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Entry version 173 (02 Jun 2021)
Sequence version 4 (23 Jan 2007)
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Protein

Flavodoxin/ferredoxin--NADP reductase

Gene

fpr

Organism
Escherichia coli (strain K12)
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

Transports electrons between flavodoxin or ferredoxin and NADPH (PubMed:8449868, PubMed:9839946, PubMed:12234497, PubMed:21306142).

Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497).

Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617).

6 Publications

Caution

PubMed:2834327 authors incorrectly assigned the protein to be part of FPR, the C-terminal of GlpX.Curated

<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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1) with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin 1 as substrate. kcat is 0.0039 sec(-1) with flavodoxin 2 as substrate (PubMed:12234497).2 Publications
  1. KM=3.85 µM for NADPH1 Publication
  2. KM=3.9 µM for NADPH1 Publication
  3. KM=2.04 mM for NADH1 Publication
  4. KM=12.0 µM for ferredoxin1 Publication
  5. KM=7.6 µM for flavodoxin 11 Publication
  6. KM=4.0 µM for flavodoxin 21 Publication
  7. KM=6.84 µM for flavodoxin1 Publication
  8. KM=17.6 µM for cytochrome c1 Publication
  9. KM=23.6 µM for potassium ferricyanide1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei17NADPCombined sources1 Publication1
Binding sitei66FAD; via carbonyl oxygenCombined sources2 Publications1
Binding sitei116FADCombined sources1 Publication1
Binding sitei184NADPCombined sources1 Publication1
Binding sitei220NADPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi50 – 53FADCombined sources2 Publications4
Nucleotide bindingi74 – 76FADCombined sources2 Publications3
Nucleotide bindingi143 – 144NADPCombined sources1 Publication2
Nucleotide bindingi173 – 174NADPCombined sources1 Publication2
Nucleotide bindingi214 – 216NADPCombined sources1 Publication3
Nucleotide bindingi247 – 248FADCombined sources1 Publication2

<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 functionOxidoreductase
LigandFAD, Flavoprotein, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:FLAVONADPREDUCT-MONOMER
MetaCyc:FLAVONADPREDUCT-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.18.1.2, 2026
1.19.1.1, 2026

<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:
Flavodoxin/ferredoxin--NADP reductaseCurated (EC:1.18.1.23 Publications, EC:1.19.1.12 Publications)
Alternative name(s):
Ferredoxin (flavodoxin):NADP(+) oxidoreductase1 Publication
Ferredoxin--NADP reductase1 Publication
Short name:
FNR1 Publication
Flavodoxin--NADP reductaseCurated
Short name:
FLDR1 Publication
Methyl viologen resistance protein A1 Publication
dA11 Publication
<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:fpr1 Publication
Synonyms:mvrA1 Publication
Ordered Locus Names:b3924, JW3895
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

<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

Cytoplasm

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

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

Mutant is highly sensitive to methyl viologen.1 Publication

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>Mutagenesisi144R → A: Increases Km for NADPH. 2-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi174R → A: Increases Km for NADPH. 13-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi184R → A: Increases Km for NADPH. 15-fold decrease in catalytic efficiency. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03147, Flavin adenine dinucleotide

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00001676432 – 248Flavodoxin/ferredoxin--NADP reductaseAdd BLAST247

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P28861

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

More...
PaxDbi
P28861

PRoteomics IDEntifications database

More...
PRIDEi
P28861

<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

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261115, 4 interactors

Protein interaction database and analysis system

More...
IntActi
P28861, 6 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3924

<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

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P28861

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
P28861

<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>Domaini2 – 101FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST100

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1018, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003827_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28861

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P28861

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06195, FNR1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR033892, FNR_bac
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00175, NAD_binding_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51384, FAD_FR, 1 hit

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

<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.

P28861-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADWVTGKVT KVQNWTDALF SLTVHAPVLP FTAGQFTKLG LEIDGERVQR
60 70 80 90 100
AYSYVNSPDN PDLEFYLVTV PDGKLSPRLA ALKPGDEVQV VSEAAGFFVL
110 120 130 140 150
DEVPHCETLW MLATGTAIGP YLSILQLGKD LDRFKNLVLV HAARYAADLS
160 170 180 190 200
YLPLMQELEK RYEGKLRIQT VVSRETAAGS LTGRIPALIE SGELESTIGL
210 220 230 240
PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG HMTAEHYW
Length:248
Mass (Da):27,751
Last modified:January 23, 2007 - v4
<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:iCBF46435A95709E4
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence Z11767 differs from that shown. Reason: Frameshift.Curated

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
L04757 Genomic DNA Translation: AAA23805.1
L19201 Genomic DNA Translation: AAB03056.1
U00096 Genomic DNA Translation: AAC76906.1
AP009048 Genomic DNA Translation: BAE77386.1
Z11767 Genomic DNA No translation available.
M19644 Genomic DNA Translation: AAA24189.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...
PIRi
S40867

NCBI Reference Sequences

More...
RefSeqi
NP_418359.1, NC_000913.3
WP_000796332.1, NZ_SSZK01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76906; AAC76906; b3924
BAE77386; BAE77386; BAE77386

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948414

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3895
eco:b3924

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2781

<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
L04757 Genomic DNA Translation: AAA23805.1
L19201 Genomic DNA Translation: AAB03056.1
U00096 Genomic DNA Translation: AAC76906.1
AP009048 Genomic DNA Translation: BAE77386.1
Z11767 Genomic DNA No translation available.
M19644 Genomic DNA Translation: AAA24189.1 Sequence problems.
PIRiS40867
RefSeqiNP_418359.1, NC_000913.3
WP_000796332.1, NZ_SSZK01000014.1

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
1FDRX-ray1.70A1-248[»]
2XNJX-ray1.90A/B2-247[»]
SMRiP28861
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261115, 4 interactors
IntActiP28861, 6 interactors
STRINGi511145.b3924

Chemistry databases

DrugBankiDB03147, Flavin adenine dinucleotide

Proteomic databases

jPOSTiP28861
PaxDbiP28861
PRIDEiP28861

Genome annotation databases

EnsemblBacteriaiAAC76906; AAC76906; b3924
BAE77386; BAE77386; BAE77386
GeneIDi948414
KEGGiecj:JW3895
eco:b3924
PATRICifig|1411691.4.peg.2781

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1480

Phylogenomic databases

eggNOGiCOG1018, Bacteria
HOGENOMiCLU_003827_3_0_6
InParanoidiP28861
PhylomeDBiP28861

Enzyme and pathway databases

BioCyciEcoCyc:FLAVONADPREDUCT-MONOMER
MetaCyc:FLAVONADPREDUCT-MONOMER
BRENDAi1.18.1.2, 2026
1.19.1.1, 2026

Miscellaneous databases

EvolutionaryTraceiP28861

Protein Ontology

More...
PROi
PR:P28861

Family and domain databases

CDDicd06195, FNR1, 1 hit
Gene3Di3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR033892, FNR_bac
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00175, NAD_binding_1, 1 hit
SUPFAMiSSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS51384, FAD_FR, 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 nameiFENR_ECOLI
<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: P28861
Secondary accession number(s): P11007, Q2M8M0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 173 of the entry and version 4 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 programProkaryotic 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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