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

 FIBA_MOUSE              Reviewed;         789 AA.
E9PV24; Q99K47;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
22-NOV-2017, entry version 65.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A {ECO:0000250|UniProtKB:P06399};
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=Fga {ECO:0000312|MGI:MGI:1316726};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|Ensembl:ENSMUSP00000133117};
[1] {ECO:0000312|Ensembl:ENSMUSP00000133117}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000133117};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2] {ECO:0000312|EMBL:AAH05467.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=7649481; DOI=10.1101/gad.9.16.2020;
Suh T.T., Holmback K., Jensen N.J., Daugherty C.C., Small K.,
Simon D.I., Potter S., Degen J.L.;
"Resolution of spontaneous bleeding events but failure of pregnancy in
fibrinogen-deficient mice.";
Genes Dev. 9:2020-2033(1995).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10930441; DOI=10.1172/JCI9896;
Ni H., Denis C.V., Subbarao S., Degen J.L., Sato T.N., Hynes R.O.,
Wagner D.D.;
"Persistence of platelet thrombus formation in arterioles of mice
lacking both von Willebrand factor and fibrinogen.";
J. Clin. Invest. 106:385-392(2000).
[5] {ECO:0000305}
FUNCTION.
PubMed=11389004; DOI=10.1182/blood.V97.12.3691;
Drew A.F., Liu H., Davidson J.M., Daugherty C.C., Degen J.L.;
"Wound-healing defects in mice lacking fibrinogen.";
Blood 97:3691-3698(2001).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12629066; DOI=10.1084/jem.20021493;
Johnson L.L., Berggren K.N., Szaba F.M., Chen W., Smiley S.T.;
"Fibrin-mediated protection against infection-stimulated
immunopathology.";
J. Exp. Med. 197:801-806(2003).
[7] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15972474; DOI=10.1128/IAI.73.7.3888-3895.2005;
Mullarky I.K., Szaba F.M., Berggren K.N., Parent M.A., Kummer L.W.,
Chen W., Johnson L.L., Smiley S.T.;
"Infection-stimulated fibrin deposition controls hemorrhage and limits
hepatic bacterial growth during listeriosis.";
Infect. Immun. 73:3888-3895(2005).
[8] {ECO:0000305}
FUNCTION.
PubMed=19332769; DOI=10.1182/blood-2008-03-145821;
Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J.,
Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.;
"Fibrinogen is required for maintenance of platelet intracellular and
cell-surface P-selectin expression.";
Blood 114:425-436(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-447, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23487423; DOI=10.4049/jimmunol.1203253;
Luo D., Lin J.S., Parent M.A., Mullarky-Kanevsky I., Szaba F.M.,
Kummer L.W., Duso D.K., Tighe M., Hill J., Gruber A., Mackman N.,
Gailani D., Smiley S.T.;
"Fibrin facilitates both innate and T cell-mediated defense against
Yersinia pestis.";
J. Immunol. 190:4149-4161(2013).
-!- 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 (PubMed:7649481). In addition, functions during the
early stages of wound repair to stabilize the lesion and guide
cell migration during re-epithelialization (PubMed:11389004). Was
originally thought to be essential for platelet aggregation, based
on in vitro studies using anticoagulated blood (PubMed:7649481).
However, subsequent studies have shown that it is not absolutely
required for thrombus formation in vivo (PubMed:10930441).
Enhances expression of SELP in activated platelets via an ITGB3-
dependent pathway (PubMed:19332769). Maternal fibrinogen is
essential for successful pregnancy (PubMed:7649481). Fibrin
deposition is also associated with infection, where it protects
against IFNG-mediated hemorrhage (PubMed:12629066). May also
facilitate the immune response via both innate and T-cell mediated
pathways (PubMed:23487423). {ECO:0000250|UniProtKB:P02671,
ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:11389004,
ECO:0000269|PubMed:12629066, ECO:0000269|PubMed:15972474,
ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:23487423,
ECO:0000269|PubMed:7649481}.
-!- 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:0000250|UniProtKB:P02671}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7649481}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=E9PV24-1; Sequence=Displayed;
Name=2;
IsoId=E9PV24-2; Sequence=VSP_057097, VSP_057098;
-!- TISSUE SPECIFICITY: Expressed in liver.
{ECO:0000269|PubMed:7649481}.
-!- 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:0000250|UniProtKB:P02671}.
-!- 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. {ECO:0000250|UniProtKB:P02671}.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers. {ECO:0000250|UniProtKB:P02671}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02671}.
