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UniProtKB - P08709 (FA7_HUMAN)

Entry version 256 (08 May 2019)
Sequence version 1 (01 Jan 1988)
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Protein

Coagulation factor VII

Gene

F7

Organism
Homo sapiens (Human)
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

Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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-|-Ile bond in factor X to form factor Xa. EC:3.4.21.21

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>Sitei113Important for S-112 for O-xylosylation1
<p>This subsection of the ‘Function’ 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 sitei253Charge relay systemBy similarity1
Active sitei302Charge relay systemBy similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei398SubstrateBy similarity1
Active sitei404Charge 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.21 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression
R-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P08709

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.215

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Coagulation factor VII (EC:3.4.21.21)
Alternative name(s):
Proconvertin
Serum prothrombin conversion accelerator
Short name:
SPCA
INN: Eptacog alfa
Cleaved into the following 2 chains:
Factor VII light chain
Factor VII heavy chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:F7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3544 F7

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		613878 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P08709

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

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

Keywords - Cellular componenti

Secreted

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Factor VII deficiency (FA7D)26 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
See also OMIM:227500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01439113L → P in FA7D; Morioka. 1 PublicationCorresponds to variant dbSNP:rs387906507EnsemblClinVar.1
Natural variantiVAR_06536959R → RR in FA7D. 1 Publication1
Natural variantiVAR_01513564F → L in FA7D. 2 Publications1
Natural variantiVAR_01440573L → Q in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs45572939Ensembl.1
Natural variantiVAR_01440679E → Q in FA7D. 1 Publication1
Natural variantiVAR_06537082C → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1448296564Ensembl.1
Natural variantiVAR_06537182C → R in FA7D. 1 PublicationCorresponds to variant dbSNP:rs745374448Ensembl.1
Natural variantiVAR_06537284Missing in FA7D. 1 Publication1
Natural variantiVAR_06537385E → K in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964935Ensembl.1
Natural variantiVAR_06537488R → G in FA7D. 1 PublicationCorresponds to variant dbSNP:rs776354144Ensembl.1
Natural variantiVAR_06537588R → P in FA7D. 1 Publication1
Natural variantiVAR_065376117N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964932Ensembl.1
Natural variantiVAR_015136120S → P in FA7D. 2 Publications1
Natural variantiVAR_014407121C → F in FA7D. 1 Publication1
Natural variantiVAR_014408125L → P in FA7D. 1 Publication1
Natural variantiVAR_014409128Y → C in FA7D. 3 Publications1
Natural variantiVAR_065377138G → D in FA7D. 1 Publication1
Natural variantiVAR_006497139R → K in FA7D. 1
Natural variantiVAR_006498139R → Q in FA7D; Charlotte. 3 PublicationsCorresponds to variant dbSNP:rs150525536Ensembl.1
Natural variantiVAR_006499139R → W in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs776796178Ensembl.1
Natural variantiVAR_014410151C → S in FA7D. 1 Publication1
Natural variantiVAR_015137154E → K in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs146795869Ensembl.1
Natural variantiVAR_065378156G → S in FA7D. 1 PublicationCorresponds to variant dbSNP:rs563972504Ensembl.1
Natural variantiVAR_006501157G → C in FA7D. 1
