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Protein

Dehydrogenase/reductase SDR family member 9

Gene

Dhrs9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831NADBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Active sitei176 – 1761Proton acceptorBy similarity
Binding sitei180 – 1801NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 5825NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrogenase/reductase SDR family member 9 (EC:1.1.-.-)
Alternative name(s):
3-alpha hydroxysteroid dehydrogenase
Short name:
3-alpha-HSD
Short-chain dehydrogenase/reductase retSDR8
Gene namesi
Name:Dhrs9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2442798. Dhrs9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 319299Dehydrogenase/reductase SDR family member 9PRO_0000042618Add
BLAST

Proteomic databases

PaxDbiQ58NB6.
PRIDEiQ58NB6.

PTM databases

PhosphoSiteiQ58NB6.

Expressioni

Gene expression databases

BgeeiQ58NB6.
CleanExiMM_DHRS9.
ExpressionAtlasiQ58NB6. baseline and differential.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ58NB6. 1 interaction.
MINTiMINT-4110286.
STRINGi10090.ENSMUSP00000069631.

Structurei

3D structure databases

ProteinModelPortaliQ58NB6.
SMRiQ58NB6. Positions 28-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00840000129713.
HOVERGENiHBG005482.
InParanoidiQ58NB6.
KOiK11149.
OMAiIMGPSAP.
OrthoDBiEOG7FXZZX.
PhylomeDBiQ58NB6.
TreeFamiTF325617.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 1 hit.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q58NB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFWLLALLF LCAFLWNYKG QLKIADIADK YVFITGCDTG FGNLAARTFD
60 70 80 90 100
KKGFRVIAAC LTESGSAALK AKTSERLHTV LLDVTDPENV KKTAQWVKSH
110 120 130 140 150
VGEKGLWGLI NNAGVLGVLA PTDWLTVDDY REPIEVNLFG LINVTLNMLP
160 170 180 190 200
LVKKARGRVI NVSSIGGRLA FGGGGYTPSK YAVEGFNDSL RRDMKAFGVH
210 220 230 240 250
VSCIEPGLFK TELADPIKTT EKKLAIWKHL SPDIKQQYGE GYIEKSLHRL
260 270 280 290 300
KSNTSSVNLD LSLVVGCMDH ALTSLFPKTR YIAGKDAKTF WIPLSHMPAV
310
LQDFLLLKQK VELANPKAV
Length:319
Mass (Da):35,242
Last modified:October 25, 2005 - v2
Checksum:iA8111F84ED57BB19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 53FWL → LWV in AAX33670 (Ref. 2) Curated
Sequence conflicti292 – 2921I → L in AAX33670 (Ref. 2) Curated
Sequence conflicti317 – 3171K → Q in AAX33670 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361479 mRNA. Translation: AAN75755.1.
AK050180 mRNA. Translation: BAC34110.1.
AK080914 mRNA. Translation: BAC38075.1.
AY936479 mRNA. Translation: AAX33670.1.
CCDSiCCDS16091.1.
RefSeqiNP_780721.1. NM_175512.2.
UniGeneiMm.211655.

Genome annotation databases

EnsembliENSMUST00000063690; ENSMUSP00000069631; ENSMUSG00000027068.
GeneIDi241452.
KEGGimmu:241452.
UCSCiuc008jyb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361479 mRNA. Translation: AAN75755.1.
AK050180 mRNA. Translation: BAC34110.1.
AK080914 mRNA. Translation: BAC38075.1.
AY936479 mRNA. Translation: AAX33670.1.
CCDSiCCDS16091.1.
RefSeqiNP_780721.1. NM_175512.2.
UniGeneiMm.211655.

3D structure databases

ProteinModelPortaliQ58NB6.
SMRiQ58NB6. Positions 28-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ58NB6. 1 interaction.
MINTiMINT-4110286.
STRINGi10090.ENSMUSP00000069631.

PTM databases

PhosphoSiteiQ58NB6.

Proteomic databases

PaxDbiQ58NB6.
PRIDEiQ58NB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063690; ENSMUSP00000069631; ENSMUSG00000027068.
GeneIDi241452.
KEGGimmu:241452.
UCSCiuc008jyb.1. mouse.

Organism-specific databases

CTDi10170.
MGIiMGI:2442798. Dhrs9.

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00840000129713.
HOVERGENiHBG005482.
InParanoidiQ58NB6.
KOiK11149.
OMAiIMGPSAP.
OrthoDBiEOG7FXZZX.
PhylomeDBiQ58NB6.
TreeFamiTF325617.

Enzyme and pathway databases

ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Miscellaneous databases

PROiQ58NB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ58NB6.
CleanExiMM_DHRS9.
ExpressionAtlasiQ58NB6. baseline and differential.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 1 hit.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Short-chain dehydrogenases/reductases in retina."
    Haeseleer F., Palczewski K.
    Methods Enzymol. 316:372-383(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Eye.
  2. "Mouse homolog of rat epithelial retinol dehydrogenase."
    Plumley H.C., Rexer B.N., Li X.-H., Ong D.E.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Uterus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Adipose tissue and Liver.

Entry informationi

Entry nameiDHRS9_MOUSE
AccessioniPrimary (citable) accession number: Q58NB6
Secondary accession number(s): Q8BGC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: June 8, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.