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

 FIBB_CHICK              Reviewed;         463 AA.
Q02020;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 126.
RecName: Full=Fibrinogen beta chain;
Contains:
RecName: Full=Fibrinopeptide B;
Contains:
RecName: Full=Fibrinogen beta chain;
Flags: Precursor; Fragment;
Name=FGB;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-13 AND 18-39.
PubMed=2009266; DOI=10.1021/bi00227a017;
Weissbach L., Oddoux C., Procyk R., Grieninger G.;
"The beta chain of chicken fibrinogen contains an atypical thrombin
cleavage site.";
Biochemistry 30:3290-3294(1991).
[2]
X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION,
AND COILED COIL DOMAIN.
PubMed=10737772; DOI=10.1073/pnas.080065697;
Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.;
"Crystal structure of native chicken fibrinogen at 5.5-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000).
[3] {ECO:0000244|PDB:1M1J}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH CALCIUM,
DISULFIDE BONDS, SUBCELLULAR LOCATION, SUBUNIT, COILED COIL DOMAIN,
AND GLYCOSYLATION AT ASN-367.
PubMed=11601975; DOI=10.1021/bi011394p;
Yang Z., Kollman J.M., Pandi L., Doolittle R.F.;
"Crystal structure of native chicken fibrinogen at 2.7 A resolution.";
Biochemistry 40:12515-12523(2001).
-!- FUNCTION: Cleaved by the protease thrombin to yield monomers
which, together with fibrinogen alpha (FGA) and fibrinogen gamma
(FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a
major function in hemostasis as one of the primary components of
blood clots. {ECO:0000250|UniProtKB:E9PV24}.
-!- 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:10737772,
ECO:0000269|PubMed:11601975}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772,
ECO:0000269|PubMed:11601975}.
-!- 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:10737772,
ECO:0000269|PubMed:11601975}.
-!- 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; M58514; AAA48770.1; -; mRNA.
PIR; A38463; A38463.
RefSeq; NP_001161155.1; NM_001167683.1.
UniGene; Gga.41812; -.
PDB; 1EI3; X-ray; 5.50 A; B/E=1-463.
PDB; 1M1J; X-ray; 2.70 A; B/E=1-463.
PDBsum; 1EI3; -.
PDBsum; 1M1J; -.
ProteinModelPortal; Q02020; -.
SMR; Q02020; -.
STRING; 9031.ENSGALP00000038105; -.
iPTMnet; Q02020; -.
PaxDb; Q02020; -.
PRIDE; Q02020; -.
GeneID; 373926; -.
KEGG; gga:373926; -.
CTD; 2244; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOGENOM; HOG000059561; -.
HOVERGEN; HBG005707; -.
InParanoid; Q02020; -.
KO; K03904; -.
PhylomeDB; Q02020; -.
EvolutionaryTrace; Q02020; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000009262; Expressed in 8 organ(s), highest expression level in liver.
GO; GO:0005577; C:fibrinogen complex; IDA:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IPI:CAFA.
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.
InterPro; IPR036056; Fibrinogen-like_C.
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; Calcium; Coiled coil;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hemostasis; Metal-binding; Reference proteome; Secreted;
Sulfation.
PEPTIDE <1 17 Fibrinopeptide B.
{ECO:0000269|PubMed:2009266}.
/FTId=PRO_0000009093.
CHAIN 18 463 Fibrinogen beta chain.
/FTId=PRO_0000009094.
DOMAIN 206 461 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
METAL 384 384 Calcium. {ECO:0000244|PDB:1M1J,
ECO:0000269|PubMed:11601975}.
METAL 386 386 Calcium. {ECO:0000244|PDB:1M1J,
ECO:0000269|PubMed:11601975}.
METAL 388 388 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1M1J,
ECO:0000269|PubMed:11601975}.
SITE 17 18 Cleavage; by thrombin; to release
fibrinopeptide B.
MOD_RES 5 5 Sulfotyrosine. {ECO:0000250}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:11601975}.