Natural variantiVAR_006500157G → S in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs763458490Ensembl.1
Natural variantiVAR_014411157G → V in FA7D. 1 PublicationCorresponds to variant dbSNP:rs771335282Ensembl.1
Natural variantiVAR_006502160Q → R in FA7D. 4 PublicationsCorresponds to variant dbSNP:rs200016360Ensembl.1
Natural variantiVAR_065379171S → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs143855920Ensembl.1
Natural variantiVAR_065380177G → R in FA7D. 1 Publication1
Natural variantiVAR_065381181L → P in FA7D. 1 Publication1
Natural variantiVAR_065382183D → N in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1258691292Ensembl.1
Natural variantiVAR_065383186S → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs764971156Ensembl.1
Natural variantiVAR_065384189P → S in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1479693459Ensembl.1
Natural variantiVAR_065385194P → L in FA7D. 1 Publication1
Natural variantiVAR_006503194P → T in FA7D; Malta-I. 2 PublicationsCorresponds to variant dbSNP:rs1234759020Ensembl.1
Natural variantiVAR_014412195C → R in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs372577568Ensembl.1
Natural variantiVAR_006504197K → E in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1250204261Ensembl.1
Natural variantiVAR_065386198I → T in FA7D. 1 PublicationCorresponds to variant dbSNP:rs762621913Ensembl.1
Natural variantiVAR_006505212R → Q in FA7D; Charlotte. 4 PublicationsCorresponds to variant dbSNP:rs868044209Ensembl.1
Natural variantiVAR_015138216G → D in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs1438503836Ensembl.1
Natural variantiVAR_006506238C → Y in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964928Ensembl.1
Natural variantiVAR_065387240G → R in FA7D. 1 Publication1
Natural variantiVAR_014413241T → N in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs1160146175Ensembl.1
Natural variantiVAR_065388250S → F in FA7D. 1 Publication1
Natural variantiVAR_065389251A → P in FA7D. 1 Publication1
Natural variantiVAR_065390251A → T in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1269916662Ensembl.1
Natural variantiVAR_065391254C → R in FA7D. 1 Publication1
Natural variantiVAR_015139254C → Y in FA7D. 2 Publications1
Natural variantiVAR_065392264L → P in FA7D. 1 PublicationCorresponds to variant dbSNP:rs753266903Ensembl.1
Natural variantiVAR_015140266A → T in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs764807079Ensembl.1
Natural variantiVAR_065393272D → N in FA7D. 1 PublicationCorresponds to variant dbSNP:rs751028917Ensembl.1
Natural variantiVAR_065394277D → N in FA7D. 1 PublicationCorresponds to variant dbSNP:rs550074221Ensembl.1
Natural variantiVAR_006507283R → W in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs779589651Ensembl.1
Natural variantiVAR_065395298T → I in FA7D. 1 Publication1
Natural variantiVAR_065396301H → Q in FA7D. 1 Publication1
Natural variantiVAR_014414302D → H in FA7D. 3 Publications1
Natural variantiVAR_014415302D → N in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs770328850Ensembl.1
Natural variantiVAR_014416304A → T in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs773627551Ensembl.1
Natural variantiVAR_006508304A → V in FA7D; Malta-II. 5 PublicationsCorresponds to variant dbSNP:rs121964931Ensembl.1
Natural variantiVAR_014417307R → C in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs147680958Ensembl.1
Natural variantiVAR_006509307R → H in FA7D; Mie. 2 PublicationsCorresponds to variant dbSNP:rs121964929Ensembl.1
Natural variantiVAR_015141312V → M in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs201991361Ensembl.1
Natural variantiVAR_065397314L → V in FA7D. 1 Publication1
Natural variantiVAR_065398321L → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs778138366Ensembl.1
Natural variantiVAR_065399323L → R in FA7D. 1 Publication1
Natural variantiVAR_006510325E → K in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs749760143Ensembl.1
Natural variantiVAR_065400326R → Q in FA7D. 1 PublicationCorresponds to variant dbSNP:rs146698837Ensembl.1
