FIBA_CHICK
ID FIBA_CHICK Reviewed; 741 AA.
AC P14448;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Fibrinogen alpha chain;
DE Contains:
DE RecName: Full=Fibrinopeptide A;
DE Contains:
DE RecName: Full=Fibrinogen alpha chain;
DE Flags: Precursor;
GN Name=FGA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 1-4.
RA Greininger G.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-741.
RX PubMed=2367530; DOI=10.1073/pnas.87.13.5198;
RA Weissbach L., Grieninger G.;
RT "Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an amino
RT acid sequence homologous to beta- and gamma-fibrinogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5198-5202(1990).
RN [3]
RP PROTEIN SEQUENCE OF 19-33, AND PYROGLUTAMATE FORMATION AT GLN-19.
RX PubMed=656462; DOI=10.1016/0005-2795(78)90486-5;
RA Takagi T., Finlayson J.S., Iwanaga S.;
RT "Amino acid sequence of chicken fibrinopeptide A.";
RL Biochim. Biophys. Acta 534:161-164(1978).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 19-509, SUBCELLULAR LOCATION,
RP SUBUNIT, AND COILED COIL DOMAIN.
RX PubMed=10737772; DOI=10.1073/pnas.080065697;
RA Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.;
RT "Crystal structure of native chicken fibrinogen at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-505, SUBUNIT, DISULFIDE BONDS,
RP COILED COIL DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=11601975; DOI=10.1021/bi011394p;
RA Yang Z., Kollman J.M., Pandi L., Doolittle R.F.;
RT "Crystal structure of native chicken fibrinogen at 2.7 A resolution.";
RL Biochemistry 40:12515-12523(2001).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen beta (FGB) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC {ECO:0000250|UniProtKB:E9PV24}.
CC -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC head to head conformation with the N-termini in a small central domain.
CC {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772,
CC ECO:0000269|PubMed:11601975}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha-E;
CC IsoId=P14448-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=P14448-2; Sequence=VSP_001535, VSP_001536;
CC -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC connects the central nodule to the C-terminal domains (distal nodules).
CC The long C-terminal ends of the alpha chains fold back, contributing a
CC fourth strand to the coiled coil structure.
CC {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}.
CC -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC exposes the N-terminal polymerization sites responsible for the
CC formation of the soft clot. The soft clot is converted into the hard
CC clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC cross-linking between gamma chains (stronger) and between alpha chains
CC (weaker) of different monomers.
CC -!- PTM: Forms F13A-mediated cross-links between a glutamine and the
CC epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen
CC heteropolymers.
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DR EMBL; U20803; AAB60686.1; -; Genomic_DNA.
DR EMBL; U20799; AAB60686.1; JOINED; Genomic_DNA.
DR EMBL; U20800; AAB60686.1; JOINED; Genomic_DNA.
DR EMBL; U20801; AAB60686.1; JOINED; Genomic_DNA.
DR EMBL; U20802; AAB60686.1; JOINED; Genomic_DNA.
DR EMBL; U20803; AAB60685.1; -; Genomic_DNA.
DR EMBL; U20799; AAB60685.1; JOINED; Genomic_DNA.
DR EMBL; U20800; AAB60685.1; JOINED; Genomic_DNA.
DR EMBL; U20801; AAB60685.1; JOINED; Genomic_DNA.
DR EMBL; U20802; AAB60685.1; JOINED; Genomic_DNA.
DR EMBL; M34096; AAA99306.1; -; mRNA.
DR EMBL; M34096; AAA99307.1; -; mRNA.
DR PDB; 1EI3; X-ray; 5.50 A; A/D=19-505.
DR PDB; 1M1J; X-ray; 2.70 A; A/D=19-505.
DR PDBsum; 1EI3; -.
DR PDBsum; 1M1J; -.
DR AlphaFoldDB; P14448; -.
DR SMR; P14448; -.
DR STRING; 9031.ENSGALP00000015061; -.
DR PaxDb; P14448; -.
DR VEuPathDB; HostDB:geneid_396307; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; P14448; -.
DR OrthoDB; 363208at2759; -.
DR PhylomeDB; P14448; -.
DR EvolutionaryTrace; P14448; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005577; C:fibrinogen complex; IMP:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:CAFA.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR CDD; cd00087; FReD; 1.
DR DisProt; DP00233; -.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR021996; Fibrinogen_aC.
DR InterPro; IPR037579; Fibrinogen_alpha.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF232; PTHR19143:SF232; 1.
DR Pfam; PF08702; Fib_alpha; 1.
DR Pfam; PF12160; Fibrinogen_aC; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SMART; SM01212; Fib_alpha; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW Coiled coil; Direct protein sequencing; Disulfide bond; Hemostasis;
KW Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:656462"
FT PEPTIDE 19..33
FT /note="Fibrinopeptide A"
FT /id="PRO_0000009046"
FT CHAIN 34..741
FT /note="Fibrinogen alpha chain"
FT /id="PRO_0000009047"
FT DOMAIN 498..739
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 270..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..506
FT /evidence="ECO:0000269|PubMed:10737772,
FT ECO:0000269|PubMed:11601975"
FT COMPBIAS 280..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT SITE 33..34
FT /note="Cleavage; by thrombin; to release fibrinopeptide A"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:656462"
FT DISULFID 46
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 55
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 64
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 68
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 180
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 184
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000269|PubMed:11601975"
FT DISULFID 310..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 674..687
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT VAR_SEQ 506..509
FT /note="DCDD -> GTQK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001535"
FT VAR_SEQ 510..741
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001536"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 70..97
FT /evidence="ECO:0007829|PDB:1M1J"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 101..178
FT /evidence="ECO:0007829|PDB:1M1J"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1M1J"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1M1J"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:1M1J"
SQ SEQUENCE 741 AA; 82438 MW; A09F5F4F186DE3A6 CRC64;
MIPVTILCVL LCLNLAWAQD GKTTFEKEGG GGRGPRILEN MHESSCKYEK NWPICVDDDW
GTKCPSCCRM QGIIDDTDQN YSQRIDNIRQ QLADSQNKYK TSNRVIVETI NILKPGLEGA
QQLDENYGHV STELRRRIVT LKQRVATQVN RIKALQNSIQ EQVVEMKRLE VDIDIKIRAC
KGSCARSFDY QVDKEGYDNI QKHLTQASSI DMHPDFQTTT LSTLKMRPLK DSNVPEHFKL
KPSPEMQAMS AFNNIKQMQV VLERPETDHV AEARGDSSPS HTGKLITSSH RRESPSLVDK
TSSASSVHRC TRTVTKKVIS GPDGPREEIV EKMVSSDGSD CSHLQGGREG STYHFSGTGD
FHKLDRLLPD LESFFTHDSV STSSRHSIGS STSSHVTGAG SSHLGTGGKD KFTDLGEEEE
DDFGGLQPSG FAAGSASHSK TVLTSSSSSF NKGGSTFETK SLKTRETSEQ LGGVQHDQSA
EDTPDFKARS FRPAAMSTRR SYNGKDCDDI RQKHTSGAKS GIFKIKPEGS NKVLSVYCDQ
ETTLGGWLLI QQRMDGSVNF NRTWQDYRRG FGSVDGKGQG ELWLGNENIH LLTQNDTLLR
VELEDWDGNA AYAEYIVQVG TEAEGYALTV SSYEGTAGDA LVAGWLEEGS EYTSHAQMQF
STFDRDQDHW EESCAEVYGG GWWYNSCQAA NLNGIYYPGG HYDPRYNVPY EIENGVVWIP
FRASDYSLKV VRMKIRPLET L
