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P06399 (FIBA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrinogen alpha chain

Cleaved into the following 2 chains:

  1. Fibrinopeptide A
  2. Fibrinogen alpha chain
Gene names
Name:Fga
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
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

The alpha chain is not glycosylated.

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. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.

Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.

Phosphorylation sites are present in the extracellular medium By similarity.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06399-1)

Also known as: Alpha-E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06399-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     547-550: DCDD → GIHA
     551-782: Missing.
Note: Major isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.3
Peptide20 – 3617Fibrinopeptide A Ref.3
PRO_0000009039
Chain37 – 782746Fibrinogen alpha chain
PRO_0000009038

Regions

Domain539 – 780242Fibrinogen C-terminal
Coiled coil68 – 547480 By similarity

Sites

Site36 – 372Cleavage; by thrombin; to release fibrinopeptide A

Amino acid modifications

Glycosylation6021N-linked (GlcNAc...) Potential
Disulfide bond48Interchain By similarity
Disulfide bond56Interchain (with beta chain) By similarity
Disulfide bond65Interchain (with C-49 in gamma chain) By similarity
Disulfide bond69Interchain (with beta chain) By similarity
Disulfide bond181Interchain (with C-165 in gamma chain) By similarity
Disulfide bond185Interchain (with beta chain) By similarity
Disulfide bond404 ↔ 434 By similarity

Natural variations

Alternative sequence547 – 5504DCDD → GIHA in isoform 2.
VSP_001533
Alternative sequence551 – 782232Missing in isoform 2.
VSP_001534

Experimental info

Sequence conflict30 – 345EAGGD → DEGAG AA sequence Ref.3
Sequence conflict1401Q → E no nucleotide entry Ref.2
Sequence conflict2121D → E no nucleotide entry Ref.2
Sequence conflict270 – 2767ASRGDLP → LREEIYQ Ref.2
Sequence conflict4731S → K in AAA41158. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha-E) [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 744834DAE76D34C2

FASTA78286,686
        10         20         30         40         50         60 
MLSLRVACLI LSLASTVWTA DTGTTSEFIE AGGDIRGPRI VERQPSQCKE TDWPFCSDED 

        70         80         90        100        110        120 
WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQKNN KDSNSLTRNI MEYLRGDFAN 

       130        140        150        160        170        180 
ANNFDNTFGQ VSEDLRRRIQ ILKRKVIEKA QQIQVLQKDV RDQLIDMKRL EVDIDIKIRS 

       190        200        210        220        230        240 
CKGSCSRSVS REINLKDYEG QQKQLEQVIA KDLLPAKDRQ YLPAIKMSPV PDLVPGSFKS 

       250        260        270        280        290        300 
QLQEGPPEWK ALTEMRQMRM ELERPGKDGA SRGDLPGDSR GDSATRGPGS KIENPMTPGH 

       310        320        330        340        350        360 
GGSGYWRPGS SGSGSDGNWG SGTTGSDDTG TWGAGSSRPS SGSGNLKPSN PDWGEFSEFG 

       370        380        390        400        410        420 
GSSSPATRKE YHTGKLVTSK GDKELLIGNE KVTSTGTSTT RRSCSKTITK TVLGNDGHRE 

       430        440        450        460        470        480 
VVKEVVTSDD GSDCGDGMDL GLTHSFSGRL DELSRMHPEL GSFYDSRFGS LTSNFKEFGS 

       490        500        510        520        530        540 
KTSDSDIFTD IENPSSHVPE FSSSSKTSTV RKQVTKSYKM ADEAASEAHQ EGDTRTTKRG 

       550        560        570        580        590        600 
RARTMRDCDD VLQTHPSGAQ NGIFSIKLPG SSKIFSVYCD QETSLGGWLL IQQRMDGSLN 

       610        620        630        640        650        660 
FNRTWQDYKR GFGSLNDKGE GEFWLGNDYL HLLTLRGSVL RVELEDWAGK EAYAEYHFRV 

       670        680        690        700        710        720 
GSEAEGYALQ VSSYQGTAGD ALMEGSVEEG TEYTSHSNMQ FSTFDRDADQ WEENCAEVYG 

       730        740        750        760        770        780 
GGWWYNSCQA ANLNGIYYPG GTYDPRNNSP YEIENGVLWV PFRGADYSLW AVRMKIRPLV 


GQ 

« Hide

Isoform 2 (Alpha) [UniParc].

Checksum: 24C2E1470DD2C7BF
Show »

FASTA55060,490

References

[1]"Fibrinogen alpha genes: conservation of bipartite transcripts and carboxy-terminal-extended alpha subunits in vertebrates."
Fu Y., Cao Y., Hertzberg K.M., Grieninger G.
Genomics 30:71-76(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evolution and structure of the fibrinogen genes. Random insertion of introns or selective loss?"
Crabtree G.R., Comeau C.M., Fowlkes D.M., Fornace A.J. Jr., Malley J.D., Kant J.A.
J. Mol. Biol. 185:1-19(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[3]"Studies on fibrinopeptides from mammals."
Blombaeck B., Blombaeck M., Grondahl N.J.
Acta Chem. Scand. 19:1789-1791(1965)
Cited for: PROTEIN SEQUENCE OF 20-36.
[4]"Molecular cloning of mRNA sequences transiently induced during rat liver regeneration."
Sobczak J., Lotti A.-M., Taroux P., Duguet M.
Exp. Cell Res. 169:47-56(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 458-550 (ISOFORM 2).
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86561 Genomic DNA. Translation: CAA60264.1.
X86561 Genomic DNA. Translation: CAA60263.1.
M35601 mRNA. Translation: AAA41158.1.
PIRI53408.
UniGeneRn.98846.

3D structure databases

ProteinModelPortalP06399.
SMRP06399. Positions 46-93, 131-215, 586-782.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP06399.
PRIDEP06399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2603. rat. [P06399-1]

Organism-specific databases

RGD2603. Fga.

Phylogenomic databases

eggNOGNOG114889.
HOGENOMHOG000285947.
HOVERGENHBG005668.
InParanoidP06399.

Gene expression databases

GenevestigatorP06399.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP06399.
PROP06399.

Entry information

Entry nameFIBA_RAT
AccessionPrimary (citable) accession number: P06399
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families