Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 142 (07 Oct 2020)
Sequence version 1 (01 Dec 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Coagulation factor IX

Gene

F9

Organism
Pan troglodytes (Chimpanzee)
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>
-Protein inferred from homologyi <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.By similarity

<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 oxygenBy similarity1
Metal bindingi48Calcium 2By similarity1
Metal bindingi53Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi53Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi54Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi54Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi61Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi63Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi66Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi67Calcium 1; via 4-carboxyglutamateBy similarity1
Metal bindingi72Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi73Calcium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi73Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi76Calcium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi76Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity1
Metal bindingi82Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi86Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
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 sitei267Charge relay systemBy similarity1
Metal bindingi281Calcium 8By similarity1
Metal bindingi283Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi286Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi288Calcium 8By similarity1
Metal bindingi291Calcium 8By similarity1
Active sitei315Charge relay systemBy similarity1
Active sitei411Charge 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

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

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium, Magnesium, Metal-binding

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:3.4.21.22By similarity)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
<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>OrganismiPan troglodytes (Chimpanzee)
<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 identifieri9598 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
<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
  • UP000002277 <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 X

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:1389, F9

<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 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 – 28Sequence analysisAdd BLAST28
<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_000002776529 – 46By similarityAdd BLAST18
<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_000002776647 – 461Coagulation factor IXAdd BLAST415
ChainiPRO_000002776747 – 191Coagulation factor IXa light chainAdd BLAST145
PropeptideiPRO_0000027768192 – 226Activation peptideAdd BLAST35
ChainiPRO_0000027769227 – 461Coagulation 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 annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei634-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 bondi64 ↔ 69By similarity
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei824-carboxyglutamatePROSITE-ProRule annotationBy similarity1
<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 annotationBy similarity1
Disulfide bondi97 ↔ 108By similarity
Glycosylationi99O-linked (Glc...) serineBy similarity1
Disulfide bondi102 ↔ 117By similarity
Glycosylationi107O-linked (Fuc...) serineBy similarity1
Modified residuei110(3R)-3-hydroxyaspartateBy similarity1
Modified residuei114PhosphoserineBy similarity1
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 335Interchain (between light and heavy chains)By similarity
Modified residuei201SulfotyrosineBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei205Phosphothreonine; alternateBy similarity1
Glycosylationi205O-linked (GalNAc...) threonine; alternateBy similarity1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi215O-linked (GalNAc...) threonineBy similarity1
Glycosylationi225O-linked (GalNAc...) threonineBy similarity1
Disulfide bondi252 ↔ 268By similarity
Disulfide bondi382 ↔ 396By similarity
Disulfide bondi407 ↔ 435By 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.By similarity
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>Sitei191 – 192Cleavage; by factor XIa2
Sitei226 – 227Cleavage; by factor XIa2

Keywords - PTMi

Cleavage on pair of basic residues, 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
Q95ND7

PRoteomics IDEntifications database

More...
PRIDEi
Q95ND7

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9598.ENSPTRP00000047240

<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
Domaini227 – 459Peptidase 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. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. 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.By similarity

<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
ENOG502QUEV, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159516

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q95ND7

KEGG Orthology (KO)

More...
KOi
K01321

Identification of Orthologs from Complete Genome Data

More...
OMAi
SCTEGYQ

Database of Orthologous Groups

More...
OrthoDBi
1314811at2759

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>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 2 potential isoforms that are computationally mapped.Show allAlign All

Q95ND7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG
60 70 80 90 100
KLEEFVQGNL ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGSCKD DINSYECWCP FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD
160 170 180 190 200
NKVVCSCTEG YRLAENQKSC EPAVPFPCGR VSVSQTSKLT RAETVFPDVD
210 220 230 240 250
YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW QVVLNGKVDA
260 270 280 290 300
FCGGSIVNEK WIVTAAHCVD TGVKITVVAG EHNIEETEHT EQKRNVIRII
310 320 330 340 350
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS
360 370 380 390 400
GYVSGWGRVF HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH
410 420 430 440 450
EGGRDSCQGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY
460
VNWIKEKTKL T
Length:461
Mass (Da):51,764
Last modified:December 1, 2001 - 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:i30C2F857C0F77F45
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H2R4I6H2R4I6_PANTR
Christmas factor
F9
466Annotation score:

Annotation score:3 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>
A0A2I3SHJ3A0A2I3SHJ3_PANTR
Christmas factor
F9
423Annotation 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>

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
AB062470 Genomic DNA Translation: BAB58885.1

NCBI Reference Sequences

More...
RefSeqi
NP_001129063.1, NM_001135591.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSPTRT00000085797; ENSPTRP00000079315; ENSPTRG00000022330

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
465887

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ptr:465887

<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
AB062470 Genomic DNA Translation: BAB58885.1
RefSeqiNP_001129063.1, NM_001135591.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000047240

Protein family/group databases

MEROPSiS01.214

Proteomic databases

PaxDbiQ95ND7
PRIDEiQ95ND7

Genome annotation databases

EnsembliENSPTRT00000085797; ENSPTRP00000079315; ENSPTRG00000022330
GeneIDi465887
KEGGiptr:465887

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2158
VGNCiVGNC:1389, F9

Phylogenomic databases

eggNOGiENOG502QUEV, Eukaryota
GeneTreeiENSGT00940000159516
InParanoidiQ95ND7
KOiK01321
OMAiSCTEGYQ
OrthoDBi1314811at2759

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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_PANTR
<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: Q95ND7
<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: November 14, 2003
Last sequence update: December 1, 2001
Last modified: October 7, 2020
This is version 142 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. 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