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Entry version 81 (16 Oct 2019)
Sequence version 1 (05 Apr 2011)
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Protein

Fibrinogen alpha chain

Gene

Fga

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots (PubMed:7649481). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (PubMed:11389004). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood (PubMed:7649481). However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (PubMed:10930441). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (PubMed:7649481). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (PubMed:12629066). May also facilitate the immune response via both innate and T-cell mediated pathways (PubMed:23487423).By similarity7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi714CalciumBy similarity1
Metal bindingi716CalciumBy similarity1
Metal bindingi718Calcium; via carbonyl oxygenBy similarity1
Metal bindingi720Calcium; via carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAdaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-114608 Platelet degranulation
R-MMU-140875 Common Pathway of Fibrin Clot Formation
R-MMU-216083 Integrin cell surface interactions
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-MMU-372708 p130Cas linkage to MAPK signaling for integrins
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5686938 Regulation of TLR by endogenous ligand
R-MMU-8957275 Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Fibrinopeptide ABy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FgaImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1316726 Fga

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Knockout mice are viable but only males are fertile (PubMed:7649481). Neonates frequently develop spontaneous hemorrhages, but in spite of this over 90% of mice survive the neonatal period (PubMed:7649481). However only half survive beyond 70 days of age; lethality is most often due to intra-abdominal hemorrhage (PubMed:7649481). Pregnancy in female mice fails at around 10 days of gestation, associated with severe intrauterine bleeding (PubMed:7649481). Secondary loss of FGB and FGG from circulating blood is observed, although FGB and FGG mRNA is normally expressed in hepatocytes (thought to be the main site of fibrinogen synthesis) (PubMed:7649481). In vitro, blood fails to clot and platelet aggregations do not form (PubMed:7649481). In vivo, platelet aggregation in injured arterioles initially occurs normally although thrombi are unstable and readily embolize (PubMed:10930441). In double knockouts of FGA and VWF, platelet aggregation is delayed and thrombi frequently embolize (PubMed:10930441). Mice succumb more rapidly to Y. pestis infection, associated with increased bacterial loads in liver and lung; however induction of the inflammatory response factors TNF, IFNG, CXCL1, and LCN2 is not affected (PubMed:23487423). Mice succumb more rapidly to T. gondii infection, with increased hemorrhagic pathology; however parasite numbers are not significantly increased and induction of the inflammatory response markers IL12, IFNG, TNF, IL10, and nitric oxide is not affected (PubMed:12629066). Mice succumb more rapidly to L. monocytogenes infection, with increased hemorrhagic pathology and increased bacterial burdens in hepatic tissue; however there is little effect on peritoneal bacterial numbers or bacterial dissemination to other tissues, and also no effect on induction of the inflammatory markers IFNG, TNF and NOS2 (PubMed:15972474).5 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisBy similarityAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000043078920 – 36Fibrinopeptide ABy similarityAdd BLAST17
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000043079037 – 789Fibrinogen alpha chainAdd BLAST753

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei46PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi48InterchainBy similarity
Disulfide bondi56Interchain (with beta chain)By similarity
Disulfide bondi65Interchain (with gamma chain)By similarity
Disulfide bondi69Interchain (with beta chain)By similarity
Disulfide bondi181Interchain (with gamma chain)By similarity
Disulfide bondi185Interchain (with C-213 in beta chain)By similarity
Disulfide bondi408 ↔ 438By similarity
Modified residuei447PhosphoserineCombined sources1
Modified residuei5044-hydroxyproline; by P4HA1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi609N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi722 ↔ 735By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.By similarity
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.By similarity
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei36 – 37Cleavage; by thrombin; to release fibrinopeptide ABy similarity2
Sitei101 – 102Cleavage; by plasmin; to break down fibrin clotsBy similarity2
Sitei122 – 123Cleavage; by hementin; to prevent blood coagulationBy similarity2
Sitei124 – 125Cleavage; by plasmin; to break down fibrin clotsBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3709

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
E9PV24

MaxQB - The MaxQuant DataBase

More...
MaxQBi
E9PV24

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
E9PV24

PeptideAtlas

More...
PeptideAtlasi
E9PV24

PRoteomics IDEntifications database

More...
PRIDEi
E9PV24

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
E9PV24

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
E9PV24

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in liver.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028001 Expressed in 63 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
E9PV24 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199636, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1916 Fibrinogen

Protein interaction database and analysis system

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IntActi
E9PV24, 5 interactors

Molecular INTeraction database

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MINTi
E9PV24

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000133117

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
E9PV24

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini546 – 787Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST242

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili69 – 554By similarityAdd BLAST486

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi266 – 348Gly-richPROSITE-ProRule annotationAdd BLAST83

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.By similarity

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2579 Eukaryota
ENOG410ZYS4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157467

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000285947

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
E9PV24

KEGG Orthology (KO)

