Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P14448

- FIBA_CHICK

UniProt

P14448 - FIBA_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Gallus gallus (Chicken)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei33 – 342Cleavage; by thrombin; to release fibrinopeptide A

GO - Biological processi

  1. platelet activation Source: InterPro
  2. protein polymerization Source: InterPro
  3. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. fibrinogen complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Peptidei19 – 3315Fibrinopeptide APRO_0000009046Add
BLAST
Chaini34 – 741708Fibrinogen alpha chainPRO_0000009047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid
Disulfide bondi46 – 46Interchain (with alpha chain)
Disulfide bondi55 – 55Interchain (with beta chain)
Disulfide bondi64 – 64Interchain (with gamma chain)
Disulfide bondi68 – 68Interchain (with beta chain)
Disulfide bondi180 – 180Interchain (with gamma chain)
Disulfide bondi184 – 184Interchain (with beta chain)
Disulfide bondi310 ↔ 341PROSITE-ProRule annotation

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.

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP14448.

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

STRINGi9031.ENSGALP00000015061.

Structurei

Secondary structure

1
741
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni60 – 623Combined sources
Helixi70 – 9728Combined sources
Turni98 – 1003Combined sources
Helixi101 – 17878Combined sources
Turni179 – 1835Combined sources
Beta strandi184 – 1863Combined sources
Turni194 – 1974Combined sources
Helixi198 – 20710Combined sources
Turni232 – 2354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50A/D19-505[»]
1M1JX-ray2.70A/D19-505[»]
DisProtiDP00233.
ProteinModelPortaliP14448.
SMRiP14448. Positions 45-238, 545-740.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14448.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini498 – 739242Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 506440Add
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.
InParanoidiP14448.
PhylomeDBiP14448.

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei506 – 5094DCDD → GTQK in isoform 2. CuratedVSP_001535
Alternative sequencei510 – 741232Missing in isoform 2. CuratedVSP_001536Add
BLAST

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 .
UniGenei Gga.34280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EI3 X-ray 5.50 A/D 19-505 [» ]
1M1J X-ray 2.70 A/D 19-505 [» ]
DisProti DP00233.
ProteinModelPortali P14448.
SMRi P14448. Positions 45-238, 545-740.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000015061.

Proteomic databases

PaxDbi P14448.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG114889.
HOGENOMi HOG000285947.
HOVERGENi HBG005668.
InParanoidi P14448.
PhylomeDBi P14448.

Miscellaneous databases

EvolutionaryTracei P14448.
PROi P14448.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR014716. 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 ]
Pfami PF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Greininger G.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-4.
  2. "Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gamma-fibrinogens."
    Weissbach L., Grieninger G.
    Proc. Natl. Acad. Sci. U.S.A. 87:5198-5202(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-741.
  3. Cited for: PROTEIN SEQUENCE OF 19-33.
  4. "Crystal structure of native chicken fibrinogen at 5.5-A resolution."
    Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.
    Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 19-509.
  5. "Crystal structure of native chicken fibrinogen at 2.7 A resolution."
    Yang Z., Kollman J.M., Pandi L., Doolittle R.F.
    Biochemistry 40:12515-12523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-509.

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 26, 2014
This is version 111 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

External Data

Dasty 3