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Protein

Prostaglandin-E(2) 9-reductase

Gene

AKR1C5

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can convert prostaglandin E2 to prostaglandin F2-alpha.

Catalytic activityi

(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH.
17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate
Binding sitei50 – 501NADP1 Publication
Sitei54 – 541Required for substrate specificity
Active sitei55 – 551Proton donor
Sitei84 – 841Lowers pKa of active site TyrBy similarity
Binding sitei117 – 1171Substrate
Binding sitei190 – 1901NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 245NADPBy similarity
Nucleotide bindingi23 – 242NADP1 Publication
Nucleotide bindingi166 – 1672NADP1 Publication
Nucleotide bindingi216 – 2216NADP1 Publication
Nucleotide bindingi270 – 28011NADP1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin-E(2) 9-reductase (EC:1.1.1.189)
Alternative name(s):
20-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.149)
Short name:
20-alpha-HSD
Gene namesi
Name:AKR1C5
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541F → L: 49% reduction in 20alpha-HSD activity; little effect on 3-alpha-HSD. 1 Publication
Mutagenesisi54 – 541F → V: 73% reduction in 20alpha-HSD activity; little effect on 3-alpha-HSD. 1 Publication
Mutagenesisi306 – 3061V → F: Greatly reduced 3alpha-HSD activity toward DHT; little effect on 20alpha-HSD activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Prostaglandin-E(2) 9-reductasePRO_0000124651Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017578.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 93Combined sources
Beta strandi15 – 228Combined sources
Helixi31 – 4414Combined sources
Beta strandi48 – 503Combined sources
Helixi53 – 553Combined sources
Helixi58 – 7013Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 856Combined sources
Helixi87 – 893Combined sources
Helixi92 – 10615Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi133 – 1375Combined sources
Helixi144 – 15613Combined sources
Beta strandi159 – 1679Combined sources
Helixi170 – 1778Combined sources
Beta strandi188 – 1925Combined sources
Helixi200 – 2089Combined sources
Beta strandi212 – 2176Combined sources
Turni225 – 2273Combined sources
Helixi235 – 2373Combined sources
Helixi239 – 24810Combined sources
Helixi252 – 26110Combined sources
Turni262 – 2643Combined sources
Beta strandi266 – 2694Combined sources
Helixi274 – 2818Combined sources
Helixi282 – 2854Combined sources
Helixi290 – 2978Combined sources
Helixi309 – 3113Combined sources
Beta strandi318 – 3214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q13X-ray2.08A/B1-323[»]
1Q5MX-ray1.32A/B2-323[»]
ProteinModelPortaliP80508.
SMRiP80508. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80508.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP80508.
OMAiHQPVALM.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPKFQRVAL SDGHFIPVLG FGTYAPEEVP KSKAMEATKI AIDAGFRHID
60 70 80 90 100
SAYFYKNEKE VGLAIRSKIA DGTVKREDIF YTSKLWCTFH RPELVRPSLE
110 120 130 140 150
DSLKNLQLDY VDLYIIHFPT ALKPGVEIIP TDEHGKAIFD TVDICATWEA
160 170 180 190 200
MEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYLNQG
210 220 230 240 250
KLLEFCKSKG IVLVAYSALG SHREPEWVDQ SAPVLLEDPL IGALAKKHQQ
260 270 280 290 300
TPALIALRYQ LQRGIVVLAK SFTEKRIKEN IQVFEFQLPS EDMKVIDSLN
310 320
RNFRYVTADF AIGHPNYPFS DEY
Length:323
Mass (Da):36,670
Last modified:February 1, 1996 - v1
Checksum:i110ADD9FF56061B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17006 mRNA. Translation: AAA31155.1.
PIRiA45366.
RefSeqiNP_001075719.1. NM_001082250.1.
UniGeneiOcu.3559.

Genome annotation databases

EnsembliENSOCUT00000021813; ENSOCUP00000017578; ENSOCUG00000026267.
GeneIDi100009071.
KEGGiocu:100009071.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17006 mRNA. Translation: AAA31155.1.
PIRiA45366.
RefSeqiNP_001075719.1. NM_001082250.1.
UniGeneiOcu.3559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q13X-ray2.08A/B1-323[»]
1Q5MX-ray1.32A/B2-323[»]
ProteinModelPortaliP80508.
SMRiP80508. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000021813; ENSOCUP00000017578; ENSOCUG00000026267.
GeneIDi100009071.
KEGGiocu:100009071.

Organism-specific databases

CTDi100009071.

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP80508.
OMAiHQPVALM.
TreeFamiTF106492.

Miscellaneous databases

EvolutionaryTraceiP80508.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of an abundant rabbit ovarian protein with 20 alpha-hydroxysteroid dehydrogenase activity."
    Lacy W.R., Washenick K.J., Cook R.G., Dunbar B.S.
    Mol. Endocrinol. 7:58-66(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Ovary.
  2. "Prostaglandin-E2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20 alpha-hydroxysteroid dehydrogenase activity."
    Wintergalen N., Thole H.H., Galla H.-J., Schlegel W.
    Eur. J. Biochem. 234:264-270(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 134-170 AND 279-314.
    Tissue: Corpus luteum.
  3. "Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily."
    Couture J.-F., Legrand P., Cantin L., Labrie F., Luu-The V., Breton R.
    J. Mol. Biol. 339:89-102(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEX WITH NADPH; NADP AND TESTOSTERONE, MUTAGENESIS OF PHE-54 AND VAL-306.

Entry informationi

Entry nameiPE2R_RABIT
AccessioniPrimary (citable) accession number: P80508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 11, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.