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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)DescriptionActionsGraphical viewLength
Binding sitei24Substrate1
Binding sitei50NADP1 Publication1
Sitei54Required for substrate specificity1
Active sitei55Proton donor1
Sitei84Lowers pKa of active site TyrBy similarity1
Binding sitei117Substrate1
Binding sitei190NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 24NADPBy similarity5
Nucleotide bindingi23 – 24NADP1 Publication2
Nucleotide bindingi166 – 167NADP1 Publication2
Nucleotide bindingi216 – 221NADP1 Publication6
Nucleotide bindingi270 – 280NADP1 PublicationAdd BLAST11

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)DescriptionActionsGraphical viewLength
Mutagenesisi54F → L: 49% reduction in 20alpha-HSD activity; little effect on 3-alpha-HSD. 1 Publication1
Mutagenesisi54F → V: 73% reduction in 20alpha-HSD activity; little effect on 3-alpha-HSD. 1 Publication1
Mutagenesisi306V → F: Greatly reduced 3alpha-HSD activity toward DHT; little effect on 20alpha-HSD activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246511 – 323Prostaglandin-E(2) 9-reductaseAdd BLAST323

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017578.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi7 – 9Combined sources3
Beta strandi15 – 22Combined sources8
Helixi31 – 44Combined sources14
Beta strandi48 – 50Combined sources3
Helixi53 – 55Combined sources3
Helixi58 – 70Combined sources13
Helixi76 – 78Combined sources3
Beta strandi80 – 85Combined sources6
Helixi87 – 89Combined sources3
Helixi92 – 106Combined sources15
Beta strandi111 – 117Combined sources7
Beta strandi133 – 137Combined sources5
Helixi144 – 156Combined sources13
Beta strandi159 – 167Combined sources9
Helixi170 – 177Combined sources8
Beta strandi188 – 192Combined sources5
Helixi200 – 208Combined sources9
Beta strandi212 – 217Combined sources6
Turni225 – 227Combined sources3
Helixi235 – 237Combined sources3
Helixi239 – 248Combined sources10
Helixi252 – 261Combined sources10
Turni262 – 264Combined sources3
Beta strandi266 – 269Combined sources4
Helixi274 – 281Combined sources8
Helixi282 – 285Combined sources4
Helixi290 – 297Combined sources8
Helixi309 – 311Combined sources3
Beta strandi318 – 321Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q13X-ray2.08A/B1-323[»]
1Q5MX-ray1.32A/B2-323[»]
ProteinModelPortaliP80508.
SMRiP80508.
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.
OMAiRKNQSAY.
OrthoDBiEOG091G0D69.
TreeFamiTF106492.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q13X-ray2.08A/B1-323[»]
1Q5MX-ray1.32A/B2-323[»]
ProteinModelPortaliP80508.
SMRiP80508.
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.
OMAiRKNQSAY.
OrthoDBiEOG091G0D69.
TreeFamiTF106492.

Miscellaneous databases

EvolutionaryTraceiP80508.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
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...

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 2, 2016
This is version 105 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.