Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 FIBA_RAT                Reviewed;         782 AA.
P06399;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 3.
22-NOV-2017, entry version 142.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=Fga;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8595905; DOI=10.1006/geno.1995.0010;
Fu Y., Cao Y., Hertzberg K.M., Grieninger G.;
"Fibrinogen alpha genes: conservation of bipartite transcripts and
carboxy-terminal-extended alpha subunits in vertebrates.";
Genomics 30:71-76(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=4046033; DOI=10.1016/0022-2836(85)90179-2;
Crabtree G.R., Comeau C.M., Fowlkes D.M., Fornace A.J. Jr.,
Malley J.D., Kant J.A.;
"Evolution and structure of the fibrinogen genes. Random insertion of
introns or selective loss?";
J. Mol. Biol. 185:1-19(1985).
[3]
PROTEIN SEQUENCE OF 20-36.
Blombaeck B., Blombaeck M., Grondahl N.J.;
"Studies on fibrinopeptides from mammals.";
Acta Chem. Scand. 19:1789-1791(1965).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 458-550 (ISOFORM 2).
STRAIN=Wistar; TISSUE=Liver;
PubMed=3817019; DOI=10.1016/0014-4827(87)90223-0;
Sobczak J., Lotti A.-M., Taroux P., Duguet M.;
"Molecular cloning of mRNA sequences transiently induced during rat
liver regeneration.";
Exp. Cell Res. 169:47-56(1987).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-326; SER-470
AND SER-526, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By similarity). {ECO:0000250|UniProtKB:P02671}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha-E;
IsoId=P06399-1; Sequence=Displayed;
Name=2; Synonyms=Alpha;
IsoId=P06399-2; Sequence=VSP_001533, VSP_001534;
Note=Major isoform.;
-!- 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.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02671}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X86561; CAA60264.1; -; Genomic_DNA.
EMBL; X86561; CAA60263.1; -; Genomic_DNA.
EMBL; M35601; AAA41158.1; -; mRNA.
PIR; I53408; I53408.
UniGene; Rn.98846; -.
ProteinModelPortal; P06399; -.
SMR; P06399; -.
STRING; 10116.ENSRNOP00000060007; -.
iPTMnet; P06399; -.
PhosphoSitePlus; P06399; -.
PaxDb; P06399; -.
PeptideAtlas; P06399; -.
PRIDE; P06399; -.
UCSC; RGD:2603; rat. [P06399-1]
RGD; 2603; Fga.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; P06399; -.
PhylomeDB; P06399; -.
PMAP-CutDB; P06399; -.
PRO; PR:P06399; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0072562; C:blood microparticle; IDA:RGD.
GO; GO:0005938; C:cell cortex; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:1903561; C:extracellular vesicle; ISO:RGD.
GO; GO:0005577; C:fibrinogen complex; ISO:RGD.
GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
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:InterPro.
GO; GO:0005198; F:structural molecule activity; ISO:RGD.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; ISO:RGD.
GO; GO:0072377; P:blood coagulation, common pathway; ISO:RGD.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:RGD.
GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
GO; GO:0043623; P:cellular protein complex assembly; ISO:RGD.
GO; GO:1990643; P:cellular response to granulocyte colony-stimulating factor; IEP:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0044468; P:envenomation resulting in modulation of blood coagulation in other organism; IEP:RGD.
GO; GO:0042730; P:fibrinolysis; ISO:RGD.
GO; GO:0043152; P:induction of bacterial agglutination; ISO:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
GO; GO:0031639; P:plasminogen activation; ISO:RGD.
GO; GO:0070527; P:platelet aggregation; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:RGD.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:RGD.
GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:RGD.
GO; GO:0006461; P:protein complex assembly; ISO:RGD.
GO; GO:0051258; P:protein polymerization; ISO:RGD.
GO; GO:0051592; P:response to calcium ion; ISO:RGD.
GO; GO:0046898; P:response to cycloheximide; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0060416; P:response to growth hormone; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IEP:RGD.
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; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis; Hydroxylation; Immunity;
Innate immunity; Metal-binding; Phosphoprotein; Reference proteome;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|Ref.3}.
PEPTIDE 20 36 Fibrinopeptide A.
/FTId=PRO_0000009039.
CHAIN 37 782 Fibrinogen alpha chain.
/FTId=PRO_0000009038.
DOMAIN 539 780 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 68 547 {ECO:0000250|UniProtKB:P02671}.
METAL 707 707 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 709 709 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 711 711 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
METAL 713 713 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
SITE 36 37 Cleavage; by thrombin; to release
fibrinopeptide A.
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 279 279 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 499 499 4-hydroxyproline; by P4HA1.
{ECO:0000250|UniProtKB:P02671}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 48 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00739}.
