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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)DescriptionActionsGraphical viewLength
Metal bindingi707CalciumBy similarity1
Metal bindingi709CalciumBy similarity1
Metal bindingi711Calcium; via carbonyl oxygenBy similarity1
Metal bindingi713Calcium; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: RGD
  • adaptive immune response Source: UniProtKB-KW
  • blood coagulation 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
  • envenomation resulting in modulation of blood coagulation in other organism Source: RGD
  • innate immune response Source: UniProtKB-KW
  • liver regeneration Source: RGD
  • platelet activation Source: InterPro
  • positive regulation of smooth muscle cell migration Source: RGD
  • protein polymerization Source: InterPro
  • response to cycloheximide Source: RGD
  • response to estradiol Source: RGD
  • response to genistein Source: RGD
  • response to growth hormone Source: RGD
  • response to insulin Source: RGD
  • response to morphine Source: RGD
  • response to thyroid hormone Source: RGD
  • response to toxic substance Source: RGD
  • response to X-ray Source: RGD
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Calcium, Metal-binding

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2603. Fga.

Subcellular locationi

  • Secreted By similarity

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
PeptideiPRO_000000903920 – 36Fibrinopeptide AAdd BLAST17
ChainiPRO_000000903837 – 782Fibrinogen alpha chainAdd BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48InterchainPROSITE-ProRule annotation
Disulfide bondi56Interchain (with beta chain)PROSITE-ProRule annotation
Disulfide bondi65Interchain (with C-49 in gamma chain)PROSITE-ProRule annotation
Disulfide bondi69Interchain (with beta chain)PROSITE-ProRule annotation
Disulfide bondi181Interchain (with C-165 in gamma chain)PROSITE-ProRule annotation
Disulfide bondi185Interchain (with beta chain)PROSITE-ProRule annotation
Modified residuei279PhosphoserineCombined sources1
Modified residuei326PhosphoserineCombined sources1
Disulfide bondi404 ↔ 434PROSITE-ProRule annotation
Modified residuei470PhosphoserineCombined sources1
Modified residuei4994-hydroxyproline; by P4HA1By similarity1
Modified residuei526PhosphoserineCombined sources1
Glycosylationi602N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi715 ↔ 728By similarity

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.
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei36 – 37Cleavage; by thrombin; to release fibrinopeptide A2
Sitei101 – 102Cleavage; by plasmin; to break down fibrin clotsBy similarity2
Sitei122 – 123Cleavage; by hementin; to prevent blood coagulationBy similarity2
Sitei124 – 125Cleavage; by plasmin; to break down fibrin clotsBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiP06399.
PeptideAtlasiP06399.
PRIDEiP06399.

PTM databases

iPTMnetiP06399.
PhosphoSitePlusiP06399.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini539 – 780Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST242

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili68 – 547By similarityAdd BLAST480

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.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP06399.
PhylomeDBiP06399.

Family and domain databases

CDDicd00087. FReD. 1 hit.
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.
SM01212. Fib_alpha. 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)DescriptionActionsGraphical viewLength
Sequence conflicti30 – 34EAGGD → DEGAG AA sequence (Ref. 3) Curated5
Sequence conflicti140Q → E no nucleotide entry (PubMed:4046033).Curated1
Sequence conflicti212D → E no nucleotide entry (PubMed:4046033).Curated1
Sequence conflicti270 – 276ASRGDLP → LREEIYQ (PubMed:4046033).Curated7
Sequence conflicti473S → K in AAA41158 (PubMed:3817019).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001533547 – 550DCDD → GIHA in isoform 2. 1 Publication4
Alternative sequenceiVSP_001534551 – 782Missing in isoform 2. 1 PublicationAdd BLAST232

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060007.

PTM databases

iPTMnetiP06399.
PhosphoSitePlusiP06399.

Proteomic databases

PaxDbiP06399.
PeptideAtlasiP06399.
PRIDEiP06399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2603. rat. [P06399-1]

Organism-specific databases

RGDi2603. Fga.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP06399.
PhylomeDBiP06399.

Miscellaneous databases

PMAP-CutDBP06399.
PROiP06399.

Family and domain databases

CDDicd00087. FReD. 1 hit.
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.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 137 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

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 one 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.