Reviewed, UniProtKB/Swiss-Prot P02676 (FIBB_BOVIN)

Names and origin

Protein names

Recommended name:
    Fibrinogen beta chain
Cleaved into the following chain:
    1- Recommended name:
            Fibrinopeptide B

Gene names

Name:

FGB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Subunit structure	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 By similarity.
Subcellular location	Secreted.
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.
Post-translational modification	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.
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	Coiled coil
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid Sulfation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	platelet activation Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	fibrinogen complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding, bridging Inferred from electronic annotation. Source: InterPro receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Peptide

1 – 21

21

Fibrinopeptide B

PRO_0000009055

Chain

22 – 468

447

Fibrinogen beta chain

PRO_0000009056

Regions

Domain

209 – 465

257

Fibrinogen C-terminal

Coiled coil

88 – 204

117

Sites

Site

21 – 22

2

Cleavage; by thrombin; to release fibrinopeptide B

Amino acid modifications

Modified residue

1

1

Pyrrolidone carboxylic acid

Modified residue

6

1

Sulfotyrosine

Glycosylation

371

1

N-linked (GlcNAc...) Probable

Disulfide bond

72

Interchain (with C-58 in alpha chain)

Disulfide bond

83

Interchain (with C-71 in alpha chain)

Disulfide bond

87

Interchain (with C-43 in gamma chain)

Disulfide bond

200

Interchain (with C-187 in alpha chain)

Disulfide bond

204

Interchain (with C-159 in gamma chain)

Disulfide bond

208 ↔ 293

By similarity

Disulfide bond

218 ↔ 247

By similarity

Disulfide bond

401 ↔ 414

By similarity

Secondary structure

1

.

.

.

.

.

.

.

468

Helix Strand Turn

Details...

Turn

77 – 79

3

Beta strand

81 – 84

4

Helix

86 – 112

27

Sequences

	Sequence		Length	Mass (Da)
	P02676-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 2DED42F443AA4B37	FASTA	468	53,340
	10 20 30 40 50 60 QFPTDYDEGQ DDRPKVGLGA RGHRPYDKKK EEAPSLRPVP PPISGGGYRA RPATATVGQK 70 80 90 100 110 120 KVERKPPDAD GCLHADPDLG VLCPTGCKLQ DTLVRQERPI RKSIEDLRNT VDSVSRTSSS 130 140 150 160 170 180 TFQYITLLKN MWKGRQNQVQ DNENVVNEYS SHLEKHQLYI DETVKNNIPT KLRVLRSILE 190 200 210 220 230 240 NLRSKIQKLE SDVSTQMEYC RTPCTVTCNI PVVSGKECEK IIRNEGETSE MYLIQPEDSS 250 260 270 280 290 300 KPYRVYCDMK TEKGGWTVIQ NRQDGSVDFG RKWDPYKQGF GNIATNAEGK KYCGVPGEYW 310 320 330 340 350 360 LGNDRISQLT NMGPTKLLIE MEDWKGDKVT ALYEGFTVQN EANKYQLSVS KYKGTAGNAL 370 380 390 400 410 420 IEGASQLVGE NRTMTIHNSM FFSTYDRDND GWKTTDPRKQ CSKEDGGGWW YNRCHAANPN 430 440 450 460 GRYYWGGAYT WDMAKHGTDD GVVWMNWQGS WYSMKKMSMK IRPYFPEQ

References

[1]	"The sequence of amino acids at the N-terminal end of bovine fibrinopeptide B." Blombaeck B., Doolittle R.F. Acta Chem. Scand. 17:1816-1819(1963) Cited for: PROTEIN SEQUENCE OF 1-4.
[2]	"Amino acid sequence of bovine fibrinopeptides." Sjoquist J., Blombaeck B., Wallen P. Ark. Kemi 16:425-436(1960) Cited for: PROTEIN SEQUENCE OF 5-21.
[3]	"Amino acid sequences of portions of the alpha and beta chains of bovine fibrinogen." Martinelli R.A., Inglis A.S., Rubira M.R., Hageman T.C., Hurrell J.G.R., Leach S.J., Scheraga H.A. Arch. Biochem. Biophys. 192:27-32(1979) [PubMed: 434821] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-53.
[4]	"Characterization of a cDNA clone coding for the beta chain of bovine fibrinogen." Chung D.W., Rixon M.W., McGillivray R.T.A., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 78:1466-1470(1981) [PubMed: 6262803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-468.
[5]	"Fibrinogen structure in projection at 18 A resolution. Electron density by co-ordinated cryo-electron microscopy and X-ray crystallography." Rao S.P., Poojary M.D., Elliott B.W. Jr., Melanson L.A., Oriel B., Cohen C. J. Mol. Biol. 222:89-98(1991) [PubMed: 1942070] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 61-468.
[6]	"Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution." Madrazo J., Brown J.H., Litvinovich S., Dominguez R., Yakovlev S., Medved L., Cohen C. Proc. Natl. Acad. Sci. U.S.A. 98:11967-11972(2001) [PubMed: 11593005] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 61-116.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V00110 mRNA. Translation: CAA23444.1.

IPI

IPI00709763.

PIR

FGBOB. A03122.
S69115.

UniGene

Bt.23917

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DEQ	X-ray	3.50	B/E/O/R	61-468	[»]
1JY2	X-ray	1.40	O/R	61-116	[»]
1JY3	X-ray	1.60	O/R	61-116	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000022120. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P02676.

Family and domain databases

InterPro

IPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR012290. Fibrinogen_a/b/g_coil.
IPR018986. Fibrinogen_bsu_coiled-coil_N.
[Graphical view]

Gene3D

G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit.
G3DSA:1.20.5.50. Fibrinogen_a/b/g_coil. 1 hit.

Pfam

PF09389. Fib_beta. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]

SMART

SM00186. FBG. 1 hit.
[Graphical view]

PROSITE

PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FIBB_BOVIN

Accession

Primary (citable) accession number: P02676

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)