FIBG_RAT
ID FIBG_RAT Reviewed; 445 AA.
AC P02680; Q68FY3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Fibrinogen gamma chain;
DE Flags: Precursor;
GN Name=Fgg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-B AND GAMMA-A).
RX PubMed=6897622; DOI=10.1016/0092-8674(82)90415-9;
RA Crabtree G.R., Kant J.A.;
RT "Organization of the rat gamma-fibrinogen gene: alternative mRNA splice
RT patterns produce the gamma A and gamma B (gamma ') chains of fibrinogen.";
RL Cell 31:159-166(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3562236; DOI=10.1093/nar/15.6.2774;
RA Morgan J.G., Holbrook N.J., Crabtree G.R.;
RT "Nucleotide sequence of the gamma chain gene of rat fibrinogen: conserved
RT intronic sequences.";
RL Nucleic Acids Res. 15:2774-2776(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RX PubMed=6232608; DOI=10.1073/pnas.81.8.2313;
RA Fowlkes D.M., Mullis N.T., Comeau C.M., Crabtree G.R.;
RT "Potential basis for regulation of the coordinately expressed fibrinogen
RT genes: homology in the 5' flanking regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2313-2316(1984).
RN [5]
RP PROTEIN SEQUENCE OF 122-134, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250|UniProtKB:P02679}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02679}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Gamma-B;
CC IsoId=P02680-1; Sequence=Displayed;
CC Name=Gamma-A;
CC IsoId=P02680-2; Sequence=VSP_001538, VSP_001539;
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:0000250|UniProtKB:P02679}.
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; J00733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00734; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; J00735; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X05860; CAA29289.1; -; Genomic_DNA.
DR EMBL; X05861; CAA29289.1; JOINED; Genomic_DNA.
DR EMBL; BC078893; AAH78893.1; -; mRNA.
DR EMBL; K01337; AAA98626.1; -; Genomic_DNA.
DR PIR; A03128; FGRTGB.
DR PIR; A90828; FGRTGA.
DR RefSeq; NP_036691.2; NM_012559.2. [P02680-2]
DR RefSeq; XP_006232587.1; XM_006232525.1. [P02680-1]
DR AlphaFoldDB; P02680; -.
DR SMR; P02680; -.
DR BioGRID; 246539; 1.
DR IntAct; P02680; 2.
DR STRING; 10116.ENSRNOP00000032735; -.
DR GlyGen; P02680; 1 site.
DR iPTMnet; P02680; -.
DR PhosphoSitePlus; P02680; -.
DR PaxDb; P02680; -.
DR PRIDE; P02680; -.
DR Ensembl; ENSRNOT00000034521; ENSRNOP00000032735; ENSRNOG00000025074. [P02680-2]
DR Ensembl; ENSRNOT00000115976; ENSRNOP00000082495; ENSRNOG00000025074. [P02680-1]
DR GeneID; 24367; -.
DR KEGG; rno:24367; -.
DR UCSC; RGD:2613; rat. [P02680-1]
DR CTD; 2266; -.
DR RGD; 2613; Fgg.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158467; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; P02680; -.
DR OMA; TYHNGMR; -.
DR OrthoDB; 523014at2759; -.
DR PhylomeDB; P02680; -.
DR TreeFam; TF336658; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-354192; Integrin signaling.
DR Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P02680; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000025074; Expressed in liver and 18 other tissues.
DR Genevisible; P02680; RN.
DR GO; GO:0072562; C:blood microparticle; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005577; C:fibrinogen complex; ISO:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR GO; GO:0042730; P:fibrinolysis; ISO:RGD.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IDA:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0036345; P:platelet maturation; IEP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
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 Alternative splicing; Blood coagulation; Calcium; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT CHAIN 26..445
FT /note="Fibrinogen gamma chain"
FT /id="PRO_0000009101"
FT DOMAIN 170..416
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 400..422
FT /note="Gamma-chain polymerization, binding amino end of
FT another fibrin alpha chain"
FT /evidence="ECO:0000250"
FT REGION 424..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 35
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 45
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 49
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 161
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 165
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 179..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 352..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CROSSLNK 424
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-432)"
FT /evidence="ECO:0000250"
FT CROSSLNK 432
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-424)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 435..437
FT /note="SVE -> GDM (in isoform Gamma-A)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:6897622"
FT /id="VSP_001538"
FT VAR_SEQ 438..445
FT /note="Missing (in isoform Gamma-A)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:6897622"
FT /id="VSP_001539"
FT CONFLICT 160
FT /note="Q -> L (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="Q -> K (in Ref. 1; J00734)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..174
FT /note="HDT -> YDI (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> T (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="F -> S (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Q -> E (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="F -> S (in Ref. 1; J00734)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="I -> T (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="S -> P (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..221
FT /note="VLQ -> EFK (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="K -> L (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="I -> N (in Ref. 1; J00734 and 2; CAA29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> G (in Ref. 1; J00734)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> G (in Ref. 1; J00735)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> S (in Ref. 1; J00735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50633 MW; EB6F4FF7A7812054 CRC64;
MNWSLQLRSF ILCWALLLLS PTGLAQYTAT RDNCCILDER FGSYCPTTCG ISDFLNSYQT
DVDTDLQTLE NILQRAENRT TEAKELIKAI QVYYNPDQPP KPGMIEGATQ KSKKMVEEIL
KYEALLLTHE SSIRYLQDIY TSNKQKITNL KQKVAQLEAQ CQEPCKDSVR IHDTTGKDCQ
DIANKGAKES GLYFIRPLKA TQQFLVYCEI DGSGNGWTVL QKRLDGSVDF KKNWIQYKEG
FGHLSPTGTT EFWLGNEKIH LISMQSTIPY ALRIQLKDWS GRTSTADYAM FRVGPESDKY
RLTYAYFIGG DAGDAFDGYD FGDDPSDKFF TSHNGMHFST WDNDNDKFEG NCAEQDGSGW
WMNKCHAGHL NGVYYQGGTY SKSSTPNGYD NGIIWATWKT RWYSMKETTM KIIPFNRLSI
GDGQQHHMGG SKQVSVEHEV DVEYP
