FIBB_BOVIN
ID FIBB_BOVIN Reviewed; 468 AA.
AC P02676;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Precursor;
GN Name=FGB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 1-4, AND PYROGLUTAMATE FORMATION AT GLN-1.
RA Blombaeck B., Doolittle R.F.;
RT "The sequence of amino acids at the N-terminal end of bovine fibrinopeptide
RT B.";
RL Acta Chem. Scand. 17:1816-1819(1963).
RN [2]
RP PROTEIN SEQUENCE OF 5-21, AND SULFATION AT TYR-6.
RA Sjoquist J., Blombaeck B., Wallen P.;
RT "Amino acid sequence of bovine fibrinopeptides.";
RL Ark. Kemi 16:425-436(1960).
RN [3]
RP PROTEIN SEQUENCE OF 22-53.
RX PubMed=434821; DOI=10.1016/0003-9861(79)90068-7;
RA Martinelli R.A., Inglis A.S., Rubira M.R., Hageman T.C., Hurrell J.G.R.,
RA Leach S.J., Scheraga H.A.;
RT "Amino acid sequences of portions of the alpha and beta chains of bovine
RT fibrinogen.";
RL Arch. Biochem. Biophys. 192:27-32(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-468.
RX PubMed=6262803; DOI=10.1073/pnas.78.3.1466;
RA Chung D.W., Rixon M.W., McGillivray R.T.A., Davie E.W.;
RT "Characterization of a cDNA clone coding for the beta chain of bovine
RT fibrinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:1466-1470(1981).
RN [5]
RP GLYCOSYLATION AT THR-4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 61-468, COILED COIL DOMAIN, AND
RP SUBUNIT.
RX PubMed=1942070; DOI=10.1016/0022-2836(91)90739-s;
RA Rao S.P., Poojary M.D., Elliott B.W. Jr., Melanson L.A., Oriel B.,
RA Cohen C.;
RT "Fibrinogen structure in projection at 18 A resolution. Electron density by
RT co-ordinated cryo-electron microscopy and X-ray crystallography.";
RL J. Mol. Biol. 222:89-98(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 61-116, SUBUNIT, DISULFIDE BONDS,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11593005; DOI=10.1073/pnas.211439798;
RA Madrazo J., Brown J.H., Litvinovich S., Dominguez R., Yakovlev S.,
RA Medved L., Cohen C.;
RT "Crystal structure of the central region of bovine fibrinogen (E5 fragment)
RT at 1.4-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11967-11972(2001).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC In addition, functions during the early stages of wound repair to
CC stabilize the lesion and guide cell migration during re-
CC epithelialization. Was originally thought to be essential for platelet
CC aggregation, based on in vitro studies using anticoagulated blood.
CC However subsequent studies have shown that it is not absolutely
CC required for thrombus formation in vivo. Enhances expression of SELP in
CC activated platelets. Maternal fibrinogen is essential for successful
CC pregnancy. Fibrin deposition is also associated with infection, where
CC it protects against IFNG-mediated hemorrhage. May also facilitate the
CC antibacterial immune response via both innate and T-cell mediated
CC pathways. {ECO:0000250|UniProtKB:E9PV24}.
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:11593005, ECO:0000269|PubMed:1942070}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11593005}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC {ECO:0000269|PubMed:11593005}.
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:1942070}.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00110; CAA23444.1; -; mRNA.
DR PIR; A03122; FGBOB.
DR PIR; S69115; S69115.
DR PDB; 1DEQ; X-ray; 3.50 A; B/E/O/R=61-468.
DR PDB; 1JY2; X-ray; 1.40 A; O/R=61-116.
DR PDB; 1JY3; X-ray; 1.60 A; O/R=61-116.
DR PDB; 2Z4E; X-ray; 2.70 A; I/J=22-26.
DR PDB; 3H32; X-ray; 3.60 A; M/N=22-26.
DR PDBsum; 1DEQ; -.
DR PDBsum; 1JY2; -.
DR PDBsum; 1JY3; -.
DR PDBsum; 2Z4E; -.
DR PDBsum; 3H32; -.
DR AlphaFoldDB; P02676; -.
DR SMR; P02676; -.
DR STRING; 9913.ENSBTAP00000029826; -.
DR GlyConnect; 735; 1 O-Linked glycan (1 site).
DR iPTMnet; P02676; -.
DR PaxDb; P02676; -.
DR PeptideAtlas; P02676; -.
DR PRIDE; P02676; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; P02676; -.
DR EvolutionaryTrace; P02676; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
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; Adaptive immunity; Blood coagulation; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Immunity; Innate immunity; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Sulfation.
FT PEPTIDE 1..21
FT /note="Fibrinopeptide B"
FT /evidence="ECO:0000269|PubMed:434821"
FT /id="PRO_0000009055"
FT CHAIN 22..468
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009056"
FT DOMAIN 209..465
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..204
FT /evidence="ECO:0000305|PubMed:1942070"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 21..22
FT /note="Cleavage; by thrombin; to release fibrinopeptide B"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 6
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 4
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 72
FT /note="Interchain (with C-58 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:11593005"
FT DISULFID 83
FT /note="Interchain (with C-71 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:11593005"
FT DISULFID 87
FT /note="Interchain (with C-43 in gamma chain)"
FT DISULFID 200
FT /note="Interchain (with C-187 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:P02675"
FT DISULFID 204
FT /note="Interchain (with C-159 in gamma chain)"
FT /evidence="ECO:0000250|UniProtKB:P02675"
FT DISULFID 208..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 218..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 401..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1JY2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1JY2"
FT HELIX 86..112
FT /evidence="ECO:0007829|PDB:1JY2"
SQ SEQUENCE 468 AA; 53340 MW; 2DED42F443AA4B37 CRC64;
QFPTDYDEGQ DDRPKVGLGA RGHRPYDKKK EEAPSLRPVP PPISGGGYRA RPATATVGQK
KVERKPPDAD GCLHADPDLG VLCPTGCKLQ DTLVRQERPI RKSIEDLRNT VDSVSRTSSS
TFQYITLLKN MWKGRQNQVQ DNENVVNEYS SHLEKHQLYI DETVKNNIPT KLRVLRSILE
NLRSKIQKLE SDVSTQMEYC RTPCTVTCNI PVVSGKECEK IIRNEGETSE MYLIQPEDSS
KPYRVYCDMK TEKGGWTVIQ NRQDGSVDFG RKWDPYKQGF GNIATNAEGK KYCGVPGEYW
LGNDRISQLT NMGPTKLLIE MEDWKGDKVT ALYEGFTVQN EANKYQLSVS KYKGTAGNAL
IEGASQLVGE NRTMTIHNSM FFSTYDRDND GWKTTDPRKQ CSKEDGGGWW YNRCHAANPN
GRYYWGGAYT WDMAKHGTDD GVVWMNWQGS WYSMKKMSMK IRPYFPEQ
