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Reviewed, UniProtKB/Swiss-Prot Q1XAA8 (AK1CN_HORSE)

Last modified June 16, 2009. Version 22. 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

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Names and origin

Protein namesRecommended name:
    Aldo-keto reductase family 1 member C23
    EC=1.1.1.-
Gene names
Name: AKR1C23
OrganismEquus caballus (Horse)
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

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Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

NADP-dependent oxidoreductase that has 20-alpha-hydroxysteroid dehydrogenase activity. Ref.1

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Detected in follicle granulosa cells (at protein level). Detected in heart, lung, liver, kidney, stomach, uterus, testis, skeletal muscle and granulosa cells of the follicle wall. Ref.1

Induction

Detected at low levels in preovulatory follicles. Up-regulated in preovulatory follicles during luteinization 12 to 36 hours after stimulation with human chorionic gonadotropin. Up-regulated in granulosa cells 12 to 39 hours after stimulation with human chorionic gonadotropin. Detected at low levels in corpora lutea. Detected at constant low levels in theca interna. Ref.1

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.12 µM for progesterone

Vmax=0.086 pmol/min/µg enzyme

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Ontologies

Keywords
   Biological processLipid metabolism
Steroid metabolism
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Aldo-keto reductase family 1 member C23
PRO_0000326224

Regions

Nucleotide binding13 – 2412NADP By similarity
Nucleotide binding166 – 1672NADP By similarity
Nucleotide binding216 – 2249NADP By similarity
Nucleotide binding269 – 27810NADP 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

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Sequences

Sequence LengthMass (Da)Tools
Q1XAA8-1 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: CF10B897919A662B

FASTA32236,672
        10         20         30         40         50         60 
MDPKGWRVEL NDGHFIHALG FGTYAPNEVP KSKAVEATKS AIDAGFRHID CAHLYDNEKE 

        70         80         90        100        110        120 
VGLAIRSKIQ DGTVKREDIF CTSKLWATSL RLQLVRPALE KSLKNLQLDY VDLYIIHFPV 

       130        140        150        160        170        180 
AVKPGEEHLP QDEQGRMIFD TVDLCATWEA MEKCKDAGLT KSIGVSNFNR RQLEMILNKP 

       190        200        210        220        230        240 
GLKHKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAYSALG SQREHWIDQS SPVLLEDPVL 

       250        260        270        280        290        300 
CAMAKKYKRT PALIALRYQL QRGVVVLAKS YNEKRIKENV QAFGFQLTSE DMKVLDGLNR 

       310        320 
NLRYVTLEMF AGHPEYPFSD DY

« Hide

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References

[1]"Human chorionic gonadotropin-dependent induction of an equine aldo-keto reductase (AKR1C23) with 20alpha-hydroxysteroid dehydrogenase activity during follicular luteinization in vivo."
Brown K.A., Boerboom D., Bouchard N., Dore M., Lussier J.G., Sirois J.
J. Mol. Endocrinol. 36:449-461(2006) [PubMed: 16720716] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Ovary.

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Cross-references

Sequence databases

AY955082 mRNA. Translation: AAY16444.1.
RefSeqNP_001075377.1.
UniGeneEca.12505

3D structure databases

SMRQ1XAA8. Positions 2-322.
ModBaseSearch...

Genome annotation databases

EnsemblENSECAG00000020877. Equus caballus. [Contig view]
GeneID100034073.
KEGGecb:100034073.

Phylogenomic databases

HOVERGENQ1XAA8.
OMAQ1XAA8. CALAKKQ.

Enzyme and pathway databases

BRENDA1.1.1.149. 1464.

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. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAK1CN_HORSE
AccessionPrimary (citable) accession number: Q1XAA8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 2, 2006
Last modified: June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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