDA R

References

[1]	"Amino acid sequence studies on artiodacty fibrinopeptides." Mross G.A., Doolittle R.F. Arch. Biochem. Biophys. 122:674-684(1967) Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

FIBB_MUNMU

Accession

Primary (citable) accession number: P14475

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1994
Last modified:	March 2, 2010
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program