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Protein

3-alpha-hydroxysteroid dehydrogenase

Gene

Akr1c9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionOxidoreductase
LigandNAD, 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-RKiP23457

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi708361 LOC191574

Subcellular locationi

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

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
OMAiYVHFPIS
OrthoDBiEOG091G0D69
PhylomeDBiP23457
TreeFamiTF106492

Family and domain databases

CDDicd06660 Aldo_ket_red, 1 hit
Gene3Di3.20.20.100, 1 hit
InterProiView protein in InterPro
IPR018170 Aldo/ket_reductase_CS
IPR020471 Aldo/keto_reductase
IPR023210 NADP_OxRdtase_dom
IPR036812 NADP_OxRdtase_dom_sf
PANTHERiPTHR11732 PTHR11732, 1 hit
PfamiView protein in Pfam
PF00248 Aldo_ket_red, 1 hit
PIRSFiPIRSF000097 AKR, 1 hit
PRINTSiPR00069 ALDKETRDTASE
SUPFAMiSSF51430 SSF51430, 1 hit
PROSITEiView protein in PROSITE
PS00798 ALDOKETO_REDUCTASE_1, 1 hit
PS00062 ALDOKETO_REDUCTASE_2, 1 hit
PS00063 ALDOKETO_REDUCTASE_3, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiDIDH_RAT
AccessioniPrimary (citable) accession number: P23457
Secondary accession number(s): Q5BKC8, Q6LDE6, Q6LDE7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: March 28, 2018
This is version 150 of the entry and version 1 of the sequence. See 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

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