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

 FIBA_BOVIN              Reviewed;         615 AA.
P02672; O97642; Q3T049;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 5.
10-MAY-2017, entry version 127.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=FGA;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-577.
Murakawa M.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 412-615.
Chung D.W., Rixon M.W., Davie E.W.;
"The biosynthesis of fibrinogen and the cloning of its cDNA.";
(In) Bradshaw R.A. (eds.);
Proteins in biology and medicine, pp.309-328, Academic Press, New York
(1982).
[4]
PROTEIN SEQUENCE OF 20-38.
Sjoquist J., Blombaeck B., Wallen P.;
"Amino acid sequence of bovine fibrinopeptides.";
Ark. Kemi 16:425-436(1960).
[5]
PROTEIN SEQUENCE OF 20-38.
PubMed=13823737;
Folk J.E., Gladner J.A., Levin Y.;
"Thrombin-induced formation of co-fibrin. III. Acid degradation
studies and summary of sequential evidence on peptide A.";
J. Biol. Chem. 234:2317-2320(1959).
[6]
PROTEIN SEQUENCE OF 39-73.
PubMed=836881;
Timpl R., Fietzek P.P., Wachter E., van Delden V.;
"Disulfide-linked cyanogen bromide peptides of bovine fibrinogen. II.
Isolation and sequence analysis of the chain constituents from the
amino terminal region.";
Biochim. Biophys. Acta 490:420-429(1977).
[7]
PROTEIN SEQUENCE OF 39-68; 262-287 AND 572-599.
Henschen A., Lottspeich F., Topfer-Petersen E., Kehl M., Timpl R.;
(In) Peeters H. (eds.);
Protides of the biological fluids, Proc. 28th colloquium, pp.47-50,
Pergamon Press, Oxford (1980).
[8]
PROTEIN SEQUENCE OF 42-71.
PubMed=434821; DOI=10.1016/0003-9861(79)90068-7;
Martinelli R.A., Inglis A.S., Rubira M.R., Hageman T.C.,
Hurrell J.G.R., Leach S.J., Scheraga H.A.;
"Amino acid sequences of portions of the alpha and beta chains of
bovine fibrinogen.";
Arch. Biochem. Biophys. 192:27-32(1979).
[9]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 20-409, SUBUNIT, AND COILED
COIL DOMAIN.
PubMed=10618375; DOI=10.1073/pnas.97.1.85;
Brown J.H., Volkmann N., Jun G., Henschen-Edman A.H., Cohen C.;
"The crystal structure of modified bovine fibrinogen.";
Proc. Natl. Acad. Sci. U.S.A. 97:85-90(2000).
[10] {ECO:0000244|PDB:2JOR}
STRUCTURE BY NMR OF 438-515, AND DISULFIDE BONDS.
PubMed=17590019; DOI=10.1021/bi700606v;
Burton R.A., Tsurupa G., Hantgan R.R., Tjandra N., Medved L.;
"NMR solution structure, stability, and interaction of the recombinant
bovine fibrinogen alphaC-domain fragment.";
Biochemistry 46:8550-8560(2007).
-!- 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. In addition, functions during the early stages of
wound repair to stabilize the lesion and guide cell migration
during re-epithelialization. Was originally thought to be
essential for platelet aggregation, based on in vitro studies
using anticoagulated blood. However, subsequent studies have shown
that it is not absolutely required for thrombus formation in vivo.
Enhances expression of SELP in activated platelets via an ITGB3-
dependent pathway. Maternal fibrinogen is essential for successful
pregnancy. Fibrin deposition is also associated with infection,
where it protects against IFNG-mediated hemorrhage. May also
facilitate the immune response via both innate and T-cell mediated
pathways. {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:10618375}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- 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:10618375}.
-!- 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; BC102564; AAI02565.1; -; mRNA.
EMBL; AF095463; AAC67562.1; -; Genomic_DNA.
PIR; A05294; A05294.
PIR; S69114; S69114.
RefSeq; NP_001028798.1; NM_001033626.1.
UniGene; Bt.17997; -.
PDB; 1DEQ; X-ray; 3.50 A; A/D/N/Q=20-409.
PDB; 1JY2; X-ray; 1.40 A; N/Q=48-100.
PDB; 1JY3; X-ray; 1.60 A; N/Q=48-100.
PDB; 2BAF; NMR; -; A=406-570.
PDB; 2JOR; NMR; -; A=438-515.
PDBsum; 1DEQ; -.
PDBsum; 1JY2; -.
PDBsum; 1JY3; -.
PDBsum; 2BAF; -.
PDBsum; 2JOR; -.
ProteinModelPortal; P02672; -.
SMR; P02672; -.
STRING; 9913.ENSBTAP00000002145; -.
Allergome; 1112; Bos d Fibrin.
PaxDb; P02672; -.
PeptideAtlas; P02672; -.
PRIDE; P02672; -.
GeneID; 522039; -.
KEGG; bta:522039; -.
CTD; 2243; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; P02672; -.
KO; K03903; -.
EvolutionaryTrace; P02672; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
GO; GO:0030674; F:protein binding, bridging; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030168; P:platelet activation; IEA:InterPro.