-!- DISRUPTION PHENOTYPE: Knockout mice are viable but only males are
fertile (PubMed:7649481). Neonates frequently develop spontaneous
hemorrhages, but in spite of this over 90% of mice survive the
neonatal period (PubMed:7649481). However only half survive beyond
70 days of age; lethality is most often due to intra-abdominal
hemorrhage (PubMed:7649481). Pregnancy in female mice fails at
around 10 days of gestation, associated with severe intrauterine
bleeding (PubMed:7649481). Secondary loss of FGB and FGG from
circulating blood is observed, although FGB and FGG mRNA is
normally expressed in hepatocytes (thought to be the main site of
fibrinogen synthesis) (PubMed:7649481). In vitro, blood fails to
clot and platelet aggregations do not form (PubMed:7649481). In
vivo, platelet aggregation in injured arterioles initially occurs
normally although thrombi are unstable and readily embolize
(PubMed:10930441). In double knockouts of FGA and VWF, platelet
aggregation is delayed and thrombi frequently embolize
(PubMed:10930441). Mice succumb more rapidly to Y. pestis
infection, associated with increased bacterial loads in liver and
lung; however induction of the inflammatory response factors TNF,
IFNG, CXCL1, and LCN2 is not affected (PubMed:23487423). Mice
succumb more rapidly to T. gondii infection, with increased
hemorrhagic pathology; however parasite numbers are not
significantly increased and induction of the inflammatory response
markers IL12, IFNG, TNF, IL10, and nitric oxide is not affected
(PubMed:12629066). Mice succumb more rapidly to L. monocytogenes
infection, with increased hemorrhagic pathology and increased
bacterial burdens in hepatic tissue; however there is little
effect on peritoneal bacterial numbers or bacterial dissemination
to other tissues, and also no effect on induction of the
inflammatory markers IFNG, TNF and NOS2 (PubMed:15972474).
{ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:12629066,
ECO:0000269|PubMed:15972474, ECO:0000269|PubMed:23487423,
ECO:0000269|PubMed:7649481}.
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EMBL; AC138394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005467; AAH05467.1; -; mRNA.
CCDS; CCDS17431.1; -. [E9PV24-2]
CCDS; CCDS50939.1; -. [E9PV24-1]
RefSeq; NP_001104518.1; NM_001111048.2. [E9PV24-1]
RefSeq; NP_034326.1; NM_010196.4. [E9PV24-2]
UniGene; Mm.88793; -.
ProteinModelPortal; E9PV24; -.
SMR; E9PV24; -.
IntAct; E9PV24; 3.
MINT; MINT-1863401; -.
STRING; 10090.ENSMUSP00000133117; -.
iPTMnet; E9PV24; -.
PhosphoSitePlus; E9PV24; -.
MaxQB; E9PV24; -.
PaxDb; E9PV24; -.
PeptideAtlas; E9PV24; -.
PRIDE; E9PV24; -.
Ensembl; ENSMUST00000029630; ENSMUSP00000029630; ENSMUSG00000028001. [E9PV24-2]
Ensembl; ENSMUST00000166581; ENSMUSP00000133117; ENSMUSG00000028001. [E9PV24-1]
GeneID; 14161; -.
KEGG; mmu:14161; -.
UCSC; uc008ppf.2; mouse. [E9PV24-2]
UCSC; uc012cqw.1; mouse. [E9PV24-1]
CTD; 2243; -.
MGI; MGI:1316726; Fga.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00830000128240; -.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; E9PV24; -.
KO; K03903; -.
OMA; PGSTGTW; -.
OrthoDB; EOG091G03M1; -.
TreeFam; TF351984; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
PRO; PR:E9PV24; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028001; -.
Genevisible; E9PV24; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:1903561; C:extracellular vesicle; ISO:MGI.
GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IMP:MGI.
GO; GO:0072377; P:blood coagulation, common pathway; ISO:MGI.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
GO; GO:0043623; P:cellular protein complex assembly; ISO:MGI.
GO; GO:0042730; P:fibrinolysis; ISO:MGI.
GO; GO:0043152; P:induction of bacterial agglutination; ISO:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0031639; P:plasminogen activation; ISO:MGI.
GO; GO:0070527; P:platelet aggregation; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:MGI.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
GO; GO:0006461; P:protein complex assembly; ISO:MGI.
GO; GO:0051258; P:protein polymerization; ISO:MGI.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR021996; Fibrinogen_aC.
InterPro; IPR020837; Fibrinogen_CS.