Natural variantiVAR_014418332T → M in FA7D. 1 PublicationCorresponds to variant dbSNP:rs200212201Ensembl.1
Natural variantiVAR_065401337R → C in FA7D. 1 PublicationCorresponds to variant dbSNP:rs139372641Ensembl.1
Natural variantiVAR_015142341V → F in FA7D. 2 Publications1
Natural variantiVAR_065402343G → S in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs1250853566Ensembl.1
Natural variantiVAR_076570344W → G in FA7D. 1 Publication1
Natural variantiVAR_065403344W → R in FA7D. 1 Publication1
Natural variantiVAR_065404345G → S in FA7D. 1 Publication1
Natural variantiVAR_065405350R → C in FA7D. 1 PublicationCorresponds to variant dbSNP:rs747876824Ensembl.1
Natural variantiVAR_006511354A → V in FA7D. 5 PublicationsCorresponds to variant dbSNP:rs36209567EnsemblClinVar.1
Natural variantiVAR_006512358M → I in FA7D. 4 PublicationsCorresponds to variant dbSNP:rs149283257Ensembl.1
Natural variantiVAR_006513358M → V in FA7D. 1 PublicationCorresponds to variant dbSNP:rs928183869Ensembl.1
Natural variantiVAR_065406360L → P in FA7D. 1 Publication1
Natural variantiVAR_065407363P → H in FA7D. 1 Publication1
Natural variantiVAR_015143363P → R in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs963430078Ensembl.1
Natural variantiVAR_006514364R → Q in FA7D; Harrow/Padua. 6 PublicationsCorresponds to variant dbSNP:rs121964926EnsemblClinVar.1
Natural variantiVAR_065408364R → W in FA7D. 1 PublicationCorresponds to variant dbSNP:rs750980786Ensembl.1
Natural variantiVAR_006515370C → F in FA7D. 6 PublicationsCorresponds to variant dbSNP:rs121964927EnsemblClinVar.1
Natural variantiVAR_065409375R → W in FA7D. 1 PublicationCorresponds to variant dbSNP:rs137919286Ensembl.1
Natural variantiVAR_065410384T → M in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs531225271EnsemblClinVar.1
Natural variantiVAR_065411387M → T in FA7D. 1 Publication1
Natural variantiVAR_065412387M → V in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1215224419Ensembl.1
Natural variantiVAR_065413388F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. 2 PublicationsCorresponds to variant dbSNP:rs121964938Ensembl.1
Natural variantiVAR_014392389C → G in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs121964934EnsemblClinVar.1
Natural variantiVAR_065414391G → C in FA7D. 1 Publication1
Natural variantiVAR_014419391G → S in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs190485816Ensembl.1
Natural variantiVAR_065415398D → E in FA7D. 1 Publication1
Natural variantiVAR_065416401K → E in FA7D. 1 PublicationCorresponds to variant dbSNP:rs748979195Ensembl.1
Natural variantiVAR_006517402G → E in FA7D. 1 Publication1
Natural variantiVAR_006516402G → R in FA7D. 1 Publication1
Natural variantiVAR_015144403D → H in FA7D. 2 Publications1
Natural variantiVAR_065417404S → N in FA7D. 1 Publication1
Natural variantiVAR_065418408H → Q in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964936EnsemblClinVar.1
Natural variantiVAR_065419408H → R in FA7D. 1 Publication1
Natural variantiVAR_065420413R → G in FA7D. 1 Publication1
Natural variantiVAR_065421414G → C in FA7D; results in severely impaired protein secretion. 1 PublicationCorresponds to variant dbSNP:rs121964937Ensembl.1
Natural variantiVAR_006519419T → M in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs121964930Ensembl.1
Natural variantiVAR_065422422V → F in FA7D. 1 Publication1
Natural variantiVAR_065423425G → A in FA7D. 1 Publication1
Natural variantiVAR_065424425G → C in FA7D. 1 Publication1
Natural variantiVAR_065425429A → T in FA7D. 1 PublicationCorresponds to variant dbSNP:rs755377592EnsemblClinVar.1
Natural variantiVAR_065426432G → D in FA7D. 1 PublicationCorresponds to variant dbSNP:rs1450120320Ensembl.1
Natural variantiVAR_014420435G → E in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs756956471Ensembl.1
Natural variantiVAR_065427437Y → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs758213652Ensembl.1

