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Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain] (Fragments)

 FIBB_PETMA              Reviewed;         477 AA.
P02678;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
23-MAY-2018, entry version 99.
RecName: Full=Fibrinogen beta chain;
Contains:
RecName: Full=Fibrinopeptide B;
Contains:
RecName: Full=Fibrinogen beta chain;
Flags: Fragments;
Petromyzon marinus (Sea lamprey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
NCBI_TaxID=7757;
[1]
PROTEIN SEQUENCE OF 1-36, AND SULFATION AT TYR-13.
PubMed=999898; DOI=10.1016/0005-2795(76)90138-0;
Cottrell B.A., Doolittle R.F.;
"Amino acid sequences of lamprey fibrinopeptides A and B and
characterizations of the junctions split by lamprey and mammalian
thrombins.";
Biochim. Biophys. Acta 453:426-438(1976).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-477.
PubMed=3790537; DOI=10.1021/bi00369a026;
Bohonus V.L., Doolittle R.F., Pontes M., Strong D.D.;
"Complementary DNA sequence of lamprey fibrinogen beta chain.";
Biochemistry 25:6512-6516(1986).
[3]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 155-477, SUBUNIT, AND COILED
COIL DOMAIN.
PubMed=12162736; DOI=10.1021/bi020299t;
Yang Z., Spraggon G., Pandi L., Everse S.J., Riley M., Doolittle R.F.;
"Crystal structure of fragment D from lamprey fibrinogen complexed
with the peptide Gly-His-Arg-Pro-amide.";
Biochemistry 41:10218-10224(2002).
[4]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 155-477, SUBCELLULAR
LOCATION, SUBUNIT, AND COILED COIL DOMAIN.
PubMed=12501189; DOI=10.1021/bi026666i;
Yang Z., Pandi L., Doolittle R.F.;
"The crystal structure of fragment double-D from cross-linked lamprey
fibrin reveals isopeptide linkages across an unexpected D-D
interface.";
Biochemistry 41:15610-15617(2002).
-!- 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. {ECO:0000269|PubMed:12162736,
ECO:0000269|PubMed:12501189}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12501189}.
-!- 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:0000269|PubMed:12162736,
ECO:0000269|PubMed:12501189}.
-!- 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.
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EMBL; M14773; AAA49261.1; -; mRNA.
PIR; A25052; A25052.
PDB; 1LWU; X-ray; 2.80 A; B/E/H/K=155-477.
PDB; 1N73; X-ray; 2.90 A; B/E=155-477.
PDBsum; 1LWU; -.
PDBsum; 1N73; -.
ProteinModelPortal; P02678; -.
SMR; P02678; -.
iPTMnet; P02678; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOVERGEN; HBG005707; -.
EvolutionaryTrace; P02678; -.
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; IPR037580; Fibrinogen_beta.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF332; PTHR19143:SF332; 1.
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.
1: Evidence at protein level;
3D-structure; Blood coagulation; Coiled coil;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
Secreted; Sulfation.
PEPTIDE 1 36 Fibrinopeptide B.
{ECO:0000269|PubMed:999898}.
/FTId=PRO_0000009096.
CHAIN <37 477 Fibrinogen beta chain.
/FTId=PRO_0000009097.
DOMAIN 221 476 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
MOD_RES 13 13 Sulfotyrosine.
{ECO:0000269|PubMed:999898}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:999898}.
DISULFID 84 84 Interchain (with alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 95 95 Interchain (with alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 99 99 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 212 212 Interchain (with alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 216 216 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 220 304 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 230 259 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 412 425 {ECO:0000255|PROSITE-ProRule:PRU00739}.
NON_CONS 36 37 {ECO:0000305}.
HELIX 162 168 {ECO:0000244|PDB:1LWU}.
HELIX 170 177 {ECO:0000244|PDB:1LWU}.
TURN 178 180 {ECO:0000244|PDB:1LWU}.
HELIX 181 188 {ECO:0000244|PDB:1LWU}.
HELIX 190 210 {ECO:0000244|PDB:1LWU}.
STRAND 213 215 {ECO:0000244|PDB:1LWU}.
STRAND 222 224 {ECO:0000244|PDB:1LWU}.
STRAND 227 229 {ECO:0000244|PDB:1LWU}.
HELIX 230 235 {ECO:0000244|PDB:1LWU}.
STRAND 242 246 {ECO:0000244|PDB:1LWU}.
STRAND 255 260 {ECO:0000244|PDB:1LWU}.
HELIX 263 265 {ECO:0000244|PDB:1LWU}.
STRAND 268 277 {ECO:0000244|PDB:1LWU}.
HELIX 285 290 {ECO:0000244|PDB:1LWU}.
STRAND 291 293 {ECO:0000244|PDB:1LWU}.
STRAND 295 297 {ECO:0000244|PDB:1LWU}.
STRAND 300 302 {ECO:0000244|PDB:1LWU}.
STRAND 310 312 {ECO:0000244|PDB:1LWU}.
HELIX 314 323 {ECO:0000244|PDB:1LWU}.
STRAND 326 333 {ECO:0000244|PDB:1LWU}.
STRAND 335 337 {ECO:0000244|PDB:1N73}.
STRAND 339 347 {ECO:0000244|PDB:1LWU}.
HELIX 352 354 {ECO:0000244|PDB:1LWU}.
STRAND 365 367 {ECO:0000244|PDB:1LWU}.
HELIX 370 373 {ECO:0000244|PDB:1LWU}.
HELIX 381 384 {ECO:0000244|PDB:1LWU}.
STRAND 401 403 {ECO:0000244|PDB:1LWU}.
TURN 412 417 {ECO:0000244|PDB:1LWU}.
STRAND 423 425 {ECO:0000244|PDB:1LWU}.
STRAND 427 429 {ECO:0000244|PDB:1LWU}.
STRAND 436 439 {ECO:0000244|PDB:1N73}.
TURN 442 444 {ECO:0000244|PDB:1LWU}.
STRAND 452 455 {ECO:0000244|PDB:1LWU}.
HELIX 456 459 {ECO:0000244|PDB:1LWU}.
STRAND 466 473 {ECO:0000244|PDB:1LWU}.
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


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