FIBA1_PETMA
ID FIBA1_PETMA Reviewed; 966 AA.
AC P02674;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Fibrinogen alpha-1 chain;
DE Contains:
DE RecName: Full=Fibrinopeptide A;
DE Contains:
DE RecName: Full=Fibrinogen alpha-1 chain;
DE Flags: Precursor; Fragment;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2611265; DOI=10.1021/bi00451a039;
RA Wang Y.Z., Patterson J., Gray J.E., Yu C., Cottrell B.A., Shimizu A.,
RA Graham D., Riley M., Doolittle R.F.;
RT "Complete sequence of the lamprey fibrinogen alpha chain.";
RL Biochemistry 28:9801-9806(1989).
RN [2]
RP PROTEIN SEQUENCE OF 6-11.
RX PubMed=999898; DOI=10.1016/0005-2795(76)90138-0;
RA Cottrell B.A., Doolittle R.F.;
RT "Amino acid sequences of lamprey fibrinopeptides A and B and
RT characterizations of the junctions split by lamprey and mammalian
RT thrombins.";
RL Biochim. Biophys. Acta 453:426-438(1976).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 87-205, SUBUNIT, COILED COIL
RP DOMAIN, AND DISULFIDE BONDS.
RX PubMed=12162736; DOI=10.1021/bi020299t;
RA Yang Z., Spraggon G., Pandi L., Everse S.J., Riley M., Doolittle R.F.;
RT "Crystal structure of fragment D from lamprey fibrinogen complexed with the
RT peptide Gly-His-Arg-Pro-amide.";
RL Biochemistry 41:10218-10224(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 87-205, SUBUNIT, SUBCELLULAR
RP LOCATION, AND COILED COIL DOMAIN.
RX PubMed=12501189; DOI=10.1021/bi026666i;
RA Yang Z., Pandi L., Doolittle R.F.;
RT "The crystal structure of fragment double-D from cross-linked lamprey
RT fibrin reveals isopeptide linkages across an unexpected D-D interface.";
RL Biochemistry 41:15610-15617(2002).
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 {ECO:0000269|PubMed:12162736, ECO:0000269|PubMed:12501189}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12501189}.
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:0000269|PubMed:12162736, ECO:0000269|PubMed:12501189}.
CC -!- PTM: Not glycosylated.
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; M30123; AAA49263.1; -; mRNA.
DR PIR; A33626; A33626.
DR PDB; 1LWU; X-ray; 2.80 A; A/D/G/J=87-205.
DR PDB; 1N73; X-ray; 2.90 A; A/D=87-205.
DR PDBsum; 1LWU; -.
DR PDBsum; 1N73; -.
DR AlphaFoldDB; P02674; -.
DR SMR; P02674; -.
DR STRING; 7757.ENSPMAP00000008504; -.
DR PRIDE; P02674; -.
DR EvolutionaryTrace; P02674; -.
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 InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR037579; Fibrinogen_alpha.
DR PANTHER; PTHR19143:SF232; PTHR19143:SF232; 1.
DR Pfam; PF08702; Fib_alpha; 1.
