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Protein

Fibrinogen alpha chain

Gene

Fga

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) 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 via an ITGB3-dependent pathway. 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 immune response via both innate and T-cell mediated pathways.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei36 – 372Cleavage; by thrombin; to release fibrinopeptide A
Sitei101 – 1022Cleavage; by plasmin; to break down fibrin clotsBy similarity
Sitei122 – 1232Cleavage; by hementin; to prevent blood coagulationBy similarity
Sitei124 – 1252Cleavage; by plasmin; to break down fibrin clotsBy similarity

GO - Biological processi

  • acute-phase response Source: RGD
  • blood coagulation Source: RGD
  • cellular response to cytokine stimulus Source: RGD
  • cellular response to granulocyte colony-stimulating factor Source: RGD
  • cellular response to interleukin-6 Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • innate immune response Source: UniProtKB-KW
  • liver regeneration Source: RGD
  • platelet activation Source: InterPro
  • protein polymerization Source: InterPro
  • response to cycloheximide Source: RGD
  • response to estradiol Source: RGD
  • response to genistein Source: RGD
  • response to morphine Source: RGD
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Gene namesi
Name:Fga
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2603. Fga.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: RGD
  • cytoplasm Source: RGD
  • extracellular space Source: RGD
  • fibrinogen complex Source: InterPro
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Peptidei20 – 3617Fibrinopeptide APRO_0000009039Add
BLAST
Chaini37 – 782746Fibrinogen alpha chainPRO_0000009038Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 – 48InterchainPROSITE-ProRule annotation
Disulfide bondi56 – 56Interchain (with beta chain)PROSITE-ProRule annotation
Disulfide bondi65 – 65Interchain (with C-49 in gamma chain)PROSITE-ProRule annotation
Disulfide bondi69 – 69Interchain (with beta chain)PROSITE-ProRule annotation
Disulfide bondi181 – 181Interchain (with C-165 in gamma chain)PROSITE-ProRule annotation
Disulfide bondi185 – 185Interchain (with beta chain)PROSITE-ProRule annotation
Disulfide bondi404 ↔ 434PROSITE-ProRule annotation
Modified residuei499 – 49914-hydroxyproline; by P4HA1By similarity
Modified residuei526 – 5261PhosphoserineBy similarity
Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiP06399.
PRIDEiP06399.

Miscellaneous databases

PMAP-CutDBP06399.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060007.

Structurei

3D structure databases

ProteinModelPortaliP06399.
SMRiP06399. Positions 46-93, 131-215, 586-782.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini539 – 780242Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili68 – 547480By similarityAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG114889.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP06399.
PhylomeDBiP06399.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06399-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLSLRVACLI LSLASTVWTA DTGTTSEFIE AGGDIRGPRI VERQPSQCKE
60 70 80 90 100
TDWPFCSDED WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQKNN
110 120 130 140 150
KDSNSLTRNI MEYLRGDFAN ANNFDNTFGQ VSEDLRRRIQ ILKRKVIEKA
160 170 180 190 200
QQIQVLQKDV RDQLIDMKRL EVDIDIKIRS CKGSCSRSVS REINLKDYEG
210 220 230 240 250
QQKQLEQVIA KDLLPAKDRQ YLPAIKMSPV PDLVPGSFKS QLQEGPPEWK
260 270 280 290 300
ALTEMRQMRM ELERPGKDGA SRGDLPGDSR GDSATRGPGS KIENPMTPGH
310 320 330 340 350
GGSGYWRPGS SGSGSDGNWG SGTTGSDDTG TWGAGSSRPS SGSGNLKPSN
360 370 380 390 400
PDWGEFSEFG GSSSPATRKE YHTGKLVTSK GDKELLIGNE KVTSTGTSTT
410 420 430 440 450
RRSCSKTITK TVLGNDGHRE VVKEVVTSDD GSDCGDGMDL GLTHSFSGRL
460 470 480 490 500
DELSRMHPEL GSFYDSRFGS LTSNFKEFGS KTSDSDIFTD IENPSSHVPE
510 520 530 540 550
FSSSSKTSTV RKQVTKSYKM ADEAASEAHQ EGDTRTTKRG RARTMRDCDD
560 570 580 590 600
VLQTHPSGAQ NGIFSIKLPG SSKIFSVYCD QETSLGGWLL IQQRMDGSLN
610 620 630 640 650
FNRTWQDYKR GFGSLNDKGE GEFWLGNDYL HLLTLRGSVL RVELEDWAGK
660 670 680 690 700
EAYAEYHFRV GSEAEGYALQ VSSYQGTAGD ALMEGSVEEG TEYTSHSNMQ
710 720 730 740 750
FSTFDRDADQ WEENCAEVYG GGWWYNSCQA ANLNGIYYPG GTYDPRNNSP
760 770 780
YEIENGVLWV PFRGADYSLW AVRMKIRPLV GQ
Length:782
Mass (Da):86,686
Last modified:October 1, 1996 - v3
Checksum:i744834DAE76D34C2
GO
Isoform 2 (identifier: P06399-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:550
Mass (Da):60,490
Checksum:i24C2E1470DD2C7BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 345EAGGD → DEGAG AA sequence (Ref. 3) Curated
Sequence conflicti140 – 1401Q → E no nucleotide entry (PubMed:4046033).Curated
Sequence conflicti212 – 2121D → E no nucleotide entry (PubMed:4046033).Curated
Sequence conflicti270 – 2767ASRGDLP → LREEIYQ (PubMed:4046033).Curated
Sequence conflicti473 – 4731S → K in AAA41158 (PubMed:3817019).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei547 – 5504DCDD → GIHA in isoform 2. 1 PublicationVSP_001533
Alternative sequencei551 – 782232Missing in isoform 2. 1 PublicationVSP_001534Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86561 Genomic DNA. Translation: CAA60264.1.
X86561 Genomic DNA. Translation: CAA60263.1.
M35601 mRNA. Translation: AAA41158.1.
PIRiI53408.
UniGeneiRn.98846.

Genome annotation databases

UCSCiRGD:2603. rat. [P06399-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86561 Genomic DNA. Translation: CAA60264.1.
X86561 Genomic DNA. Translation: CAA60263.1.
M35601 mRNA. Translation: AAA41158.1.
PIRiI53408.
UniGeneiRn.98846.

3D structure databases

ProteinModelPortaliP06399.
SMRiP06399. Positions 46-93, 131-215, 586-782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060007.

Proteomic databases

PaxDbiP06399.
PRIDEiP06399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2603. rat. [P06399-1]

Organism-specific databases

RGDi2603. Fga.

Phylogenomic databases

eggNOGiNOG114889.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP06399.
PhylomeDBiP06399.

Miscellaneous databases

PMAP-CutDBP06399.
PROiP06399.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFIBA_RAT
AccessioniPrimary (citable) accession number: P06399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.