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Protein

3-alpha-hydroxysteroid dehydrogenase

Gene

Akr1c9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Besides being a 3-alpha-hydroxysteroid dehydrogenase, the enzyme can accomplish diverse functions: as quinone reductase, as an aromatic alcohol dehydrogenase, as dihydrodiol dehydrogenase, and as 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase.

Catalytic activityi

A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.

Enzyme regulationi

Potently inhibited by the nonsteroidal anti-inflammatory drugs (NSAID).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50NADP1 Publication1
Active sitei55Proton donor1
Sitei84Lowers pKa of active site TyrBy similarity1
Binding sitei117Substrate1
Binding sitei190NADP1 Publication1
Binding sitei227Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 24NADP1 Publication5
Nucleotide bindingi166 – 167NADP1 Publication2
Nucleotide bindingi216 – 221NADP1 Publication6
Nucleotide bindingi270 – 280NADP1 PublicationAdd BLAST11

GO - Molecular functioni

  • androsterone dehydrogenase (B-specific) activity Source: UniProtKB-EC
  • steroid dehydrogenase activity Source: RGD

GO - Biological processi

  • hippocampus development Source: RGD
  • steroid metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14305.
BRENDAi1.1.1.213. 5301.
1.6.5.10. 5301.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
R-RNO-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-RNO-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
R-RNO-5365859. RA biosynthesis pathway.
R-RNO-975634. Retinoid metabolism and transport.
SABIO-RKP23457.

Names & Taxonomyi

Protein namesi
Recommended name:
3-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.50)
Short name:
3-alpha-HSD
Alternative name(s):
Hydroxyprostaglandin dehydrogenase
Gene namesi
Name:Akr1c9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi708361. LOC191574.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075221.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001246541 – 3223-alpha-hydroxysteroid dehydrogenaseAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Blocked amino end (Met)1

Proteomic databases

PaxDbiP23457.
PRIDEiP23457.

PTM databases

iPTMnetiP23457.
PhosphoSitePlusiP23457.

Expressioni

Tissue specificityi

In brain, highest levels found in olfactory bulb. Moderate levels present in cerebellum, cerebral cortex, hypothalamus and pituitary. Low levels present in amygdala, brain stem, caudate putamen, cingulate cortex, hippocampus, midbrain, and thalamus.1 Publication

Gene expression databases

BgeeiENSRNOG00000017672.
GenevisibleiP23457. RN.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

MINTiMINT-4567560.
STRINGi10116.ENSRNOP00000023835.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi7 – 9Combined sources3
Turni11 – 13Combined sources3
Beta strandi15 – 22Combined sources8
Turni28 – 30Combined sources3
Helixi33 – 43Combined sources11
Beta strandi48 – 50Combined sources3
Turni53 – 56Combined sources4
Helixi58 – 70Combined sources13
Helixi76 – 78Combined sources3
Beta strandi80 – 85Combined sources6
Helixi87 – 89Combined sources3
Helixi92 – 94Combined sources3
Helixi95 – 106Combined sources12
Beta strandi109 – 117Combined sources9
Beta strandi124 – 129Combined sources6
Beta strandi131 – 137Combined sources7
Helixi144 – 156Combined sources13
Beta strandi159 – 167Combined sources9
Helixi170 – 177Combined sources8
Beta strandi187 – 192Combined sources6
Helixi200 – 209Combined sources10
Beta strandi212 – 217Combined sources6
Turni225 – 227Combined sources3
Helixi235 – 237Combined sources3
Helixi239 – 247Combined sources9
Helixi252 – 262Combined sources11
Beta strandi266 – 269Combined sources4
Helixi274 – 280Combined sources7
Turni281 – 284Combined sources4
Helixi290 – 297Combined sources8
Helixi309 – 311Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFSX-ray2.50A/B1-322[»]
1LWIX-ray2.70A/B1-322[»]
1RALX-ray3.00A1-308[»]
ProteinModelPortaliP23457.
SMRiP23457.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23457.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP23457.
OMAiMLDYCKS.
OrthoDBiEOG091G0D69.
PhylomeDBiP23457.
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.

