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Fibrinogen alpha-2 chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha-2 chain]

 FIBA2_PETMA             Reviewed;         641 AA.
P33573;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 85.
RecName: Full=Fibrinogen alpha-2 chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha-2 chain;
Flags: Precursor;
Petromyzon marinus (Sea lamprey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
NCBI_TaxID=7757;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1549566; DOI=10.1073/pnas.89.6.2066;
Pan Y., Doolittle R.F.;
"cDNA sequence of a second fibrinogen alpha chain in lamprey: an
archetypal version alignable with full-length beta and gamma chains.";
Proc. Natl. Acad. Sci. U.S.A. 89:2066-2070(1992).
-!- FUNCTION: Fibrinogen has a double function: yielding monomers that
polymerize into fibrin and acting as a cofactor in platelet
aggregation.
-!- 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:P02674}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02674}.
-!- 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:P02674}.
-!- 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; M84565; AAA73183.1; -; mRNA.
EMBL; M84482; AAA49264.1; -; mRNA.
PIR; A41932; A41932.
ProteinModelPortal; P33573; -.
SMR; P33573; -.
PRIDE; P33573; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
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.
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; IPR037579; Fibrinogen_alpha.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF232; PTHR19143:SF232; 2.
Pfam; PF08702; Fib_alpha; 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.
2: Evidence at transcript level;
Blood coagulation; Coiled coil; Disulfide bond; Glycoprotein;
Hemostasis; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
PEPTIDE 24 31 Fibrinopeptide A. {ECO:0000250}.
/FTId=PRO_0000009051.
CHAIN 32 641 Fibrinogen alpha-2 chain.
/FTId=PRO_0000009052.
DOMAIN 395 636 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 107 226 {ECO:0000250}.
COMPBIAS 293 316 Ser-rich.
SITE 31 32 Cleavage; by thrombin; to release
fibrinopeptide A.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 45 45 Interchain (with alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 54 54 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 63 63 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 67 67 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 179 179 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 183 183 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 404 435 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 571 584 {ECO:0000255|PROSITE-ProRule:PRU00739}.
SEQUENCE 641 AA; 70757 MW; CA991A8DD698BFB5 CRC64;
MTLRGVSMVL TWCLLVSKAW SSGDDSSIDI RGPRLVMPSQ ARDSCSTQQT TELCVEGNWG
RKCPGGCRML SMLSRTEKDS MRRVDELTKR LARMIQLHTE IHSYYRSVSD VSNQVVTDRE
DTEARFYALL SDLERKIIYL QRRINGQLTL LSQLRNGIAQ QTSTILQLEV DTDVALRTCK
GACARQVRYR VDKEMNLQLE KANAYLSGIN LALFEEIVHE SFSVERDDAR SLHPYSGGPA
SDSEPRDGDG TASQATGFRS DATDPGVSHG NSSKSFGNVD ERSKVEKDVN VASTSSVSSS
SSSSSSSSST SSTISSTQKT EELSFKKVSV STAAVAGKDT DDFQWDSVQT ASQTEEGFVR
DTGADSTWNQ HNVQWNSDFG TASDDEPDFQ ARSHRTNLSE YIDCLDVLQR RPGGKASGLY
EVRPRGAKRA LTVHCEQDTD GGGWTLVQQR EDGSLNFNRS FSAYREGFGT VDGSGHGELW
LGLEAMYLLA HEDSTMRVEL QGWDGAGAHA EYTVTLRDDS KGYALQVSDY RGTAGNALVS
GVADDPELTS HGGMTFSTYD RDTDKWSDGS CAEWYGGGWW INACQAANLN GVYYQGGPYD
PREKPPYEVE NGVVWATYRG SDYSLKRTAV RFRRVQIPIV E


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