GO; GO:0051258; P:protein polymerization; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR021996; Fibrinogen_aC.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF12160; Fibrinogen_aC; 1.
SMART; SM01212; Fib_alpha; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Blood coagulation; Coiled coil;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hemostasis; Immunity; Innate immunity;
Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:13823737,
ECO:0000269|Ref.4}.
PEPTIDE 20 38 Fibrinopeptide A.
{ECO:0000269|PubMed:836881,
ECO:0000269|Ref.7}.
/FTId=PRO_0000009005.
CHAIN 39 615 Fibrinogen alpha chain.
/FTId=PRO_0000009006.
COILED 71 602 {ECO:0000305|PubMed:10618375}.
COMPBIAS 448 451 Poly-Thr.
COMPBIAS 537 542 Poly-Ser.
SITE 38 39 Cleavage; by thrombin; to release
fibrinopeptide A.
CARBOHYD 325 325 O-linked (GalNAc...) threonine.
{ECO:0000250}.
DISULFID 50 50 Interchain.
{ECO:0000250|UniProtKB:P02671}.
DISULFID 58 58 Interchain (with C-72 in beta chain).
{ECO:0000250|UniProtKB:P14448}.
DISULFID 67 67 Interchain (with C-47 in gamma chain).
{ECO:0000250|UniProtKB:P14448}.
DISULFID 71 71 Interchain (with C-83 in beta chain).
{ECO:0000250|UniProtKB:P14448}.
DISULFID 183 183 Interchain (with C-163 in gamma chain).
{ECO:0000250|UniProtKB:P14448}.
DISULFID 187 187 Interchain (with C-200 in beta chain).
{ECO:0000250|UniProtKB:P14448}.
DISULFID 455 485 {ECO:0000244|PDB:2BAF,
ECO:0000244|PDB:2JOR,
ECO:0000269|PubMed:17590019}.
CONFLICT 189 189 R -> K (in Ref. 2; AAC67562).
{ECO:0000305}.
CONFLICT 238 239 RE -> KK (in Ref. 2; AAC67562).
{ECO:0000305}.
CONFLICT 360 372 Missing (in Ref. 2; AAC67562).
{ECO:0000305}.
CONFLICT 375 375 A -> G (in Ref. 2; AAC67562).
{ECO:0000305}.
CONFLICT 457 458 KV -> S (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 612 612 S -> T (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
HELIX 60 62 {ECO:0000244|PDB:1JY2}.
STRAND 66 68 {ECO:0000244|PDB:1JY2}.
HELIX 70 95 {ECO:0000244|PDB:1JY2}.
STRAND 417 419 {ECO:0000244|PDB:2BAF}.
STRAND 421 423 {ECO:0000244|PDB:2BAF}.
STRAND 443 445 {ECO:0000244|PDB:2BAF}.
STRAND 450 453 {ECO:0000244|PDB:2BAF}.
TURN 454 456 {ECO:0000244|PDB:2BAF}.
STRAND 457 459 {ECO:0000244|PDB:2BAF}.
TURN 466 468 {ECO:0000244|PDB:2JOR}.
STRAND 475 477 {ECO:0000244|PDB:2BAF}.
STRAND 480 482 {ECO:0000244|PDB:2JOR}.
STRAND 483 486 {ECO:0000244|PDB:2BAF}.
STRAND 497 500 {ECO:0000244|PDB:2JOR}.
STRAND 505 507 {ECO:0000244|PDB:2BAF}.
TURN 537 539 {ECO:0000244|PDB:2BAF}.
TURN 555 558 {ECO:0000244|PDB:2BAF}.
SEQUENCE 615 AA; 67012 MW; A79B48E292DF627B CRC64;
MFSVRDLCLV LSLVGAIKTE DGSDPPSGDF LTEGGGVRGP RLVERQQSAC KETGWPFCSD
EDWNTKCPSG CRMKGLIDEV DQDFTSRINK LRDSLFNYQK NSKDSNTLTK NIVELMRGDF
AKANNNDNTF KQISEDLRSR IEILRRKVIE QVQRIKVLQK NVRDQLVDMK RLEVDIDIKI
RSCKGSCSRA LEHKVDLEDY KNQQKQLEQV IAINLLPSRD IQYLPLIKMS TITGPVPREF
KSQLQEAPLE WKALLEMQQT KMVLETFGGD GHARGDSVSQ GTGLAPGSPR KPGTSSIGNV
NPGSYGPGSS GTWNPGRPEP GSAGTWNPGR PEPGSAGTWN PGRPEPGSAG TWNPGRPEPG
SAGTWNPGRP EPGSAGTWNT GSSGSSSFRP DSSGHGNIRP SSPDWGTFRE EGSVSSGTKQ
EFHTGKLVTT KGDKELLIDN EKVTSGHTTT TRRSCSKVIT KTVTNADGRT ETTKEVVKSE
DGSDCGDADF DWHHTFPSRG NLDDFFHRDK DDFFTRSSHE FDGRTGLAPE FAALGESGSS
SSKTSTHSKQ FVSSSTTVNR GGSAIESKHF KMEDEAESLE DLGFKGAHGT QKGHTKARPA
RGIHTSPLGE PSLTP


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