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Reviewed, UniProtKB/Swiss-Prot P14475 (FIBB_MUNMU)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesRecommended name:
    Fibrinogen beta chain
Cleaved into the following chain:
    1- Recommended name:
            Fibrinopeptide B
Gene names
Name: FGB
OrganismMuntiacus muntjak (Barking deer) (Indian muntjac)
Taxonomic identifier9888 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeMuntiacinaeMuntiacus

Protein attributes

Sequence length21 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processBlood coagulation
   Cellular componentSecreted
   DomainCoiled coil
   PTMDisulfide bond
Pyrrolidone carboxylic acid
Sulfation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 2121Fibrinopeptide B
PRO_0000009079

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Modified residue61Sulfotyrosine

Experimental info

Non-terminal residue211

Sequences

Sequence LengthMass (Da)Tools
P14475-1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: FCEE75188F0C1627

FASTA212,514
        10         20 
QHSTDYDEVE DDRAKLHLDA R 

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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

ModBaseSearch...

Phylogenomic databases

HOVERGENP14475.

Family and domain databases

InterProIPR002181. Fibrinogen_a/b/g_C.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFIBB_MUNMU
AccessionPrimary (citable) accession number: P14475
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information