Reviewed, UniProtKB/Swiss-Prot P02678 (FIBB_PETMA)

Names and origin

Protein names	Recommended name:     Fibrinogen beta chain Cleaved into the following chain:     1- Recommended name:             Fibrinopeptide B
Organism	Petromyzon marinus (Sea lamprey)
Taxonomic identifier	7757 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Hyperoartia › Petromyzontiformes › Petromyzontidae › Petromyzon

Protein attributes

Sequence length	477 AA.
Sequence status	Fragments.
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 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 – 36

36

Fibrinopeptide B Ref.1

PRO_0000009096

Chain

‹37 – 477

›441

Fibrinogen beta chain

PRO_0000009097

Regions

Domain

221 – 476

256

Fibrinogen C-terminal

Amino acid modifications

Modified residue

13

1

Sulfotyrosine Ref.1

Glycosylation

27

1

N-linked (GlcNAc...) Ref.1

Disulfide bond

84

Interchain (with alpha chain) By similarity

Disulfide bond

95

Interchain (with alpha chain) By similarity

Disulfide bond

99

Interchain (with gamma chain) By similarity

Disulfide bond

212

Interchain (with alpha chain) By similarity

Disulfide bond

216

Interchain (with gamma chain) By similarity

Disulfide bond

220 ↔ 304

By similarity

Disulfide bond

230 ↔ 259

By similarity

Disulfide bond

412 ↔ 425

By similarity

Experimental info

Non-adjacent residues

36 – 37

2

Secondary structure

1

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477

Helix Strand Turn

Details...

Helix

162 – 168

7

Helix

170 – 177

8

Turn

178 – 180

3

Helix

181 – 188

8

Helix

190 – 210

21

Beta strand

213 – 215

3

Beta strand

222 – 224

3

Beta strand

227 – 229

3

Helix

230 – 235

6

Beta strand

242 – 246

5

Beta strand

255 – 260

6

Helix

263 – 265

3

Beta strand

268 – 277

10

Helix

285 – 290

6

Beta strand

291 – 293

3

Beta strand

295 – 297

3

Beta strand

300 – 302

3

Beta strand

310 – 312

3

Helix

314 – 323

10

Beta strand

326 – 333

8

Beta strand

339 – 347

9

Helix

352 – 354

3

Beta strand

365 – 367

3

Helix

370 – 373

4

Helix

381 – 384

4

Beta strand

401 – 403

3

Turn

412 – 417

6

Beta strand

423 – 425

3

Beta strand

427 – 429

3

Turn

442 – 444

3

Beta strand

452 – 455

4

Helix

456 – 459

4

Beta strand

466 – 473

8

Sequences

	Sequence		Length	Mass (Da)
	P02678-1 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: B8A95E7E32D09D18	FASTA	477	54,270
	10 20 30 40 50 60 EDLSLVGQPE NDYDTGDDBT AADPDSNNTA AALDVRRPLP SGTRVRRPPL RHRRLAPGAV 70 80 90 100 110 120 MSRDPPASPR PQEAQKAIRD EGGCMLPESD LGVLCPTGCE LREELLKQRD PVRYKISMLK 130 140 150 160 170 180 QNLTYFINSF DRMASDSNTL KQNVQTLRRR LNSRSSTHVN AQKEIENRYK EVKIRIESTV 190 200 210 220 230 240 AGSLRSMKSV LEHLRAKMQR MEEAIKTQKE LCSAPCTVNC RVPVVSGMHC EDIYRNGGRT 250 260 270 280 290 300 SEAYYIQPDL FSEPYKVFCD MESHGGGWTV VQNRVDGSSN FARDWNTYKA EFGNIAFGNG 310 320 330 340 350 360 KSICNIPGEY WLGTKTVHQL TKQHTQQVLF DMSDWEGSSV YAQYASFRPE NEAQGYRLWV 370 380 390 400 410 420 EDYSGNAGNA LLEGATQLMG DNRTMTIHNG MQFSTFDRDN DNWNPGDPTK HCSREDAGGW 430 440 450 460 470 WYNRCHAANP NGRYYWGGIY TKEQADYGTD DGVVWMNWKG SWYSMRQMAM KLRPKWP

References

[1]	"Amino acid sequences of lamprey fibrinopeptides A and B and characterizations of the junctions split by lamprey and mammalian thrombins." Cottrell B.A., Doolittle R.F. Biochim. Biophys. Acta 453:426-438(1976) [PubMed: 999898] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-36.
[2]	"Complementary DNA sequence of lamprey fibrinogen beta chain." Bohonus V.L., Doolittle R.F., Pontes M., Strong D.D. Biochemistry 25:6512-6516(1986) [PubMed: 3790537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-477.
[3]	"Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide." Yang Z., Spraggon G., Pandi L., Everse S.J., Riley M., Doolittle R.F. Biochemistry 41:10218-10224(2002) [PubMed: 12162736] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 155-477.
[4]	"The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface." Yang Z., Pandi L., Doolittle R.F. Biochemistry 41:15610-15617(2002) [PubMed: 12501189] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 155-477.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14773 mRNA. Translation: AAA49261.1.

PIR

A25052.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LWU	X-ray	2.80	B/E/H/K	155-477	[»]
1N73	X-ray	2.90	B/E	155-477	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P02678.

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. 2 hits.
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_PETMA

Accession

Primary (citable) accession number: P02678

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)