DISULFID 56 56 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 65 65 Interchain (with C-49 in gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 69 69 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 181 181 Interchain (with C-165 in gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 185 185 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 404 434 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 715 728 {ECO:0000250|UniProtKB:P02671}.
VAR_SEQ 547 550 DCDD -> GIHA (in isoform 2).
{ECO:0000303|PubMed:3817019}.
/FTId=VSP_001533.
VAR_SEQ 551 782 Missing (in isoform 2).
{ECO:0000303|PubMed:3817019}.
/FTId=VSP_001534.
CONFLICT 30 34 EAGGD -> DEGAG (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 140 140 Q -> E (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 212 212 D -> E (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 270 276 ASRGDLP -> LREEIYQ (in Ref. 2).
{ECO:0000305}.
CONFLICT 473 473 S -> K (in Ref. 4; AAA41158).
{ECO:0000305}.
SEQUENCE 782 AA; 86686 MW; 744834DAE76D34C2 CRC64;
MLSLRVACLI LSLASTVWTA DTGTTSEFIE AGGDIRGPRI VERQPSQCKE TDWPFCSDED
WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQKNN KDSNSLTRNI MEYLRGDFAN
ANNFDNTFGQ VSEDLRRRIQ ILKRKVIEKA QQIQVLQKDV RDQLIDMKRL EVDIDIKIRS
CKGSCSRSVS REINLKDYEG QQKQLEQVIA KDLLPAKDRQ YLPAIKMSPV PDLVPGSFKS
QLQEGPPEWK ALTEMRQMRM ELERPGKDGA SRGDLPGDSR GDSATRGPGS KIENPMTPGH
GGSGYWRPGS SGSGSDGNWG SGTTGSDDTG TWGAGSSRPS SGSGNLKPSN PDWGEFSEFG
GSSSPATRKE YHTGKLVTSK GDKELLIGNE KVTSTGTSTT RRSCSKTITK TVLGNDGHRE
VVKEVVTSDD GSDCGDGMDL GLTHSFSGRL DELSRMHPEL GSFYDSRFGS LTSNFKEFGS
KTSDSDIFTD IENPSSHVPE FSSSSKTSTV RKQVTKSYKM ADEAASEAHQ EGDTRTTKRG
RARTMRDCDD VLQTHPSGAQ NGIFSIKLPG SSKIFSVYCD QETSLGGWLL IQQRMDGSLN
FNRTWQDYKR GFGSLNDKGE GEFWLGNDYL HLLTLRGSVL RVELEDWAGK EAYAEYHFRV
GSEAEGYALQ VSSYQGTAGD ALMEGSVEEG TEYTSHSNMQ FSTFDRDADQ WEENCAEVYG
GGWWYNSCQA ANLNGIYYPG GTYDPRNNSP YEIENGVLWV PFRGADYSLW AVRMKIRPLV
GQ


Related products :

Catalog number Product name Quantity
29-638 FGA is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form f 0.1 mg
25-722 FGA is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form f 0.05 mg
ARP41759_P050 FGA(fibrinogen alpha chain) 50 µg
ARP41758_T100 Fibrinogen alpha chain 0.1 mg
ARP41759_P050 Fibrinogen alpha chain 50 µg
GTX19079 Fibrinogen alpha chain 100 µg
AP17364PU-N Fibrinogen alpha chain (N_term) 0.1 mg
CSB-EL008607DO Dog fibrinogen alpha chain (FGA) ELISA kit 96T
ER212 Fibrinogen alpha chain Elisa Kit 96T
NB100-73042 Fibrinogen alpha chain 0.2 mg
CSB-EL008607CA Cat fibrinogen alpha chain (FGA) ELISA kit 96T
AJ1294a Fibrinogen alpha Antibody chain 100ul
CSB-E17440r Rat fibrinogen alpha chain (Fga) ELISA kit 96T
18-003-43712 Fibrinogen alpha chain - N_A Polyclonal 0.1 mg Protein A
FGD1 FGA Gene fibrinogen alpha chain
AJ1294a Fibrinogen alpha Antibody chain
EH697 Fibrinogen alpha chain Elisa Kit 96T
GWB-B1ABBA Fibrinogen alpha chain, Antibody
E1381709 Fibrinogen alpha Chain (FGA) ELISA Kit 1
EM1020 Fibrinogen Alpha chain Elisa Kit 96T
CSB-EL008607BO Bovine fibrinogen alpha chain (FGA) ELISA kit 96T
AP17364CP-N Fibrinogen alpha chain Control Peptide 0.1 mg
CSB-E17440r Rat fibrinogen alpha chain (Fga) ELISA kit SpeciesRat 96T
E1237p ELISA FGA,Fibrinogen alpha chain,Pig,Sus scrofa 96T
CSB-EL008607HU Human Fibrinogen alpha chain (FGA) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur