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Reviewed, UniProtKB/Swiss-Prot Q6AYQ2 (AK1CL_RAT)

Last modified June 16, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aldo-keto reductase family 1 member C21
    EC=1.1.1.-
Alternative name(s):
    17-alpha-hydroxysteroid dehydrogenase
      Short name=17-alpha-HSD
    3-alpha-hydroxysteroid dehydrogenase
Gene names
Name: Akr1c21
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into epitestosterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Biological processLipid metabolism
Steroid metabolism
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

steroid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Aldo-keto reductase family 1 member C21
PRO_0000326223

Regions

Nucleotide binding13 – 2412NADP By similarity
Nucleotide binding166 – 1672NADP By similarity
Nucleotide binding216 – 2249NADP By similarity
Nucleotide binding270 – 27910NADP By similarity

Sites

Active site551Proton donor By similarity
Binding site311Substrate By similarity
Binding site501NADP By similarity
Binding site1171Substrate By similarity
Site841Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue881Phosphothreonine By similarity
Modified residue891Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AYQ2-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 53909644919456D1

FASTA31836,135
        10         20         30         40         50         60 
MNSKCHCVKL NDGHFIPVLG FGTAMPSELP KSKAKEVTKI AIDAGFHHFD SAFVYNTEDH 

        70         80         90        100        110        120 
VGEAIREKIA NGTTRREDIF YTSKLWCTSL HPELVRSSLE CSLKKLQLDY VDLYLIHFPM 

       130        140        150        160        170        180 
ALKPGDENFP VDEHGKLLFD TVDLCATWEA MEKCKDAGLA KSIGVSNFNR RQLEKILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHLYLNQM KLLDFCKTNG IILVAYGVLG TQRYNGWVDQ NSPVLLNEPV 

       250        260        270        280        290        300 
LSSMAKKYNQ TPALIALRHQ LQRGIVVLNT SLKEERIKEN MKLSPEDMKV LDDLNRNLRY 

       310 
IAGGIFEGHP NFPFLDEY 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

BC078957 mRNA. Translation: AAH78957.1.
IPIIPI00555261.
RefSeqNP_001013075.1.
UniGeneRn.139229

3D structure databases

SMRQ6AYQ2. Positions 6-318.
ModBaseSearch...

PTM databases

PhosphoSiteQ6AYQ2.

Proteomic databases

PRIDEQ6AYQ2.

Genome annotation databases

EnsemblENSRNOG00000029844. Rattus norvegicus. [Contig view]
GeneID291283.
KEGGrno:291283.

Organism-specific databases

RGD1311841. Akr1c21.

Phylogenomic databases

HOVERGENQ6AYQ2.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. False negative.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio632346.

Entry information

Entry nameAK1CL_RAT
AccessionPrimary (citable) accession number: Q6AYQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 13, 2004
Last modified: June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents