Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P17635 (FMO2_RABIT)

Entry version 138 (25 May 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

FMO2

Organism
Oryctolagus cuniculus (Rabbit)
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

Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation (PubMed:3785145, PubMed:10950853, PubMed:16620765, PubMed:11302936, PubMed:15144220, PubMed:15294458).

Most drug substrates are tertiary amines such as prochlorperazine and trifluoperazine which are N-oxygenated to form the N-oxide, or sulfides such as thiourea and ethionamide, which are S-oxygenated to the sulfoxide (PubMed:3785145, PubMed:15144220, PubMed:16620765).

Others include primary alkylamines such as N-dodecylamine and octan-1-amine that are sequentially monooxygenated to oximes through intermediate hydroxylamines and both steps are NADPH- and oxygen-dependent (PubMed:3785145).

Also metabolized N-Deacetyl ketoconazole (DAK) to N-hydroxy-DAK and appears to further metabolizes N-hydroxy-DAK to two others metabolites (PubMed:10950853).

Also catalyzes S-oxygenation of the thioether-containing organophosphate insecticides, phorate and disulfoton (PubMed:15294458).

6 Publications

<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

<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

Protein has several cofactor binding sites:

<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

  1. KM=36 µM for thiourea1 Publication
  2. KM=21 µM for ethylenethiourea1 Publication
  3. KM=82 µM for N-phenylthiourea1 Publication
  4. KM=25 µM for ANTU1 Publication
  5. KM=310 µM for N,N-dimethylaniline1 Publication
  6. KM=500 µM for (S)-nicotine1 Publication
  7. KM=330 µM for N,N-dimethylaniline1 Publication
  8. KM=46 µM for N,N-dimethyloctylamine1 Publication
  9. KM=31 µM for trifluoperazine1 Publication
  10. KM=1000 µM for desmethylperazine1 Publication
  11. KM=120 µM for N-methyloctylamine1 Publication
  12. KM=17 µM for N-methyloctylhydroxylamine1 Publication
  13. KM=12000 µM for octan-1-amine1 Publication
  14. KM=290 µM for N-dodecylamine1 Publication
  15. KM=70 µM for N-methyloctylhydroxylamine1 Publication
  16. KM=3 µM for N-dodecylhydroxylamine1 Publication
  17. KM=57 µM for phorate1 Publication
  18. KM=32 µM for disulfoton1 Publication
  1. Vmax=450 nmol/min/mg enzyme toward N,N-dimethylaniline1 Publication
  2. Vmax=450 nmol/min/mg enzyme toward N,N-dimethyloctylamine1 Publication
  3. Vmax=450 nmol/min/mg enzyme toward trifluoperazine1 Publication
  4. Vmax=900 nmol/min/mg enzyme toward desmethylperazine 11 Publication
  5. Vmax=550 nmol/min/mg enzyme toward N-methyloctylamine1 Publication
  6. Vmax=500 nmol/min/mg enzyme toward N-methyloctylhydroxylamine1 Publication
  7. Vmax=1600 nmol/min/mg enzyme toward octan-1-amine1 Publication
  8. Vmax=1600 nmol/min/mg enzyme toward N-dodecylamine1 Publication
  9. Vmax=600 nmol/min/mg enzyme toward N-methyloctylhydroxylamine1 Publication
  10. Vmax=600 nmol/min/mg enzyme toward N-dodecylhydroxylamine1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei32FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi9 – 13FADBy similarity5
Nucleotide bindingi40 – 41FADBy similarity2
Nucleotide bindingi60 – 61NADPBy similarity2
Nucleotide bindingi61 – 62FADBy similarity2
Nucleotide bindingi195 – 198NADPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
LigandFAD, Flavoprotein, Magnesium, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.13.8, 1749

<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:
Dimethylaniline monooxygenase [N-oxide-forming] 2By similarity (EC:1.14.13.-4 Publications, EC:1.14.13.82 Publications)
Alternative name(s):
Dimethylaniline oxidase 2
FMO 1B1
Pulmonary flavin-containing monooxygenase 2
Short name:
FMO 2
<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:FMO2By similarity
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
<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
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei510 – 530HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi510 – 535Missing : Increases protein solubility in the absence of detergent. 1 PublicationAdd BLAST26

<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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<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_00001476502 – 535Dimethylaniline monooxygenase [N-oxide-forming] 2Add BLAST534

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 residuei2N-acetylalanine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P17635

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17635

<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

Lung.