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KOi
K03903

Identification of Orthologs from Complete Genome Data

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OMAi
WVSFRGA

Database of Orthologous Groups

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OrthoDBi
363208at2759

TreeFam database of animal gene trees

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TreeFami
TF351984

Family and domain databases

Conserved Domains Database

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CDDi
cd00087 FReD, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR021996 Fibrinogen_aC
IPR020837 Fibrinogen_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08702 Fib_alpha, 1 hit
PF12160 Fibrinogen_aC, 1 hit
PF00147 Fibrinogen_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56496 SSF56496, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: E9PV24-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLSLRVTCLI LSVASTVWTT DTEDKGEFLS EGGGVRGPRV VERHQSQCKD
60 70 80 90 100
SDWPFCSDDD WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQRNN
110 120 130 140 150
KDSNSLTRNI MEYLRGDFAN ANNFDNTYGQ VSEDLRRRIE ILRRKVIEKA
160 170 180 190 200
QQIQALQSNV RAQLIDMKRL EVDIDIKIRS CKGSCSRAVN REINLQDYEG
210 220 230 240 250
HQKQLQQVIA KELLPTKDRQ YLPALKMSPV PDLVPGSFKS QLQEAPPEWK
260 270 280 290 300
ALTEMRQMRM ELERPGKDGG SRGDSPGDSR GDSRGDFATR GPGSKAENPT
310 320 330 340 350
NPGPGGSGYW RPGNSGSGSD GNRNPGTTGS DGTGDWGTGS PRPGSDSGNF
360 370 380 390 400
RPANPNWGVF SEFGDSSSPA TRKEYHTGKA VTSKGDKELL IGKEKVTSSG
410 420 430 440 450
TSTTHRSCSK TITKTVTGPD GRREVVKEVI TSDDGSDCGD ATELDISHSF
460 470 480 490 500
SGSLDELSER HPDLSGFFDN HFGLISPNFK EFGSKTHSDS DILTNIEDPS
510 520 530 540 550
SHVPEFSSSS KTSTVKKQVT KTYKMADEAG SEAHREGETR NTKRGRARAR
560 570 580 590 600
PTRDCDDVLQ TQTSGAQNGI FSIKPPGSSK VFSVYCDQET SLGGWLLIQQ
610 620 630 640 650
RMDGSLNFNR TWQDYKRGFG SLNDKGEGEF WLGNDYLHLL TLRGSVLRVE
660 670 680 690 700
LEDWAGKEAY AEYHFRVGSE AEGYALQVSS YRGTAGDALV QGSVEEGTEY
710 720 730 740 750
TSHSNMQFST FDRDADQWEE NCAEVYGGGW WYNSCQAANL NGIYYPGGTY
760 770 780
DPRNNSPYEI ENGVVWVPFR GADYSLRAVR MKIRPLVGQ
Length:789
Mass (Da):87,429
Last modified:April 5, 2011 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i16B968D6E4952CF7
GO
Isoform 2 (identifier: E9PV24-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     554-557: DCDD → GIDT
     558-789: Missing.

Show »
Length:557
Mass (Da):61,326
Checksum:iC47F496D1BA432DE
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057097554 – 557DCDD → GIDT in isoform 2. 1 Publication4
Alternative sequenceiVSP_057098558 – 789Missing in isoform 2. 1 PublicationAdd BLAST232

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AC138394 Genomic DNA No translation available.
BC005467 mRNA Translation: AAH05467.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS17431.1 [E9PV24-2]
CCDS50939.1 [E9PV24-1]

NCBI Reference Sequences

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RefSeqi
NP_001104518.1, NM_001111048.2 [E9PV24-1]
NP_034326.1, NM_010196.4 [E9PV24-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000029630; ENSMUSP00000029630; ENSMUSG00000028001 [E9PV24-2]
ENSMUST00000166581; ENSMUSP00000133117; ENSMUSG00000028001 [E9PV24-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
14161

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14161

UCSC genome browser

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UCSCi
uc008ppf.2 mouse [E9PV24-2]
uc012cqw.1 mouse [E9PV24-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC138394 Genomic DNA No translation available.
BC005467 mRNA Translation: AAH05467.1
CCDSiCCDS17431.1 [E9PV24-2]
CCDS50939.1 [E9PV24-1]
RefSeqiNP_001104518.1, NM_001111048.2 [E9PV24-1]
NP_034326.1, NM_010196.4 [E9PV24-2]

3D structure databases

SMRiE9PV24
ModBaseiSearch...

Protein-protein interaction databases

BioGridi199636, 1 interactor
ComplexPortaliCPX-1916 Fibrinogen
IntActiE9PV24, 5 interactors
MINTiE9PV24
STRINGi10090.ENSMUSP00000133117

PTM databases

iPTMnetiE9PV24
PhosphoSitePlusiE9PV24

Proteomic databases

CPTACinon-CPTAC-3709
jPOSTiE9PV24
MaxQBiE9PV24
PaxDbiE9PV24
PeptideAtlasiE9PV24
PRIDEiE9PV24

Genome annotation databases

EnsembliENSMUST00000029630; ENSMUSP00000029630; ENSMUSG00000028001 [E9PV24-2]
ENSMUST00000166581; ENSMUSP00000133117; ENSMUSG00000028001 [E9PV24-1]
GeneIDi14161
KEGGimmu:14161
UCSCiuc008ppf.2 mouse [E9PV24-2]
uc012cqw.1 mouse [E9PV24-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2243
MGIiMGI:1316726 Fga

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000157467
HOGENOMiHOG000285947
InParanoidiE9PV24
KOiK03903
OMAiWVSFRGA
OrthoDBi363208at2759
TreeFamiTF351984

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-140875 Common Pathway of Fibrin Clot Formation
R-MMU-216083 Integrin cell surface interactions
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-MMU-372708 p130Cas linkage to MAPK signaling for integrins
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5686938 Regulation of TLR by endogenous ligand
R-MMU-8957275 Post-translational protein phosphorylation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Fga mouse

Protein Ontology

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PROi
PR:E9PV24

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028001 Expressed in 63 organ(s), highest expression level in liver
GenevisibleiE9PV24 MM

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR021996 Fibrinogen_aC
IPR020837 Fibrinogen_CS
PfamiView protein in Pfam
PF08702 Fib_alpha, 1 hit
PF12160 Fibrinogen_aC, 1 hit
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFIBA_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: E9PV24
Secondary accession number(s): Q99K47
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: April 5, 2011
Last modified: October 16, 2019
This is version 81 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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