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Available under the names Niastase or Novoseven (Novo Nordisk). Used for the treatment of bleeding episodes in hemophilia A or B patients with antibodies to coagulation factors VIII or IX.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi112S → A: Complete loss of O-glycosylation and O-xylosylation by POGLUT1. 1 Publication1
Mutagenesisi113S → A: No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		2155

MalaCards human disease database

More...MalaCardsi		F7
MIMi227500 phenotype

Open Targets

More...OpenTargetsi		ENSG00000057593

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		327 Congenital factor VII deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA160

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3991

Drug and drug target database

More...DrugBanki		DB04590 (2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID
DB07207 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE
DB04758 2-[2-ETHANESULFONYLAMINO-3-(1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIM IDOYL-BENZYLAMIDE)
DB04606 2-[2-ETHANESULFONYLAMINO-3-(5-PROPOXY-1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIMIDOYL-BENZYLAMIDE)
DB04593 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID
DB07376 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID)
DB00100 Coagulation Factor IX (Recombinant)
DB00036 Coagulation factor VIIa Recombinant Human
DB00170 Menadione
DB04767 N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2363

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		F7

Domain mapping of disease mutations (DMDM)

More...DMDMi		119766

<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_processing_section">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_000002772921 – 601 PublicationAdd BLAST40
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002773061 – 212Factor VII light chainAdd BLAST152
ChainiPRO_0000027731213 – 466Factor VII heavy chainAdd BLAST254

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 residuei664-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei744-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotation2 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 bondi77 ↔ 82
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei804-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei854-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei894-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei954-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Disulfide bondi110 ↔ 121
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000007112O-linked (Glc...) serine; alternate4 Publications1
Glycosylationi112O-linked (Xyl...) serine; alternate4 Publications1
Disulfide bondi115 ↔ 130
GlycosylationiCAR_000180120O-linked (Fuc) serine2 Publications1
Modified residuei123(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi132 ↔ 141
Disulfide bondi151 ↔ 162
Disulfide bondi158 ↔ 172
Disulfide bondi174 ↔ 187
Disulfide bondi195 ↔ 322
Glycosylationi205N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi219 ↔ 224
Disulfide bondi238 ↔ 254
Disulfide bondi370 ↔ 389
Glycosylationi382N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi400 ↔ 428

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

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
O- and N-glycosylated. N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines.5 Publications
Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei212 – 213Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin2

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08709

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08709

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

More...PaxDbi		P08709

PeptideAtlas

More...PeptideAtlasi		P08709

PRoteomics IDEntifications database

More...PRIDEi		P08709

ProteomicsDB human proteome resource

More...ProteomicsDBi		52160
52161 [P08709-2]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		98

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08709

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

More...PhosphoSitePlusi		P08709

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P08709

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P08709

<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.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000057593 Expressed in 127 organ(s), highest expression level in right lobe of liver

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P08709 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P08709 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA004826

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

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

Heterodimer of a light chain and a heavy chain linked by a disulfide bond.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
F3P137267EBI-355972,EBI-1040727

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108453, 19 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2808 Factor VII - TF complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P08709

Database of interacting proteins

More...DIPi		DIP-6135N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P08709

Protein interaction database and analysis system

More...IntActi		P08709, 10 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000364731