DR SMART; SM01212; Fib_alpha; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Hemostasis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL <1..5
FT /evidence="ECO:0000269|PubMed:999898"
FT PEPTIDE 6..11
FT /note="Fibrinopeptide A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000009049"
FT CHAIN 12..966
FT /note="Fibrinogen alpha-1 chain"
FT /id="PRO_0000009050"
FT REPEAT 391..408
FT /note="1"
FT REPEAT 409..426
FT /note="2"
FT REPEAT 427..444
FT /note="3"
FT REPEAT 445..462
FT /note="4"
FT REPEAT 463..480
FT /note="5"
FT REPEAT 481..498
FT /note="6"
FT REPEAT 499..516
FT /note="7"
FT REPEAT 517..534
FT /note="8"
FT REPEAT 535..552
FT /note="9"
FT REPEAT 553..570
FT /note="10"
FT REPEAT 571..588
FT /note="11"
FT REPEAT 589..606
FT /note="12"
FT REPEAT 607..624
FT /note="13"
FT REPEAT 625..642
FT /note="14"
FT REPEAT 643..660
FT /note="15"
FT REPEAT 661..678
FT /note="16"
FT REPEAT 679..696
FT /note="17"
FT REPEAT 697..714
FT /note="18"
FT REPEAT 715..732
FT /note="19"
FT REPEAT 733..750
FT /note="20"
FT REPEAT 751..768
FT /note="21"
FT REPEAT 769..786
FT /note="22; approximate"
FT REGION 208..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..786
FT /note="22 X 18 AA approximate tandem repeats of [FN]-T-G-S-
FT [AG]-[QK]-G-G-S-W-[SG]-T-G-G-[RS]-T-[AE]-[TP]"
FT REGION 831..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..205
FT /evidence="ECO:0000269|PubMed:12162736"
FT COMPBIAS 208..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 11..12
FT /note="Cleavage; by thrombin; to release fibrinopeptide A"
FT /evidence="ECO:0000250"
FT DISULFID 26
FT /note="Interchain (with alpha chain)"
FT DISULFID 34
FT /note="Interchain (with beta chain)"
FT DISULFID 43
FT /note="Interchain (with gamma chain)"
FT DISULFID 47
FT /note="Interchain (with beta chain)"
FT DISULFID 159
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000269|PubMed:12162736"
FT DISULFID 163
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000269|PubMed:12162736"
FT NON_TER 1
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1LWU"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 114..158
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1LWU"
SQ SEQUENCE 966 AA; 97314 MW; 410520898AA799EE CRC64;
QVCIADDISL RGPRLTEQRS AGQGSCASAT ADLCVHGDWG RKCPNGCRMQ GLMSHAEKDI
GKRIGDLTER LARLGRLYTQ VHTDFRAVSD TSGQTLNEHN ELEVRYSEVL RELERRIIHL
QRRINMQLQQ LTLLQHNIKT QVSQILRVEV DIDVALRTCK GSCARYLEYR LDKEKNLQLE
KAASYIANLK FERFEEVVVE ETLNRRVETS SHAFQPTHGQ GTPQPGHGTH SLSATSSITS
APNFVPHRQP TYVDHGRLSN PNEVAHSASS SSTHTSSSSS PSQPVSRDSA FPLPGSNTGT
SEWDFNFHDE STPGNGPRDE AAASSSAHSP STASHDTATS TTSFSSGTSG KDVAPLGTGV
THDGGVRTSG SLMDGGSSDT GTGGVSKTTT FTGSAQGGSW STGGSTATNT GSAQGGSWST
GGRTEPNTGS GQGGSWGTGG RTEPNTGSGQ GGSWGTGGRT EPNTGSGQGG SWGTGGRTEP
NTGSAQGGSW GTGGRTEPNT GSAQGGSWGT GGRTEPNTGS AQGGSWSTGG RTEPNTGSAK
GGSWGTGGRT EPNTGSAKGG SWSTGGRTEP NTGSAKGGSW GTGGRTEPNT GSAQGGSWGT
GGRTEPNTGS AQGGSWGTGG RTEPNTGSAQ GGSWGTGGRT EPNTGSAQGG SWGTGGRTEP
NTGSAQGGSW STGGRTEPNT GSGQGGSWGT GGRTEPNTGS GQGGSWSTGG RTEPNTGSGQ
GGSWGTGGRT EPNTGSAQGG SWGTGGRTEP NTGSAQGGSW GTGGSTATNT GSAQGGGGYA
AGGTGAQTGS GSTSTHSAHS ASGGMSSLDM LPALPDFGTW DMPDHSDIFS RRRVSTSSTT
SSSSGGGHAG AAAGGGGDGA SRFGSLFTTD FGPEFHEEFR SMLPGASRLS SSSSSSTRST
SSTSGGKVVT ESVVTKVLSN GTTITHHTKH VSTSDGTGAA SDGVSPLLTG RKTKAARSRR
AKATRP