DISULFID 69 69 Interchain (with alpha chain).
{ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
DISULFID 80 80 Interchain (with alpha chain).
{ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
DISULFID 84 84 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 197 197 Interchain (with alpha chain).
{ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
DISULFID 201 201 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 205 289 {ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
DISULFID 215 244 {ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
DISULFID 397 410 {ECO:0000244|PDB:1M1J,
ECO:0000255|PROSITE-ProRule:PRU00739,
ECO:0000269|PubMed:11601975}.
NON_TER 1 1
TURN 74 76 {ECO:0000244|PDB:1M1J}.
STRAND 78 81 {ECO:0000244|PDB:1M1J}.
HELIX 85 162 {ECO:0000244|PDB:1M1J}.
HELIX 164 196 {ECO:0000244|PDB:1M1J}.
STRAND 207 209 {ECO:0000244|PDB:1M1J}.
STRAND 212 214 {ECO:0000244|PDB:1M1J}.
HELIX 215 220 {ECO:0000244|PDB:1M1J}.
STRAND 227 231 {ECO:0000244|PDB:1M1J}.
STRAND 240 245 {ECO:0000244|PDB:1M1J}.
HELIX 248 250 {ECO:0000244|PDB:1M1J}.
STRAND 253 261 {ECO:0000244|PDB:1M1J}.
HELIX 270 275 {ECO:0000244|PDB:1M1J}.
STRAND 284 288 {ECO:0000244|PDB:1M1J}.
STRAND 294 296 {ECO:0000244|PDB:1M1J}.
HELIX 299 306 {ECO:0000244|PDB:1M1J}.
STRAND 311 318 {ECO:0000244|PDB:1M1J}.
STRAND 320 322 {ECO:0000244|PDB:1M1J}.
STRAND 324 334 {ECO:0000244|PDB:1M1J}.
HELIX 337 339 {ECO:0000244|PDB:1M1J}.
STRAND 343 352 {ECO:0000244|PDB:1M1J}.
HELIX 355 358 {ECO:0000244|PDB:1M1J}.
HELIX 366 369 {ECO:0000244|PDB:1M1J}.
HELIX 397 400 {ECO:0000244|PDB:1M1J}.
STRAND 408 410 {ECO:0000244|PDB:1M1J}.
STRAND 412 414 {ECO:0000244|PDB:1M1J}.
HELIX 427 429 {ECO:0000244|PDB:1M1J}.
STRAND 437 440 {ECO:0000244|PDB:1M1J}.
HELIX 441 444 {ECO:0000244|PDB:1M1J}.
STRAND 446 448 {ECO:0000244|PDB:1M1J}.
STRAND 451 459 {ECO:0000244|PDB:1M1J}.
SEQUENCE 463 AA; 52678 MW; 2044CD49BA79EC7B CRC64;
ASVEYDNEED SPQIDARAHR PLDKRQEAAP TLRPVAPPIS GTGYQPRPPK QDKQAMKKGP
IIYPDAGGCK HPLDELGVLC PTGCELQTTL LKQEKTVKPV LRDLKDRVAK FSDTSTTMYQ
YVNMIDNKLV KTQKQRKDND IILSEYNTEM ELHYNYIKDN LDNNIPSSLR VLRAVIDSLH
KKIQKLENAI ATQTDYCRSP CVASCNIPVV SGRECEDIYR KGGETSEMYI IQPDPFTTPY
RVYCDMETDN GGWTLIQNRQ DGSVNFGRAW DEYKRGFGNI AKSGGKKYCD TPGEYWLGND
KISQLTKIGP TKVLIEMEDW NGDKVSALYG GFTIHNEGNK YQLSVSNYKG NAGNALMEGA
SQLYGENRTM TIHNGMYFST YDRDNDGWLT TDPRKQCSKE DGGGWWYNRC HAANPNGRYY
WGGTYSWDMA KHGTDDGIVW MNWKGSWYSM KKMSMKIKPY FPD


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