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9986.ENSOCUP00000004486

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P17635

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

More...SMRi		P17635

Database of comparative protein structure models

More...ModBasei		Search...

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

<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 FMO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1399, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17635

Database of Orthologous Groups

More...OrthoDBi		405736at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 4 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR000960, Flavin_mOase
IPR020946, Flavin_mOase-like
IPR002254, Flavin_mOase_2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00743, FMO-like, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000332, FMO, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00370, FMOXYGENASE
PR01122, FMOXYGENASE2

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P17635-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG 
        60         70         80         90        100
RASIYQSVIT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL 
       110        120        130        140        150
LKYIQFQTTV ISVKKRPDFA SSGQWEVVTQ SNSKQQSAVF DAVMVCSGHH 
       160        170        180        190        200
ILPNIPLKSF PGIEKFKGQY FHSRQYKHPA GLEGKRILVI GIGNSASDIA 
       210        220        230        240        250
VELSKKAAQV YISTRKGSWV MSRISEDGYP WDMVFHTRFS SMLRNVLPRM 
       260        270        280        290        300
IVKWMMEQQM NRWFNHENYG LAPENKYLMK EPVLNDDLPS RILYGTIKVK 
       310        320        330        340        350
RRVKELTESA AIFEDGTVEE DIDVIVFATG YTFAFPFLEE SLVKIEDNMV 
       360        370        380        390        400
SLYKYMFPPQ LEKSTFACLG LIQPLGSIFP TVELQARWAT RVFKGLCSLP 
       410        420        430        440        450
SKETMMADII KRNENRIALF GESLSQKLQT NYIDYLDELA LEIGAKPDLV 
       460        470        480        490        500
SFLFKDPKLA VKLYFGPCNS YQYRLVGPGQ WEGARNAIFT QKQRILKPLK 
       510        520        530 
TRTLKASSNF PVSFLLKFLG LFALVLAFLF QLQWF
Length:535
Mass (Da):61,144
Last modified:January 23, 2007 - v3
<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:iD51910BDA41C55C2
GO

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

There are two allelic forms.

Natural variant

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 varianti120A → S in PFMO-2 and PFMO-4. 1
Natural varianti136Q → E in PFMO-2 and PFMO-4. 1

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
M32029 mRNA Translation: AAA31442.1

Protein sequence database of the Protein Information Resource

More...PIRi		B35182

NCBI Reference Sequences

More...RefSeqi		NP_001075753.1, NM_001082284.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		100009119

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ocu:100009119

<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
M32029 mRNA Translation: AAA31442.1
PIRiB35182
RefSeqiNP_001075753.1, NM_001082284.1

3D structure databases

AlphaFoldDBiP17635
SMRiP17635
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004486

PTM databases

iPTMnetiP17635

Proteomic databases

PRIDEiP17635

Genome annotation databases

GeneIDi100009119
KEGGiocu:100009119

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2327

Phylogenomic databases

eggNOGiKOG1399, Eukaryota
InParanoidiP17635
OrthoDBi405736at2759

Enzyme and pathway databases

BRENDAi1.14.13.8, 1749

Family and domain databases

Gene3Di3.50.50.60, 4 hits
InterProiView protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR000960, Flavin_mOase
IPR020946, Flavin_mOase-like
IPR002254, Flavin_mOase_2
PfamiView protein in Pfam
PF00743, FMO-like, 1 hit
PIRSFiPIRSF000332, FMO, 1 hit
PRINTSiPR00370, FMOXYGENASE
PR01122, FMOXYGENASE2
SUPFAMiSSF51905, SSF51905, 2 hits

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 nameiFMO2_RABIT
<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: P17635
<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: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 138 of the entry and version 3 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

Direct protein sequencing, Reference proteome

Documents

  1. 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