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Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Gallus gallus (Chicken)
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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi666CalciumBy similarity1
Metal bindingi668CalciumBy similarity1
Metal bindingi670Calcium; via carbonyl oxygenBy similarity1
Metal bindingi672Calcium; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
PeptideiPRO_000000904619 – 33Fibrinopeptide AAdd BLAST15
ChainiPRO_000000904734 – 741Fibrinogen alpha chainAdd BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Pyrrolidone carboxylic acid1
Disulfide bondi46Interchain (with alpha chain)1 Publication
Disulfide bondi55Interchain (with beta chain)1 Publication
Disulfide bondi64Interchain (with gamma chain)1 Publication
Disulfide bondi68Interchain (with beta chain)1 Publication
Disulfide bondi180Interchain (with gamma chain)1 Publication
Disulfide bondi184Interchain (with beta chain)1 Publication
Disulfide bondi310 ↔ 341PROSITE-ProRule annotation
Disulfide bondi674 ↔ 687By 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei33 – 34Cleavage; by thrombin; to release fibrinopeptide A2

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP14448.
PRIDEiP14448.

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.2 Publications

Protein-protein interaction databases

STRINGi9031.ENSGALP00000015061.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni60 – 62Combined sources3
Helixi70 – 97Combined sources28
Turni98 – 100Combined sources3
Helixi101 – 178Combined sources78
Turni179 – 183Combined sources5
Beta strandi184 – 186Combined sources3
Turni194 – 197Combined sources4
Helixi198 – 207Combined sources10
Turni232 – 235Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50A/D19-505[»]
1M1JX-ray2.70A/D19-505[»]
DisProtiDP00233.
ProteinModelPortaliP14448.
SMRiP14448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14448.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini498 – 739Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST242

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili67 – 5062 PublicationsAdd BLAST440

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.2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP14448.
PhylomeDBiP14448.

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: P14448-1) [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
MIPVTILCVL LCLNLAWAQD GKTTFEKEGG GGRGPRILEN MHESSCKYEK
60 70 80 90 100
NWPICVDDDW GTKCPSCCRM QGIIDDTDQN YSQRIDNIRQ QLADSQNKYK
110 120 130 140 150
TSNRVIVETI NILKPGLEGA QQLDENYGHV STELRRRIVT LKQRVATQVN
160 170 180 190 200
RIKALQNSIQ EQVVEMKRLE VDIDIKIRAC KGSCARSFDY QVDKEGYDNI
210 220 230 240 250
QKHLTQASSI DMHPDFQTTT LSTLKMRPLK DSNVPEHFKL KPSPEMQAMS
260 270 280 290 300
AFNNIKQMQV VLERPETDHV AEARGDSSPS HTGKLITSSH RRESPSLVDK
310 320 330 340 350
TSSASSVHRC TRTVTKKVIS GPDGPREEIV EKMVSSDGSD CSHLQGGREG
360 370 380 390 400
STYHFSGTGD FHKLDRLLPD LESFFTHDSV STSSRHSIGS STSSHVTGAG
410 420 430 440 450
SSHLGTGGKD KFTDLGEEEE DDFGGLQPSG FAAGSASHSK TVLTSSSSSF
460 470 480 490 500
NKGGSTFETK SLKTRETSEQ LGGVQHDQSA EDTPDFKARS FRPAAMSTRR
510 520 530 540 550
SYNGKDCDDI RQKHTSGAKS GIFKIKPEGS NKVLSVYCDQ ETTLGGWLLI
560 570 580 590 600
QQRMDGSVNF NRTWQDYRRG FGSVDGKGQG ELWLGNENIH LLTQNDTLLR
610 620 630 640 650
VELEDWDGNA AYAEYIVQVG TEAEGYALTV SSYEGTAGDA LVAGWLEEGS
660 670 680 690 700
EYTSHAQMQF STFDRDQDHW EESCAEVYGG GWWYNSCQAA NLNGIYYPGG
710 720 730 740
HYDPRYNVPY EIENGVVWIP FRASDYSLKV VRMKIRPLET L
Length:741
Mass (Da):82,438
Last modified:October 1, 1996 - v4
Checksum:iA09F5F4F186DE3A6
GO
Isoform 2 (identifier: P14448-2) [UniParc]FASTAAdd to basket
Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     506-509: DCDD → GTQK
     510-741: Missing.

Show »
Length:509
Mass (Da):56,174
Checksum:iF102655C269D290B
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001535506 – 509DCDD → GTQK in isoform 2. Curated4
Alternative sequenceiVSP_001536510 – 741Missing in isoform 2. CuratedAdd BLAST232

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20803
, U20799, U20800, U20801, U20802 Genomic DNA. Translation: AAB60686.1.
U20803
, U20799, U20800, U20801, U20802 Genomic DNA. Translation: AAB60685.1.
M34096 mRNA. Translation: AAA99306.1.
M34096 mRNA. Translation: AAA99307.1.
UniGeneiGga.34280.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20803
, U20799, U20800, U20801, U20802 Genomic DNA. Translation: AAB60686.1.
U20803
, U20799, U20800, U20801, U20802 Genomic DNA. Translation: AAB60685.1.
M34096 mRNA. Translation: AAA99306.1.
M34096 mRNA. Translation: AAA99307.1.
UniGeneiGga.34280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50A/D19-505[»]
1M1JX-ray2.70A/D19-505[»]
DisProtiDP00233.
ProteinModelPortaliP14448.
SMRiP14448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000015061.

Proteomic databases

PaxDbiP14448.
PRIDEiP14448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP14448.
PhylomeDBiP14448.

Miscellaneous databases

EvolutionaryTraceiP14448.

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_CHICK
AccessioniPrimary (citable) accession number: P14448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.