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 - Q9GKX2 (DHRS4_RABIT)

Entry version 94 (25 May 2022)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
Add a publicationFeedback
Protein

Dehydrogenase/reductase SDR family member 4

Gene

DHRS4

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

NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones (PubMed:12604222, PubMed:9880795, PubMed:19056333).

Reduces all-trans-retinal and 9-cis retinal (Probable). Reduces 3-ketosteroids and benzil into 3alpha-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin (By similarity).

In the reverse reaction, catalyze the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency (By similarity).

Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds (PubMed:12604222, PubMed:19056333).

By similarity1 Publication3 Publications

Miscellaneous

Primate DHRS4s display different stereoselectivity and catalytic efficiency in the oxidoreduction of some substrates as compared to other mammal DHRS4s due to a difference in conserved amino acid residues.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by flavonoids (kaempferol, quercetin, quercitrin, genistein), myristic acid, pyrazole, barbital, phenobarbital and CuSO4.1 Publication1 Publication

<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 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).1 Publication
  1. KM=0.028 mM for 16-Ketoestrone (at pH6)1 Publication
  2. KM=0.045 mM for 16-Ketoestrone (at pH7.4)1 Publication
  3. KM=0.007 mM for all-trans-Retinal (at pH7.4)1 Publication
  4. KM=0.079 mM for 9-cis-retinal (at pH7.4)1 Publication
  5. KM=0.11 mM for Isatin (at pH6)1 Publication
  6. KM=0.061 mM for Isatin (at pH7.4)1 Publication
  7. KM=0.89 mM for Propiophenone (at pH6)1 Publication
  8. KM=0.063 mM for Heptanophenone (at pH6)1 Publication
  9. KM=0.027 mM for Nonanophenone (at pH6)1 Publication
  10. KM=0.095 mM for 4-Hexanoylpyridine (at pH6)1 Publication
  11. KM=0.022 mM for Hexanophenone (at pH6)1 Publication
  12. KM=0.11 mM for Valerophenone (at pH6)1 Publication
  13. KM=0.18 mM for n-Butyrophenone (at pH6)1 Publication
  14. KM=0.52 mM for 3-Benzoylpyridine (at pH6)1 Publication
  15. KM=0.69 mM for 4-Benzoylpyridine (at pH6)1 Publication
  16. KM=1.7 mM for 2,3-Hexanedione (at pH6)1 Publication
  17. KM=0.4 mM for 1-phenyl-1,2-propanedione (at pH6)1 Publication
  18. KM=0.11 mM for Benzil (at pH6)1 Publication
  19. KM=13 mM for Diacetyl (at pH6)1 Publication
  20. KM=1.8 mM for Pyridine-4-aldehyde (at pH6)1 Publication
  21. KM=0.006 mM for 1-Phenylisatin (at pH6)1 Publication
  22. KM=0.001 mM for 9,10-Phenanthrenequinone (at pH6)1 Publication
  23. KM=0.001 mM for 9,10-Phenanthrenequinone (at pH7.4)1 Publication
  24. KM=0.12 mM for Menadione (at pH6)1 Publication
  25. KM=0.27 mM for S---1-Phenyl-1-butanol (at pH7.4)1 Publication
  26. KM=0.034 mM for all-trans-Retinol (at pH7.4)1 Publication
  27. KM=0.33 mM for 3-Benzoylpyridine (at pH6)1 Publication
  28. KM=0.63 mM for 4-Benzoylpyridine (at pH6)1 Publication
  29. KM=1.55 mM for 4-Acetylpyridine (at pH6)1 Publication
  30. KM=1.8 mM for Pyridine-3-aldehyde (at pH6)1 Publication
  31. KM=0.9 mM for Pyridine-4-aldehyde (at pH6)1 Publication
  32. KM=0.59 mM for 4-Nitroacetophenone (at pH6)1 Publication
  33. KM=0.18 mM for Menadione (at pH6)1 Publication
  34. KM=0.028 mM for 5beta-Pregnane-3,20-dione (at pH7.4)1 Publication
  1. Vmax=48.7 µmol/min/mg enzyme with 16-Ketoestrone as substrate (at pH6)1 Publication
  2. Vmax=24.2 µmol/min/mg enzyme with 16-Ketoestrone as substrate (at pH7.4)1 Publication
  3. Vmax=2.54 µmol/min/mg enzyme with all-trans-Retinal as substrate (at pH7.4)1 Publication
  4. Vmax=6.34 µmol/min/mg enzyme with 9-cis-retinal as substrate (at pH7.4)1 Publication
  5. Vmax=83.6 µmol/min/mg enzyme with Isatin as substrate (at pH6)1 Publication
  6. Vmax=34.5 µmol/min/mg enzyme with Isatin as substrate (at pH7.4)1 Publication
  7. Vmax=1 µmol/min/mg enzyme with Propiophenone as substrate (at pH6)1 Publication
  8. Vmax=6.5 µmol/min/mg enzyme with Heptanophenone as substrate (at pH6)1 Publication
  9. Vmax=3.5 µmol/min/mg enzyme with Nonanophenoneas substrate (at pH6)1 Publication
  10. Vmax=55.7 µmol/min/mg enzyme with 4-Hexanoylpyridine as substrate (at pH6)1 Publication
  11. Vmax=5.8 µmol/min/mg enzyme with Hexanophenone as substrate (at pH6)1 Publication
  12. Vmax=5.8 µmol/min/mg enzyme with Valerophenone as substrate (at pH6)1 Publication
  13. Vmax=3.3 µmol/min/mg enzyme with n-Butyrophenone as substrate (at pH6)1 Publication
  14. Vmax=3.8 µmol/min/mg enzyme with 3-benzoylpyridine as substrate (at pH6)1 Publication
  15. Vmax=13.3 µmol/min/mg enzyme with 4-Benzoylpyridine as substrate (at pH6)1 Publication
  16. Vmax=115 µmol/min/mg enzyme with 2,3-Hexanedione as substrate (at pH6)1 Publication
  17. Vmax=115 µmol/min/mg enzyme with 1-phenyl-1,2-propanedione as substrate (at pH6)1 Publication
  18. Vmax=66.8 µmol/min/mg enzyme for the reduction of Benzil into S-benzoin (at pH6)1 Publication
  19. Vmax=110 µmol/min/mg enzyme with Diacetyl as substrate (at pH6)1 Publication
  20. Vmax=98.9 µmol/min/mg enzyme with Pyridine-4-aldehyde as substrate (at pH6)1 Publication
  21. Vmax=152 µmol/min/mg enzyme with 1-Phenylisatin as substrate (at pH6)1 Publication
  22. Vmax=121 µmol/min/mg enzyme with 9,10-Phenanthrenequinone as substrate (at pH6)1 Publication
  23. Vmax=78 µmol/min/mg enzyme with 9,10-Phenanthrenequinone as substrate (at pH7.4)1 Publication
  24. Vmax=2.6 µmol/min/mg enzyme with Menadione as substrate (at pH6)1 Publication
  25. Vmax=1.35 µmol/min/mg enzyme with S---1-Phenyl-1-butanol as substrate (at pH7.4)1 Publication
  26. Vmax=0.034 µmol/min/mg enzyme with all-trans-Retinol as substrate (at pH7.4)1 Publication
  27. Vmax=0.76 µmol/min/mg enzyme with 3-Benzoylpyridine as substrate (at pH6)1 Publication
  28. Vmax=2.98 µmol/min/mg enzyme with 4-Benzoylpyridine as substrate (at pH6)1 Publication
  29. Vmax=1.76 µmol/min/mg enzyme with 4-Acetylpyridine as substrate (at pH6)1 Publication
  30. Vmax=3.64 µmol/min/mg enzyme with Pyridine-3-aldehyde as substrate (at pH6)1 Publication
  31. Vmax=10.5 µmol/min/mg enzyme with Pyridine-4-aldehyde as substrate (at pH6)1 Publication
  32. Vmax=1.73 µmol/min/mg enzyme with 4-Nitroacetophenone as substrate (at pH6)1 Publication
  33. Vmax=2.47 µmol/min/mg enzyme with Menadione as substrate (at pH6)1 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 sitei151SubstrateBy similarity1
<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>Sitei158Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoinBy similarity1
Sitei161Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoinBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei164Proton acceptorPROSITE-ProRule annotation1
Binding sitei168NADPBy similarity1
Sitei177Important for the maintenance of the quaternary structure, the catalytic activity and cold stabilityBy 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 bindingi18 – 42NADPBy similarityAdd BLAST25

