FIBB_PETMA
ID FIBB_PETMA Reviewed; 477 AA.
AC P02678;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 23-FEB-2022, entry version 108.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Fragments;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP PROTEIN SEQUENCE OF 1-36, AND SULFATION AT TYR-13.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-477.
RX PubMed=3790537; DOI=10.1021/bi00369a026;
RA Bohonus V.L., Doolittle R.F., Pontes M., Strong D.D.;
RT "Complementary DNA sequence of lamprey fibrinogen beta chain.";
RL Biochemistry 25:6512-6516(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 155-477, SUBUNIT, AND COILED COIL
RP DOMAIN.
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 155-477, SUBCELLULAR LOCATION,
RP SUBUNIT, 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: 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.
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DR EMBL; M14773; AAA49261.1; -; mRNA.
DR PIR; A25052; A25052.
DR PDB; 1LWU; X-ray; 2.80 A; B/E/H/K=155-477.
DR PDB; 1N73; X-ray; 2.90 A; B/E=155-477.
DR PDBsum; 1LWU; -.
DR PDBsum; 1N73; -.
DR SMR; P02678; -.
DR STRING; 7757.ENSPMAP00000007060; -.
DR iPTMnet; P02678; -.
DR EvolutionaryTrace; P02678; -.
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; IPR037580; Fibrinogen_beta.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF332; PTHR19143:SF332; 1.
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 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis; Reference proteome; Secreted;
KW Sulfation.
FT PEPTIDE 1..36
FT /note="Fibrinopeptide B"
FT /evidence="ECO:0000269|PubMed:999898"
FT /id="PRO_0000009096"
FT CHAIN <37..477
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009097"
FT DOMAIN 221..476
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:999898"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:999898"
FT DISULFID 84
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 95
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 99
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 212
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 216
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 220..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 230..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 412..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT NON_CONS 36..37
FT /evidence="ECO:0000305"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1LWU"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 190..210
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1N73"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1LWU"
FT TURN 412..417
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1N73"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:1LWU"
SQ SEQUENCE 477 AA; 54270 MW; B8A95E7E32D09D18 CRC64;
EDLSLVGQPE NDYDTGDDBT AADPDSNNTA AALDVRRPLP SGTRVRRPPL RHRRLAPGAV
MSRDPPASPR PQEAQKAIRD EGGCMLPESD LGVLCPTGCE LREELLKQRD PVRYKISMLK
QNLTYFINSF DRMASDSNTL KQNVQTLRRR LNSRSSTHVN AQKEIENRYK EVKIRIESTV
AGSLRSMKSV LEHLRAKMQR MEEAIKTQKE LCSAPCTVNC RVPVVSGMHC EDIYRNGGRT
SEAYYIQPDL FSEPYKVFCD MESHGGGWTV VQNRVDGSSN FARDWNTYKA EFGNIAFGNG
KSICNIPGEY WLGTKTVHQL TKQHTQQVLF DMSDWEGSSV YAQYASFRPE NEAQGYRLWV
EDYSGNAGNA LLEGATQLMG DNRTMTIHNG MQFSTFDRDN DNWNPGDPTK HCSREDAGGW
WYNRCHAANP NGRYYWGGIY TKEQADYGTD DGVVWMNWKG SWYSMRQMAM KLRPKWP