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;
Adaptive immunity; Alternative splicing; Blood coagulation; Calcium;
Coiled coil; Complete proteome; Disulfide bond; Glycoprotein;
Hemostasis; Hydroxylation; Immunity; Innate immunity; Metal-binding;
Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000250|UniProtKB:P06399,
ECO:0000255}.
PEPTIDE 20 36 Fibrinopeptide A.
{ECO:0000250|UniProtKB:P06399}.
/FTId=PRO_0000430789.
CHAIN 37 789 Fibrinogen alpha chain.
/FTId=PRO_0000430790.
DOMAIN 546 787 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 69 554 {ECO:0000250|UniProtKB:P14448}.
COMPBIAS 266 348 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
METAL 714 714 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 716 716 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 718 718 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
METAL 720 720 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
SITE 36 37 Cleavage; by thrombin; to release
fibrinopeptide A.
{ECO:0000250|UniProtKB:P06399}.
SITE 101 102 Cleavage; by plasmin; to break down
fibrin clots.
{ECO:0000250|UniProtKB:P02671}.
SITE 122 123 Cleavage; by hementin; to prevent blood
coagulation.
{ECO:0000250|UniProtKB:P02671}.
SITE 124 125 Cleavage; by plasmin; to break down
fibrin clots.
{ECO:0000250|UniProtKB:P02671}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 504 504 4-hydroxyproline; by P4HA1.
{ECO:0000250|UniProtKB:P02671}.
CARBOHYD 609 609 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 48 Interchain.
{ECO:0000250|UniProtKB:P02671}.
DISULFID 56 56 Interchain (with beta chain).
{ECO:0000250|UniProtKB:P02671}.
DISULFID 65 65 Interchain (with gamma chain).
{ECO:0000250|UniProtKB:P02671}.
DISULFID 69 69 Interchain (with beta chain).
{ECO:0000250|UniProtKB:P02671}.
DISULFID 181 181 Interchain (with gamma chain).
{ECO:0000250|UniProtKB:P02671}.
DISULFID 185 185 Interchain (with C-213 in beta chain).
{ECO:0000250|UniProtKB:P02671}.
DISULFID 408 438 {ECO:0000250|UniProtKB:P02671}.
DISULFID 722 735 {ECO:0000250|UniProtKB:P02671}.
VAR_SEQ 554 557 DCDD -> GIDT (in isoform 2).
{ECO:0000305|PubMed:15489334}.
/FTId=VSP_057097.
VAR_SEQ 558 789 Missing (in isoform 2).
{ECO:0000305|PubMed:15489334}.
/FTId=VSP_057098.
SEQUENCE 789 AA; 87429 MW; 16B968D6E4952CF7 CRC64;
MLSLRVTCLI LSVASTVWTT DTEDKGEFLS EGGGVRGPRV VERHQSQCKD SDWPFCSDDD
WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQRNN KDSNSLTRNI MEYLRGDFAN
ANNFDNTYGQ VSEDLRRRIE ILRRKVIEKA QQIQALQSNV RAQLIDMKRL EVDIDIKIRS
CKGSCSRAVN REINLQDYEG HQKQLQQVIA KELLPTKDRQ YLPALKMSPV PDLVPGSFKS
QLQEAPPEWK ALTEMRQMRM ELERPGKDGG SRGDSPGDSR GDSRGDFATR GPGSKAENPT
NPGPGGSGYW RPGNSGSGSD GNRNPGTTGS DGTGDWGTGS PRPGSDSGNF RPANPNWGVF
SEFGDSSSPA TRKEYHTGKA VTSKGDKELL IGKEKVTSSG TSTTHRSCSK TITKTVTGPD
GRREVVKEVI TSDDGSDCGD ATELDISHSF SGSLDELSER HPDLSGFFDN HFGLISPNFK
EFGSKTHSDS DILTNIEDPS SHVPEFSSSS KTSTVKKQVT KTYKMADEAG SEAHREGETR
NTKRGRARAR PTRDCDDVLQ TQTSGAQNGI FSIKPPGSSK VFSVYCDQET SLGGWLLIQQ
RMDGSLNFNR TWQDYKRGFG SLNDKGEGEF WLGNDYLHLL TLRGSVLRVE LEDWAGKEAY
AEYHFRVGSE AEGYALQVSS YRGTAGDALV QGSVEEGTEY TSHSNMQFST FDRDADQWEE
NCAEVYGGGW WYNSCQAANL NGIYYPGGTY DPRNNSPYEI ENGVVWVPFR GADYSLRAVR
MKIRPLVGQ


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