<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 functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.300, 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:
Dehydrogenase/reductase SDR family member 41 Publication (EC:1.1.1.1843 Publications, EC:1.1.1.3001 Publication)
Alternative name(s):
NADPH-dependent carbonyl reductase1 Publication
Short name:
CR1 Publication
Short name:
RACR1 Publication
NADPH-dependent retinol dehydrogenase/reductase1 Publication
Short name:
NDRD1 Publication
Peroxisomal short-chain alcohol dehydrogenase
Short name:
PSCD
Short chain dehydrogenase/reductase family 25C member 2By similarity
Short name:
Protein SDR25C2By similarity
rabNRDR
<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:DHRS4
<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

Keywords - Cellular componenti

Peroxisome

<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 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_0000054651‹1 – 260Dehydrogenase/reductase SDR family member 4Add BLAST›260

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 residuei74N6-acetyllysine; alternateBy similarity1
Modified residuei74N6-succinyllysine; alternateBy similarity1
Modified residuei198N6-acetyllysine; alternateBy similarity1
Modified residuei198N6-succinyllysine; alternateBy similarity1
Modified residuei202PhosphoserineBy similarity1
Modified residuei209N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in liver and kidney. Detected at lower levels in heart, lung, spleen, small intestine, testis, brain and stomach.1 Publication

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9986.ENSOCUP00000019647

<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		Q9GKX2

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

More...SMRi		Q9GKX2

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi258 – 260Peroxisomal targeting signalBy similarity3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions.By similarity
Three specific residues, Phe-158, Leu-161 and Asn-177 are conserved between non-primate mammals whereas the respective residues are serine, phenylalanine and threonine in primates (PubMed:19056333). The two residues at positions 158 and 161 are molecular determinants responsible for the stereoselective reduction of 3-ketosteroids and benzil (PubMed:19056333). The presence of an asparagine at position 177 is important for the maintenance of the quaternary structure resulting in stability at cold temperature and improved catalytic activity toward retinal (PubMed:19056333).1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0725, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9GKX2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029511, DHRS4-like
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam

The PANTHER Classification System

More...PANTHERi		PTHR43943:SF8, PTHR43943:SF8, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00081, GDHRDH
PR00080, SDRFAMILY

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735, SSF51735, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00061, ADH_SHORT, 1 hit

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

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

Q9GKX2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASSGVTRRD PLANKVAIVT ASTDGIGLAI ARRLAQDGAH VVISSRKQQN 
        60         70         80         90        100
VDRAVAALQA EGLSVTGTVC HVGKAEDRER LVATALNLHG GIDILVSNAA 
       110        120        130        140        150
VNPFFGKLMD VTEEVWDKIL DINVKAMALM TKAVVPEMEK RGGGSVVIVA 
       160        170        180        190        200
SIAAFNPFSG LGPYNVSKTA LVGLTKNLAL ELAAQNIRVN CLAPGLIKTS 
       210        220        230        240        250
FSKALWEDKA QEENIIQKLR IRRLGKPEEC AGIVSFLCSE DASYITGETV 
       260
VVAGGAPSRL
Length:260
Mass (Da):27,430
Last modified:March 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5B0585B58911B90C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

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
AB045133 mRNA Translation: BAB18777.1

<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
AB045133 mRNA Translation: BAB18777.1

3D structure databases

AlphaFoldDBiQ9GKX2
SMRiQ9GKX2
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019647

Phylogenomic databases

eggNOGiKOG0725, Eukaryota
InParanoidiQ9GKX2

Enzyme and pathway databases

BRENDAi1.1.1.300, 1749

Family and domain databases

InterProiView protein in InterPro
IPR029511, DHRS4-like
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam
PANTHERiPTHR43943:SF8, PTHR43943:SF8, 1 hit
PRINTSiPR00081, GDHRDH
PR00080, SDRFAMILY
SUPFAMiSSF51735, SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061, ADH_SHORT, 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 nameiDHRS4_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: Q9GKX2
<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: October 10, 2003
Last sequence update: March 1, 2001
Last modified: May 25, 2022
This is version 94 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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