Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - O88947 (FA10_MOUSE)

Entry version 186 (23 Feb 2022)
Sequence version 1 (01 Nov 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Coagulation factor X

Gene

F10

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

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. EC:3.4.21.6

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei273Charge relay systemBy similarity1
Active sitei319Charge relay systemBy similarity1
Active sitei416Charge relay systemBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-140834, Extrinsic Pathway of Fibrin Clot Formation
R-MMU-140837, Intrinsic Pathway of Fibrin Clot Formation
R-MMU-140875, Common Pathway of Fibrin Clot Formation
R-MMU-159740, Gamma-carboxylation of protein precursors
R-MMU-159763, Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-MMU-159782, Removal of aminoterminal propeptides from gamma-carboxylated proteins

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.216

<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%5Fand%5Ftaxonomy%5Fsection">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:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Cleaved into the following 3 chains:
Factor X light chain
Factor X heavy chain
Activated factor Xa heavy chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:F10
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 8

Organism-specific databases

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

More...MGIi		MGI:103107, F10

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000031444

<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

Keywords - Cellular componenti

Secreted

<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 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002779221 – 40By similarityAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002779341 – 481Coagulation factor XAdd BLAST441
ChainiPRO_000002779441 – 180Factor X light chainBy similarityAdd BLAST140
ChainiPRO_0000027795184 – 481Factor X heavy chainBy similarityAdd BLAST298
PropeptideiPRO_0000027796184 – 231Activation peptideBy similarityAdd BLAST48
ChainiPRO_0000027797232 – 481Activated factor Xa heavy chainBy similarityAdd BLAST250

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 residuei464-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotationBy similarity1
<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 bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 339Interchain (between light and heavy chains)PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi187N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi218N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi238 ↔ 243By similarity
Disulfide bondi258 ↔ 274By similarity
Disulfide bondi387 ↔ 401By similarity
Disulfide bondi412 ↔ 440By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.By similarity
Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3413

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O88947

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

More...PaxDbi		O88947

PeptideAtlas

More...PeptideAtlasi		O88947

PRoteomics IDEntifications database

More...PRIDEi		O88947

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		275832

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O88947, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O88947

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

More...PhosphoSitePlusi		O88947

<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

Plasma; synthesized in the liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000031444, Expressed in liver and 124 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O88947, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O88947, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds.

Forms a heterodimer with SERPINA5 (By similarity).

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		199566, 10 interactors

Protein interaction database and analysis system

More...IntActi		O88947, 2 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000068389

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O88947, protein

<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		O88947

Database of comparative protein structure models

More...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%5Fand%5Fdomains%5Fsection">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>Domaini41 – 85GlaPROSITE-ProRule annotationAdd BLAST45
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini125 – 165EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini232 – 464Peptidase S1PROSITE-ProRule annotationAdd BLAST233

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QS4N, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157694

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006842_19_5_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O88947

TreeFam database of animal gene trees

More...TreeFami		TF327329

Family and domain databases

Conserved Domains Database

More...CDDi		cd00190, Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
4.10.740.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017857, Coagulation_fac-like_Gla_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR035972, GLA-like_dom_SF
IPR000294, GLA_domain
IPR012224, Pept_S1A_FX
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00008, EGF, 1 hit
PF00594, Gla, 1 hit
PF00089, Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001143, Factor_X, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722, CHYMOTRYPSIN
PR00001, GLABLOOD

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 2 hits
SM00179, EGF_CA, 1 hit
SM00069, GLA, 1 hit
SM00020, Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 1 hit
SSF57630, SSF57630, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS00011, GLA_1, 1 hit
PS50998, GLA_2, 1 hit
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

O88947-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK 
        60         70         80         90        100
GNLERECMEE ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA 
       110        120        130        140        150
CRDGIGGYTC TCSEGFEGKN CELFVRKLCR LDNGDCDQFC REEQNSVVCS 
       160        170        180        190        200
CASGYFLGND GKSCISTAPF PCGKITTGRR KRSVALNTSD SELDLEDALL 
       210        220        230        240        250
DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD GECPWQALLI 
       260        270        280        290        300
NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH 
       310        320        330        340        350
EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL 
       360        370        380        390        400
MTQKTGIVSG FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF 
       410        420        430        440        450
CAGYEAKLED ACQGDSGGPH VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT 
       460        470        480 
KVTTFLKWID RSMKARVGPT AETPRTAGPP N
Length:481
Mass (Da):54,018
Last modified:November 1, 1998 - 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:i8AC09DE5EF9D271E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U3V1Q3U3V1_MOUSE
Coagulation factor X
F10
493Annotation score:

Annotation score:2 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>
D3Z215D3Z215_MOUSE
Coagulation factor X
F10
321Annotation score:

Annotation score:2 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>
D3Z521D3Z521_MOUSE
Coagulation factor X
F10
319Annotation score:

Annotation score:2 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>
D3Z7R3D3Z7R3_MOUSE
Coagulation factor X
F10
119Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti250I → V in AAH03877 (PubMed:15489334).Curated1
Sequence conflicti294E → D in CAA10933 (PubMed:9783672).Curated1
Sequence conflicti298M → L in CAA10933 (PubMed:9783672).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF087644 mRNA Translation: AAC36345.1
AJ222677 mRNA Translation: CAA10933.1
AF211347 Genomic DNA Translation: AAF22980.1
BC003877 mRNA Translation: AAH03877.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS40226.1

NCBI Reference Sequences

More...RefSeqi		NP_031998.3, NM_007972.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14058

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14058

UCSC genome browser

More...UCSCi		uc009kws.2, mouse

<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
AF087644 mRNA Translation: AAC36345.1
AJ222677 mRNA Translation: CAA10933.1
AF211347 Genomic DNA Translation: AAF22980.1
BC003877 mRNA Translation: AAH03877.1
CCDSiCCDS40226.1
RefSeqiNP_031998.3, NM_007972.4

3D structure databases

SMRiO88947
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi199566, 10 interactors
IntActiO88947, 2 interactors
STRINGi10090.ENSMUSP00000068389

Protein family/group databases

MEROPSiS01.216

PTM databases

GlyGeniO88947, 2 sites
iPTMnetiO88947
PhosphoSitePlusiO88947

Proteomic databases

CPTACinon-CPTAC-3413
jPOSTiO88947
PaxDbiO88947
PeptideAtlasiO88947
PRIDEiO88947
ProteomicsDBi275832

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		11687, 683 antibodies from 35 providers

The DNASU plasmid repository

More...DNASUi		14058

Genome annotation databases

EnsembliENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444
GeneIDi14058
KEGGimmu:14058
UCSCiuc009kws.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2159
MGIiMGI:103107, F10
VEuPathDBiHostDB:ENSMUSG00000031444

Phylogenomic databases

eggNOGiENOG502QS4N, Eukaryota
GeneTreeiENSGT00940000157694
HOGENOMiCLU_006842_19_5_1
InParanoidiO88947
TreeFamiTF327329

Enzyme and pathway databases

ReactomeiR-MMU-140834, Extrinsic Pathway of Fibrin Clot Formation
R-MMU-140837, Intrinsic Pathway of Fibrin Clot Formation
R-MMU-140875, Common Pathway of Fibrin Clot Formation
R-MMU-159740, Gamma-carboxylation of protein precursors
R-MMU-159763, Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-MMU-159782, Removal of aminoterminal propeptides from gamma-carboxylated proteins

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		14058, 2 hits in 65 CRISPR screens

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

More...ChiTaRSi		F10, mouse

Protein Ontology

More...PROi		PR:O88947
RNActiO88947, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000031444, Expressed in liver and 124 other tissues
ExpressionAtlasiO88947, baseline and differential
GenevisibleiO88947, MM

Family and domain databases

CDDicd00190, Tryp_SPc, 1 hit
Gene3Di2.40.10.10, 2 hits
4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857, Coagulation_fac-like_Gla_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR035972, GLA-like_dom_SF
IPR000294, GLA_domain
IPR012224, Pept_S1A_FX
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER
PfamiView protein in Pfam
PF00008, EGF, 1 hit
PF00594, Gla, 1 hit
PF00089, Trypsin, 1 hit
PIRSFiPIRSF001143, Factor_X, 1 hit
PRINTSiPR00722, CHYMOTRYPSIN
PR00001, GLABLOOD
SMARTiView protein in SMART
SM00181, EGF, 2 hits
SM00179, EGF_CA, 1 hit
SM00069, GLA, 1 hit
SM00020, Tryp_SPc, 1 hit
SUPFAMiSSF50494, SSF50494, 1 hit
SSF57630, SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS00011, GLA_1, 1 hit
PS50998, GLA_2, 1 hit
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiFA10_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: O88947
Secondary accession number(s): O54740, Q99L32
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 1, 1998
Last modified: February 23, 2022
This is version 186 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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again