P23457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSISLRVAL NDGNFIPVLG FGTTVPEKVA KDEVIKATKI AIDNGFRHFD
60 70 80 90 100
SAYLYEVEEE VGQAIRSKIE DGTVKREDIF YTSKLWSTFH RPELVRTCLE
110 120 130 140 150
KTLKSTQLDY VDLYIIHFPM ALQPGDIFFP RDEHGKLLFE TVDICDTWEA
160 170 180 190 200
MEKCKDAGLA KSIGVSNFNC RQLERILNKP GLKYKPVCNQ VECHLYLNQS
210 220 230 240 250
KMLDYCKSKD IILVSYCTLG SSRDKTWVDQ KSPVLLDDPV LCAIAKKYKQ
260 270 280 290 300
TPALVALRYQ LQRGVVPLIR SFNAKRIKEL TQVFEFQLAS EDMKALDGLN
310 320
RNFRYNNAKY FDDHPNHPFT DE
Length:322
Mass (Da):37,028
Last modified:November 1, 1991 - v1
Checksum:i592EFC584726A4F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti108L → Q in AAB19918 (PubMed:1922097).Curated1
Sequence conflicti273 – 274NA → KP in AAB19918 (PubMed:1922097).Curated2
Sequence conflicti280L → P in AAB19918 (PubMed:1922097).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64393 mRNA. Translation: AAA40605.1.
M61937 mRNA. Translation: AAA41077.1.
D17310 mRNA. Translation: BAA04132.1.
S57790 mRNA. Translation: AAB19918.1.
AF180334
, AF180326, AF180327, AF180328, AF180329, AF180330, AF180331, AF180332, AF180333 Genomic DNA. Translation: AAF25813.1.
BC091123 mRNA. Translation: AAH91123.1.
S35751 mRNA. Translation: AAB21512.1.
S35752 mRNA. Translation: AAB21513.1.
PIRiA39350.
PC2175.
RefSeqiNP_612556.1. NM_138547.3.
UniGeneiRn.10021.
Rn.206655.

Genome annotation databases

EnsembliENSRNOT00000023835; ENSRNOP00000023835; ENSRNOG00000017672.
GeneIDi191574.
KEGGirno:191574.
UCSCiRGD:708361. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64393 mRNA. Translation: AAA40605.1.
M61937 mRNA. Translation: AAA41077.1.
D17310 mRNA. Translation: BAA04132.1.
S57790 mRNA. Translation: AAB19918.1.
AF180334
, AF180326, AF180327, AF180328, AF180329, AF180330, AF180331, AF180332, AF180333 Genomic DNA. Translation: AAF25813.1.
BC091123 mRNA. Translation: AAH91123.1.
S35751 mRNA. Translation: AAB21512.1.
S35752 mRNA. Translation: AAB21513.1.
PIRiA39350.
PC2175.
RefSeqiNP_612556.1. NM_138547.3.
UniGeneiRn.10021.
Rn.206655.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFSX-ray2.50A/B1-322[»]
1LWIX-ray2.70A/B1-322[»]
1RALX-ray3.00A1-308[»]
ProteinModelPortaliP23457.
SMRiP23457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4567560.
STRINGi10116.ENSRNOP00000023835.

Chemistry databases

ChEMBLiCHEMBL1075221.

PTM databases

iPTMnetiP23457.
PhosphoSitePlusiP23457.

Proteomic databases

PaxDbiP23457.
PRIDEiP23457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023835; ENSRNOP00000023835; ENSRNOG00000017672.
GeneIDi191574.
KEGGirno:191574.
UCSCiRGD:708361. rat.

Organism-specific databases

CTDi105387.
RGDi708361. LOC191574.

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP23457.
OMAiMLDYCKS.
OrthoDBiEOG091G0D69.
PhylomeDBiP23457.
TreeFamiTF106492.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14305.
BRENDAi1.1.1.213. 5301.
1.6.5.10. 5301.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
R-RNO-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-RNO-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
R-RNO-5365859. RA biosynthesis pathway.
R-RNO-975634. Retinoid metabolism and transport.
SABIO-RKP23457.

Miscellaneous databases

EvolutionaryTraceiP23457.
PROiP23457.

Gene expression databases

BgeeiENSRNOG00000017672.
GenevisibleiP23457. RN.

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 nameiDIDH_RAT
AccessioniPrimary (citable) accession number: P23457
Secondary accession number(s): Q5BKC8, Q6LDE6, Q6LDE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 143 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.