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P08709

<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

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1BF9NMR-A105-145[»]
1CVWX-ray2.28H213-466[»]
L150-204[»]
1DANX-ray2.00H213-466[»]
L61-212[»]
1DVAX-ray3.00H/I213-466[»]
L/M102-202[»]
1F7ENMR-A105-147[»]
1F7MNMR-A105-147[»]
1FAKX-ray2.10H213-466[»]
L61-212[»]
1FF7NMR-A105-147[»]
1FFMNMR-A105-147[»]
1J9CX-ray2.90H213-466[»]
L108-202[»]
1JBUX-ray2.00H213-466[»]
L150-212[»]
1KLIX-ray1.69H213-466[»]
L144-212[»]
1KLJX-ray2.44H213-466[»]
L144-212[»]
1NL8model-H213-466[»]
M61-202[»]
1O5DX-ray2.05H213-466[»]
L61-212[»]
1QFKX-ray2.80H213-466[»]
L109-212[»]
1W0YX-ray2.50H213-466[»]
L61-202[»]
1W2KX-ray3.00H213-466[»]
L61-202[»]
1W7XX-ray1.80H213-466[»]
L150-204[»]
1W8BX-ray3.00H213-466[»]
L148-204[»]
1WQVX-ray2.50H213-466[»]
L61-212[»]
1WSSX-ray2.60H213-466[»]
L61-212[»]
1WTGX-ray2.20H213-466[»]
L61-212[»]
1WUNX-ray2.40H213-466[»]
L61-212[»]
1WV7X-ray2.70H213-466[»]
L61-212[»]
1YGCX-ray2.00H213-466[»]
L150-212[»]
1Z6JX-ray2.00H213-466[»]
L61-202[»]
2A2QX-ray1.80H213-466[»]
L61-212[»]
2AEIX-ray2.52H213-466[»]
L61-212[»]
2AERX-ray1.87H213-466[»]
L61-202[»]
2B7DX-ray2.24H213-466[»]
L61-212[»]
2B8OX-ray2.80H213-466[»]
L61-202[»]
2BZ6X-ray1.60H213-466[»]
L150-202[»]
2C4FX-ray1.72H213-466[»]
L61-202[»]
2EC9X-ray2.00H213-466[»]
L61-202[»]
2F9BX-ray2.54H213-466[»]
L61-212[»]
2FIRX-ray2.00H213-466[»]
L61-202[»]
2FLBX-ray1.95H213-466[»]
L61-212[»]
2FLRX-ray2.35H213-466[»]
L61-212[»]
2PUQX-ray2.05H213-466[»]
L109-202[»]
2ZP0X-ray2.70H213-466[»]
L61-212[»]
2ZWLX-ray2.20H213-466[»]
L61-212[»]
2ZZUX-ray2.50H213-466[»]
L61-212[»]
3ELAX-ray2.20H213-466[»]
L61-212[»]
3TH2X-ray1.72H213-466[»]
L61-202[»]
3TH3X-ray2.70H213-466[»]
L61-202[»]
3TH4X-ray1.80H213-466[»]
L61-202[»]
4IBLX-ray1.80H213-466[»]
L61-212[»]
4ISHX-ray1.82H213-466[»]
L150-204[»]
4ISIX-ray1.94H213-466[»]
L150-204[»]
4JYUX-ray1.80H213-466[»]
L150-204[»]
4JYVX-ray2.19H213-466[»]
L150-204[»]
4JZDX-ray2.20H213-466[»]
L150-204[»]
4JZEX-ray1.52H213-466[»]
L150-204[»]
4JZFX-ray1.84H213-466[»]
L150-204[»]
4NA9X-ray2.24H213-466[»]
L150-204[»]
4NG9X-ray2.20H213-466[»]
L150-204[»]
4NGAX-ray2.15H213-466[»]
L150-204[»]
4X8SX-ray2.10H213-466[»]
L150-204[»]
4X8TX-ray2.20H213-466[»]
L150-204[»]
4X8UX-ray2.10H213-466[»]
L150-204[»]
4X8VX-ray2.50H213-466[»]
L150-204[»]
4YLQX-ray1.40H213-466[»]
L61-212[»]
4YT6X-ray2.07H213-466[»]
L148-204[»]
4YT7X-ray2.30H213-466[»]
L148-204[»]
4Z6AX-ray2.25H213-466[»]
L108-203[»]
4ZMAX-ray2.30H213-466[»]
L61-212[»]
4ZXXX-ray2.60H213-466[»]
L150-204[»]
4ZXYX-ray2.06H213-466[»]
L150-204[»]
5I46X-ray2.06H213-466[»]
L150-204[»]
5L0SX-ray1.45B105-145[»]
5L2YX-ray1.82H213-466[»]
L150-204[»]
5L2ZX-ray1.79H213-466[»]
L147-204[»]
5L30X-ray1.73H213-466[»]
L147-204[»]
5PA8X-ray1.98A149-212[»]
C213-466[»]
5PA9X-ray1.55A149-212[»]
C213-466[»]
5PAAX-ray1.98A149-212[»]
C213-466[»]
5PABX-ray1.99H213-466[»]
L149-212[»]
5PACX-ray1.50A149-212[»]
B213-466[»]
5PAEX-ray1.45A149-212[»]
B213-466[»]
5PAFX-ray1.50A149-212[»]
B213-466[»]
5PAGX-ray1.36A149-212[»]
B213-466[»]
5PAIX-ray1.73A149-212[»]
B213-466[»]
5PAJX-ray1.70A149-212[»]
B213-466[»]
5PAKX-ray1.56A149-212[»]
C213-466[»]
5PAMX-ray1.60A149-212[»]
B213-466[»]
5PANX-ray1.62A149-212[»]
B213-466[»]
5PAOX-ray1.40A149-212[»]
C213-466[»]
5PAQX-ray1.59A149-212[»]
B213-466[»]
5PARX-ray2.10A149-212[»]
C213-466[»]
5PASX-ray1.48A149-212[»]
C213-466[»]
5PATX-ray1.60A149-212[»]
B213-466[»]
5PAUX-ray1.55A149-212[»]
C213-466[»]
5PAVX-ray1.40A149-212[»]
C213-466[»]
5PAWX-ray2.20A149-212[»]
B213-466[»]
5PAXX-ray1.36A149-212[»]
C213-466[»]
5PAYX-ray1.66A149-212[»]
C213-466[»]
5PB0X-ray1.98A149-212[»]
B213-466[»]
5PB1X-ray1.90A149-212[»]
D213-466[»]
5PB2X-ray1.45A149-212[»]
C213-466[»]
5PB3X-ray1.90A149-212[»]
C213-466[»]
5PB4X-ray2.43A149-212[»]
C213-466[»]
5PB5X-ray1.84A149-212[»]
B213-466[»]
5PB6X-ray1.90A149-212[»]
C213-466[»]
5TQEX-ray1.90H213-466[»]
L150-204[»]
5TQFX-ray1.85H213-466[»]
L150-204[»]
5TQGX-ray1.90H213-466[»]
L150-204[»]
5U6JX-ray2.30H213-466[»]
L150-204[»]

