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UniProtKB - P00741 (FA9_BOVIN)

Entry version 207 (25 May 2022)
Sequence version 2 (27 May 2015)
Previous versions | rss
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Protein

Coagulation factor IX

Gene

F9

Organism
Bos taurus (Bovine)
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 IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.

1 Publication

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi47Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi48Calcium 2Combined sources1 Publication1
Metal bindingi53Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi53Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi61Calcium 4; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi61Magnesium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi66Calcium 4; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi66Magnesium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi67Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi72Calcium 5; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi72Magnesium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi73Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi73Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi76Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi76Calcium 5; via 4-carboxyglutamateBy similarity1
Metal bindingi76Magnesium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi82Calcium 6; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi82Magnesium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi86Calcium 6; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi86Magnesium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi93Calcium 7By similarity1
Metal bindingi94Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi96Calcium 7By similarity1
Metal bindingi110Calcium 7By similarity1
Metal bindingi111Calcium 7; via carbonyl oxygenBy similarity1
<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 sitei268Charge relay systemBy similarity1
Metal bindingi282Calcium 8By similarity1
Metal bindingi284Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi289Calcium 8By similarity1
Metal bindingi292Calcium 8By similarity1
Active sitei316Charge relay systemBy similarity1
Active sitei412Charge 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, Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00741

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.214

<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 IX (EC:3.4.21.22)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
Coagulation factor IXa light chain
Coagulation factor IXa 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:F9
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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: Unplaced

<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 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

Keywords - Diseasei

Hemophilia

<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 – 25Sequence analysisAdd BLAST25
<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_000002774126 – 462Coagulation factor IXAdd BLAST437
<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_000043308429 – 46By similarityAdd BLAST18
ChainiPRO_000002774247 – 192Coagulation factor IXa light chainAdd BLAST146
PropeptideiPRO_0000027743193 – 227Activation peptideAdd BLAST35
ChainiPRO_0000027744228 – 462Coagulation factor IXa heavy chainAdd BLAST235

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 residuei534-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
<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 bondi64 ↔ 69Combined sources1 Publication
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Modified residuei824-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
<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>Glycosylationi85O-linked (GalNAc...) threonineBy similarity1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications1
Disulfide bondi97 ↔ 108By similarity
GlycosylationiCAR_00000899O-linked (Glc...) serine3 Publications1
Disulfide bondi102 ↔ 117By similarity
Modified residuei110(3R)-3-hydroxyaspartate1 Publication1
Modified residuei114PhosphoserineBy similarity1
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 336Interchain (between light and heavy chains)By similarity
Modified residuei202SulfotyrosineBy similarity1
Glycosylationi204N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei205PhosphoserineBy similarity1
Glycosylationi214N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi219N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi253 ↔ 269By similarity
Glycosylationi307N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi383 ↔ 397By similarity
Disulfide bondi408 ↔ 436By 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

Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.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>Sitei192 – 193Cleavage; by factor XIa2
Sitei227 – 228Cleavage; by factor XIa2

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

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

More...PaxDbi		P00741

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		97, 5 N-Linked glycans, 1 O-Linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P00741

<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

Detected in blood plasma (at protein level) (PubMed:12695512).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000004003, Expressed in liver and 17 other tissues

<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

Heterodimer of a light chain and a heavy chain; disulfide-linked,

Interacts with SERPINC1 (By similarity).

Interacts with the heterodimeric snake venom coagulation factor IX-binding protein (PubMed:12695512).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000005227

<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

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P00741

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

More...SMRi		P00741

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00741

<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>Domaini47 – 92GlaPROSITE-ProRule annotationAdd BLAST46
Domaini93 – 129EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini130 – 171EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini228 – 460Peptidase S1PROSITE-ProRule annotationAdd BLAST233

<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

Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain (PubMed:12695512). Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (By similarity). Under physiological ion concentrations, Ca2+ is displaced by Mg2+ from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (PubMed:12695512).By similarity1 Publication

<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, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QUEV, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00741

Database of Orthologous Groups

More...OrthoDBi		1314811at2759

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
IPR035694, Coagulation_factor_IX
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

The PANTHER Classification System

More...PANTHERi		PTHR24278:SF31, PTHR24278:SF31, 1 hit

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>Sequencei

<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.

P00741-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWCLNMIMAE SPGLVTICLL GYLLSAECTV FLDRENATKI LHRPKRYNSG 
        60         70         80         90        100
KLEEFVRGNL ERECKEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN 
       110        120        130        140        150
PCLNGGMCKD DINSYECWCQ AGFEGTNCEL DATCSIKNGR CKQFCKRDTD 
       160        170        180        190        200
NKVVCSCTDG YRLAEDQKSC EPAVPFPCGR VSVSHISKKL TRAETIFSNT 
       210        220        230        240        250
NYENSSEAEI IWDNVTQSNQ SFDEFSRVVG GEDAERGQFP WQVLLHGEIA 
       260        270        280        290        300
AFCGGSIVNE KWVVTAAHCI KPGVKITVVA GEHNTEKPEP TEQKRNVIRA 
       310        320        330        340        350
IPYHSYNASI NKYSHDIALL ELDEPLELNS YVTPICIADR DYTNIFLKFG 
       360        370        380        390        400
YGYVSGWGKV FNRGRSASIL QYLKVPLVDR ATCLRSTKFS IYSHMFCAGY 
       410        420        430        440        450
HEGGKDSCQG DSGGPHVTEV EGTSFLTGII SWGEECAMKG KYGIYTKVSR 
       460 
YVNWIKEKTK LT
Length:462
Mass (Da):52,046
Last modified:May 27, 2015 - v2
<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:i415B2A7BD6EA256A
GO

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 conflicti110D → T AA sequence (PubMed:291916).Curated1
Sequence conflicti347L → S AA sequence (PubMed:291916).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
DAAA02067809 Genomic DNA No translation available.
DAAA02067810 Genomic DNA No translation available.
J00007 mRNA Translation: AAA30520.1

Protein sequence database of the Protein Information Resource

More...PIRi		A14757, KFBO

NCBI Reference Sequences

More...RefSeqi		XP_005227591.1, XM_005227534.3

<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
DAAA02067809 Genomic DNA No translation available.
DAAA02067810 Genomic DNA No translation available.
J00007 mRNA Translation: AAA30520.1
PIRiA14757, KFBO
RefSeqiXP_005227591.1, XM_005227534.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J34X-ray1.55C47-92[»]
1J35X-ray1.80C47-92[»]
AlphaFoldDBiP00741
SMRiP00741
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005227

Protein family/group databases

MEROPSiS01.214

PTM databases

GlyConnecti97, 5 N-Linked glycans, 1 O-Linked glycan (1 site)
iPTMnetiP00741

Proteomic databases

PaxDbiP00741

Phylogenomic databases

eggNOGiENOG502QUEV, Eukaryota
InParanoidiP00741
OrthoDBi1314811at2759
TreeFamiTF327329

Enzyme and pathway databases

SABIO-RKiP00741

Miscellaneous databases

EvolutionaryTraceiP00741

Gene expression databases

BgeeiENSBTAG00000004003, Expressed in liver and 17 other tissues

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
IPR035694, Coagulation_factor_IX
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
PANTHERiPTHR24278:SF31, PTHR24278:SF31, 1 hit
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 nameiFA9_BOVIN
<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: P00741
Secondary accession number(s): F1MFL4
<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: July 21, 1986
Last sequence update: May 27, 2015
Last modified: May 25, 2022
This is version 207 of the entry and version 2 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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