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Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]

 FIBA_CHICK              Reviewed;         741 AA.
P14448;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 4.
23-MAY-2018, entry version 129.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=FGA;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE OF 1-4.
Greininger G.;
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-741.
PubMed=2367530; DOI=10.1073/pnas.87.13.5198;
Weissbach L., Grieninger G.;
"Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an
amino acid sequence homologous to beta- and gamma-fibrinogens.";
Proc. Natl. Acad. Sci. U.S.A. 87:5198-5202(1990).
[3]
PROTEIN SEQUENCE OF 19-33, AND PYROGLUTAMATE FORMATION AT GLN-19.
PubMed=656462; DOI=10.1016/0005-2795(78)90486-5;
Takagi T., Finlayson J.S., Iwanaga S.;
"Amino acid sequence of chicken fibrinopeptide A.";
Biochim. Biophys. Acta 534:161-164(1978).
[4]
X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 19-509, SUBCELLULAR LOCATION,
SUBUNIT, AND COILED COIL DOMAIN.
PubMed=10737772; DOI=10.1073/pnas.080065697;
Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.;
"Crystal structure of native chicken fibrinogen at 5.5-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-505, SUBUNIT, DISULFIDE
BONDS, COILED COIL DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=11601975; DOI=10.1021/bi011394p;
Yang Z., Kollman J.M., Pandi L., Doolittle R.F.;
"Crystal structure of native chicken fibrinogen at 2.7 A resolution.";
Biochemistry 40:12515-12523(2001).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:E9PV24}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10737772,
ECO:0000269|PubMed:11601975}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772,
ECO:0000269|PubMed:11601975}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha-E;
IsoId=P14448-1; Sequence=Displayed;
Name=2; Synonyms=Alpha;
IsoId=P14448-2; Sequence=VSP_001535, VSP_001536;
-!- DOMAIN: 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. {ECO:0000269|PubMed:10737772,
ECO:0000269|PubMed:11601975}.
-!- PTM: 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.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers.
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EMBL; U20803; AAB60686.1; -; Genomic_DNA.
EMBL; U20799; AAB60686.1; JOINED; Genomic_DNA.
EMBL; U20800; AAB60686.1; JOINED; Genomic_DNA.
EMBL; U20801; AAB60686.1; JOINED; Genomic_DNA.
EMBL; U20802; AAB60686.1; JOINED; Genomic_DNA.
EMBL; U20803; AAB60685.1; -; Genomic_DNA.
EMBL; U20799; AAB60685.1; JOINED; Genomic_DNA.
EMBL; U20800; AAB60685.1; JOINED; Genomic_DNA.
EMBL; U20801; AAB60685.1; JOINED; Genomic_DNA.
EMBL; U20802; AAB60685.1; JOINED; Genomic_DNA.
EMBL; M34096; AAA99306.1; -; mRNA.
EMBL; M34096; AAA99307.1; -; mRNA.
UniGene; Gga.34280; -.
PDB; 1EI3; X-ray; 5.50 A; A/D=19-505.
PDB; 1M1J; X-ray; 2.70 A; A/D=19-505.
PDBsum; 1EI3; -.
PDBsum; 1M1J; -.
DisProt; DP00233; -.
ProteinModelPortal; P14448; -.
SMR; P14448; -.
STRING; 9031.ENSGALP00000015061; -.
PaxDb; P14448; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; P14448; -.
PhylomeDB; P14448; -.
EvolutionaryTrace; P14448; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005577; C:fibrinogen complex; IMP:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IPI:CAFA.
GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
GO; GO:0030168; P:platelet activation; IEA:InterPro.
GO; GO:0051258; P:protein polymerization; IEA:InterPro.
CDD; cd00087; FReD; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR021996; Fibrinogen_aC.
InterPro; IPR037579; Fibrinogen_alpha.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF232; PTHR19143:SF232; 1.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF12160; Fibrinogen_aC; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SMART; SM01212; Fib_alpha; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Calcium;
Coiled coil; Complete proteome; Direct protein sequencing;
Disulfide bond; Hemostasis; Metal-binding;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:656462}.
PEPTIDE 19 33 Fibrinopeptide A.
/FTId=PRO_0000009046.
CHAIN 34 741 Fibrinogen alpha chain.
/FTId=PRO_0000009047.
DOMAIN 498 739 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 67 506 {ECO:0000269|PubMed:10737772,
ECO:0000269|PubMed:11601975}.
METAL 666 666 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 668 668 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 670 670 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
METAL 672 672 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
SITE 33 34 Cleavage; by thrombin; to release
fibrinopeptide A.
MOD_RES 19 19 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:656462}.
DISULFID 46 46 Interchain (with alpha chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 55 55 Interchain (with beta chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 64 64 Interchain (with gamma chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 68 68 Interchain (with beta chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 180 180 Interchain (with gamma chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 184 184 Interchain (with beta chain).
{ECO:0000269|PubMed:11601975}.
DISULFID 310 341 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 674 687 {ECO:0000250|UniProtKB:P02671}.
VAR_SEQ 506 509 DCDD -> GTQK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_001535.
VAR_SEQ 510 741 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_001536.
TURN 60 62 {ECO:0000244|PDB:1M1J}.
HELIX 70 97 {ECO:0000244|PDB:1M1J}.
TURN 98 100 {ECO:0000244|PDB:1M1J}.
HELIX 101 178 {ECO:0000244|PDB:1M1J}.
TURN 179 183 {ECO:0000244|PDB:1M1J}.
STRAND 184 186 {ECO:0000244|PDB:1M1J}.
TURN 194 197 {ECO:0000244|PDB:1M1J}.
HELIX 198 207 {ECO:0000244|PDB:1M1J}.
TURN 232 235 {ECO:0000244|PDB:1M1J}.
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


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