Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P14448

- FIBA_CHICK

UniProt

P14448 - FIBA_CHICK

Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 4 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.

    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

    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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. fibrinogen complex Source: InterPro

    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 – 623
    Helixi70 – 9728
    Turni98 – 1003
    Helixi101 – 17878
    Turni179 – 1835
    Beta strandi184 – 1863
    Turni194 – 1974
    Helixi198 – 20710
    Turni232 – 2354

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MIPVTILCVL LCLNLAWAQD GKTTFEKEGG GGRGPRILEN MHESSCKYEK    50
    NWPICVDDDW GTKCPSCCRM QGIIDDTDQN YSQRIDNIRQ QLADSQNKYK 100
    TSNRVIVETI NILKPGLEGA QQLDENYGHV STELRRRIVT LKQRVATQVN 150
    RIKALQNSIQ EQVVEMKRLE VDIDIKIRAC KGSCARSFDY QVDKEGYDNI 200
    QKHLTQASSI DMHPDFQTTT LSTLKMRPLK DSNVPEHFKL KPSPEMQAMS 250
    AFNNIKQMQV VLERPETDHV AEARGDSSPS HTGKLITSSH RRESPSLVDK 300
    TSSASSVHRC TRTVTKKVIS GPDGPREEIV EKMVSSDGSD CSHLQGGREG 350
    STYHFSGTGD FHKLDRLLPD LESFFTHDSV STSSRHSIGS STSSHVTGAG 400
    SSHLGTGGKD KFTDLGEEEE DDFGGLQPSG FAAGSASHSK TVLTSSSSSF 450
    NKGGSTFETK SLKTRETSEQ LGGVQHDQSA EDTPDFKARS FRPAAMSTRR 500
    SYNGKDCDDI RQKHTSGAKS GIFKIKPEGS NKVLSVYCDQ ETTLGGWLLI 550
    QQRMDGSVNF NRTWQDYRRG FGSVDGKGQG ELWLGNENIH LLTQNDTLLR 600
    VELEDWDGNA AYAEYIVQVG TEAEGYALTV SSYEGTAGDA LVAGWLEEGS 650
    EYTSHAQMQF STFDRDQDHW EESCAEVYGG GWWYNSCQAA NLNGIYYPGG 700
    HYDPRYNVPY EIENGVVWIP FRASDYSLKV VRMKIRPLET L 741
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 109 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