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

More...SMRi		P08709

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08709

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 105GlaPROSITE-ProRule annotationAdd BLAST45
Domaini106 – 142EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini147 – 188EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini213 – 452Peptidase S1PROSITE-ProRule annotationAdd BLAST240

<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		ENOG410IIMB Eukaryota
COG5640 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154474

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08709

KEGG Orthology (KO)

More...KOi		K01320

Identification of Orthologs from Complete Genome Data

More...OMAi		SKDACKG

Database of Orthologous Groups

More...OrthoDBi		265965at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08709

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		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
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR033190 F7
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

The PANTHER Classification System

More...PANTHERi		PTHR24278:SF26 PTHR24278:SF26, 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, 1 hit
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

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

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

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

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform A (identifier: P08709-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE 
        60         70         80         90        100
AHGVLHRRRR ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF 
       110        120        130        140        150
WISYSDGDQC ASSPCQNGGS CKDQLQSYIC FCLPAFEGRN CETHKDDQLI 
       160        170        180        190        200
CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL LADGVSCTPT VEYPCGKIPI 
       210        220        230        240        250
LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG TLINTIWVVS 
       260        270        280        290        300
AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN 
       310        320        330        340        350
HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR 
       360        370        380        390        400
GATALELMVL NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC 
       410        420        430        440        450
KGDSGGPHAT HYRGTWYLTG IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL 
       460 
MRSEPRPGVL LRAPFP
Length:466
Mass (Da):51,594
Last modified:January 1, 1988 - 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:i9B5D501669D67B06
GO
Isoform B (identifier: P08709-2) [UniParc]