FIBG_BOVIN
ID FIBG_BOVIN Reviewed; 444 AA.
AC P12799;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Fibrinogen gamma-B chain;
DE Short=Gamma';
DE Flags: Precursor;
GN Name=FGG;
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 NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2771651; DOI=10.1093/nar/17.15.6397;
RA Brown W.M., Dziegielewska K.M., Foreman R.C., Saunders N.R.;
RT "Nucleotide and deduced amino acid sequence of a gamma subunit of bovine
RT fibrinogen.";
RL Nucleic Acids Res. 17:6397-6397(1989).
RN [2]
RP PROTEIN SEQUENCE OF 25-63.
RX PubMed=836881; DOI=10.1016/0005-2795(77)90017-4;
RA Timpl R., Fietzek P.P., Wachter E., van Delden V.;
RT "Disulfide-linked cyanogen bromide peptides of bovine fibrinogen. II.
RT Isolation and sequence analysis of the chain constituents from the amino
RT terminal region.";
RL Biochim. Biophys. Acta 490:420-429(1977).
RN [3]
RP PROTEIN SEQUENCE OF 409-436.
RX PubMed=11946783; DOI=10.1016/0014-5793(72)80517-9;
RA Sharp J.J., Cassman K.G., Doolittle R.F.;
RT "Amino acid sequence of the carboxy-terminal cyanogen bromide fragment from
RT bovine and human fibrinogen gamma-chains.";
RL FEBS Lett. 25:334-336(1972).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-436, SUBUNIT, AND COILED COIL
RP DOMAIN.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), SUBUNIT, AND COILED COIL DOMAIN.
RX PubMed=10618375; DOI=10.1073/pnas.97.1.85;
RA Brown J.H., Volkmann N., Jun G., Henschen-Edman A.H., Cohen C.;
RT "The crystal structure of modified bovine fibrinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:85-90(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-72, 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: Together with fibrinogen alpha (FGA) and fibrinogen beta
CC (FGB), polymerizes to form an insoluble fibrin matrix. 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 via an ITGB3-dependent pathway. Maternal fibrinogen
CC is essential for successful pregnancy. Fibrin deposition is also
CC associated with infection, where it protects against IFNG-mediated
CC hemorrhage. May also facilitate the antibacterial immune response via
CC both innate and T-cell mediated pathways.
CC {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:10618375, ECO:0000269|PubMed:11593005,
CC ECO:0000269|PubMed:1942070}.
CC -!- SUBCELLULAR LOCATION: Secreted {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:10618375, 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.
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DR EMBL; X15556; CAA33562.1; -; mRNA.
DR PIR; A05295; A05295.
DR PIR; S05313; S05313.
DR PIR; S69116; S69116.
DR RefSeq; NP_776336.1; NM_173911.2.
DR PDB; 1DEQ; X-ray; 3.50 A; C/F/P/S=25-432.
DR PDB; 1JY2; X-ray; 1.40 A; P/S=25-72.
DR PDB; 1JY3; X-ray; 1.60 A; P/S=25-72.
DR PDBsum; 1DEQ; -.
DR PDBsum; 1JY2; -.
DR PDBsum; 1JY3; -.
DR AlphaFoldDB; P12799; -.
DR SMR; P12799; -.
DR STRING; 9913.ENSBTAP00000008877; -.
DR PaxDb; P12799; -.
DR PeptideAtlas; P12799; -.
DR PRIDE; P12799; -.
DR GeneID; 280792; -.
DR KEGG; bta:280792; -.
DR CTD; 2266; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; P12799; -.
DR OrthoDB; 523014at2759; -.
DR EvolutionaryTrace; P12799; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
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; IPR020837; Fibrinogen_CS.
DR InterPro; IPR037581; Fibrinogen_gamma.
DR PANTHER; PTHR19143:SF338; PTHR19143:SF338; 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; Blood coagulation; Calcium; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:836881"
FT CHAIN 25..444
FT /note="Fibrinogen gamma-B chain"
FT /id="PRO_0000009098"
FT DOMAIN 168..415
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 25..165
FT /evidence="ECO:0000305|PubMed:1942070"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 32
FT /note="Interchain (with C-33)"
FT /evidence="ECO:0000269|PubMed:11593005,
FT ECO:0007744|PDB:1JY2"
FT DISULFID 33
FT /note="Interchain (with C-32)"
FT /evidence="ECO:0000269|PubMed:11593005,
FT ECO:0007744|PDB:1JY2"
FT DISULFID 43
FT /note="Interchain (with C-87 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:P02679"
FT DISULFID 47
FT /note="Interchain (with C-67 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:P02679"
FT DISULFID 159
FT /note="Interchain (with C-204 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:P02679"
FT DISULFID 163
FT /note="Interchain (with C-183 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:P02679"
FT DISULFID 177..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 351..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 433..436
FT /note="VGVE -> AGDV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1JY3"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1JY2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1JY2"
FT HELIX 46..71
FT /evidence="ECO:0007829|PDB:1JY2"
SQ SEQUENCE 444 AA; 50244 MW; 4573C994DE715C49 CRC64;
MSWSSHPPSV IFYILSLLSS ACLAYVATRD NCCILDERFG SYCPTTCGIA DFLNNYQTSV
DKDLRTLEGI LYQVENKTSE ARELVKAIQI SYNPDQPSKP NNIESATKNS KSMMEEIMKY
ETLISTHEST IRFLQEVYNS NSQKIVNLRD KVVQLEANCQ EPCQDTVKIH DVTGRDCQDV
ANKGAKESGL YFIRPLKAKQ FLVYCEIDGS GNGWTVFQKR LDGSLDFKKN WIQYKEGFGH
LSPTGTGNTE FWLGNEKIHL ISTQSSIPYV LRIQLEDWNG RTSTADYASF KVTGENDKYR
LTYAYFIGGD AGDAFDGYDF GDDSSDKFFT SHNGMQFSTW DSDNDKYDGN CAEQVGIGWW
MNKCHAGHLN GVYYQGGTYS KTSTPNGYDN GIIWATWKSR WYSMKKTTMK IIPLNRLAIG
EGQQHQLGGA KQVGVEHHVE IEYD
