ID   FIBA2_PETMA             Reviewed;         641 AA.
AC   P33573;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Fibrinogen alpha-2 chain;
DE   Contains:
DE     RecName: Full=Fibrinopeptide A;
DE   Contains:
DE     RecName: Full=Fibrinogen alpha-2 chain;
DE   Flags: Precursor;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1549566; DOI=10.1073/pnas.89.6.2066;
RA   Pan Y., Doolittle R.F.;
RT   "cDNA sequence of a second fibrinogen alpha chain in lamprey: an archetypal
RT   version alignable with full-length beta and gamma chains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2066-2070(1992).
CC   -!- FUNCTION: Fibrinogen has a double function: yielding monomers that
CC       polymerize into fibrin and acting as a cofactor in platelet
CC       aggregation.
CC   -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC       identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC       head to head conformation with the N-termini in a small central domain
CC       (By similarity). {ECO:0000250|UniProtKB:P02674}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02674}.
CC   -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC       connects the central nodule to the C-terminal domains (distal nodules).
CC       The long C-terminal ends of the alpha chains fold back, contributing a
CC       fourth strand to the coiled coil structure.
CC       {ECO:0000250|UniProtKB:P02674}.
CC   -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC       cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC       exposes the N-terminal polymerization sites responsible for the
CC       formation of the soft clot. The soft clot is converted into the hard
CC       clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC       cross-linking between gamma chains (stronger) and between alpha chains
CC       (weaker) of different monomers.
CC   -!- PTM: Forms F13A-mediated cross-links between a glutamine and the
CC       epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen
CC       heteropolymers.
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DR   EMBL; M84565; AAA73183.1; -; mRNA.
DR   EMBL; M84482; AAA49264.1; -; mRNA.
DR   PIR; A41932; A41932.
DR   AlphaFoldDB; P33573; -.
DR   SMR; P33573; -.
DR   STRING; 7757.ENSPMAP00000003059; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 1.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR   InterPro; IPR037579; Fibrinogen_alpha.
DR   InterPro; IPR020837; Fibrinogen_CS.
DR   PANTHER; PTHR19143:SF232; PTHR19143:SF232; 2.
DR   Pfam; PF08702; Fib_alpha; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM01212; Fib_alpha; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Coiled coil; Disulfide bond; Glycoprotein; Hemostasis;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..31
FT                   /note="Fibrinopeptide A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000009051"
FT   CHAIN           32..641
FT                   /note="Fibrinogen alpha-2 chain"
FT                   /id="PRO_0000009052"
FT   DOMAIN          395..636
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          228..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          107..226
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        247..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            31..32
FT                   /note="Cleavage; by thrombin; to release fibrinopeptide A"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45
FT                   /note="Interchain (with alpha chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        54
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        63
FT                   /note="Interchain (with gamma chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        67
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        179
FT                   /note="Interchain (with gamma chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        183
FT                   /note="Interchain (with beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        404..435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        571..584
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   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