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O88876 (DHRS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short-chain dehydrogenase/reductase 3
EC=1.1.1.300
Alternative name(s):
Retinal short-chain dehydrogenase/reductase 1
Short name=retSDR1
Gene names
Name:Dhrs3
Synonyms:Rsdr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH By similarity.

Catalytic activity

All-trans-retinol + NADP+ = all-trans-retinal + NADPH.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

In the embryo, expressed in developing osteogenic and chondrogenic tissues of vertebra, rib, tooth and limb bud. Ref.2

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNADP-retinol dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88876-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O88876-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     114-153: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Short-chain dehydrogenase/reductase 3
PRO_0000054645

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane195 – 21521Helical; Potential
Transmembrane258 – 27821Helical; Potential

Sites

Active site1881Proton acceptor By similarity
Binding site1751Substrate By similarity

Natural variations

Alternative sequence1 – 2626Missing in isoform 2.
VSP_050734
Alternative sequence114 – 15340Missing in isoform 2.
VSP_050735

Experimental info

Sequence conflict681L → F in AAH10972. Ref.5
Sequence conflict2341F → L Ref.1
Sequence conflict2341F → L Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: E530F36877C3C610

FASTA30233,652
        10         20         30         40         50         60 
MVWKWLGALV VFPLQMIYLV TKAAVGMVLP PKLRDLSRES VLITGGGRGI GRHLAREFAE 

        70         80         90        100        110        120 
RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQMAKAV REKVGDITIL 

       130        140        150        160        170        180 
VNNAAVVHGK SLMDSDDDAL LKSQHVNTLG QFWTTKAFLP RMLELQNGHI VCLNSVLALS 

       190        200        210        220        230        240 
AIPGAIDYCT SKASAFAFME SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP 

       250        260        270        280        290        300 
LKPETVARRT VDAVQQNQAL LLLPWTMNIL IILKSILPQA ALEEIHRFSG TYTCMNTFKG 


RT

« Hide

Isoform 2 [UniParc].

Checksum: 49DD2E6FC940669A
Show »

FASTA23626,431

References

« Hide 'large scale' references
[1]"Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal."
Haeseleer F., Huang J., Lebioda L., Saari J.C., Palczewski K.
J. Biol. Chem. 273:21790-21799(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[2]"Bmp-2 downstream targets in mesenchymal development identified by subtractive cloning from recombinant mesenchymal progenitors (C3H10T1/2)."
Baechner D., Ahrens M., Schroeder D., Hoffmann A., Lauber J., Betat N., Steinert P., Flohe L., Gross G.
Dev. Dyn. 213:398-411(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Mesenchymal cell.
[3]"Structure of retinal short-chain dehydrogenase/reductase retSDR1 gene."
Haeseleer F., Palczewski K.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
Tissue: Retina.
[4]"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. expand/collapse author list , 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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow and Mesonephros.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Colon, Kidney and Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF061743 mRNA. Translation: AAC63265.1.
X95281 mRNA. Translation: CAA64602.1.
AF179241 expand/collapse EMBL AC list , AF179238, AF179239, AF179240 Genomic DNA. Translation: AAD55403.1.
AK032958 mRNA. Translation: BAC28098.1.
AK151419 mRNA. Translation: BAE30384.1.
BC008980 mRNA. Translation: AAH08980.1.
BC010972 mRNA. Translation: AAH10972.1.
BC013540 mRNA. Translation: AAH13540.1.
IPIIPI00122691.
IPI00128328.
RefSeqNP_001165895.1. NM_001172424.1.
NP_035433.1. NM_011303.6.
UniGeneMm.14063.

3D structure databases

ProteinModelPortalO88876.
SMRO88876. Positions 34-290.
ModBaseSearch...

PTM databases

PhosphoSiteO88876.

Proteomic databases

PaxDbO88876.
PRIDEO88876.

Protocols and materials databases

DNASU20148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105744; ENSMUSP00000101370; ENSMUSG00000066026.
ENSMUST00000154208; ENSMUSP00000122552; ENSMUSG00000066026.
GeneID20148.
KEGGmmu:20148.
UCSCuc008vrn.2. mouse.

Organism-specific databases

CTD9249.
MGIMGI:1315215. Dhrs3.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00540000069900.
HOVERGENHBG051352.
InParanoidO88876.
KOK11146.
OMAIHRFSGT.

Gene expression databases

ArrayExpressO88876.
BgeeO88876.
CleanExMM_DHRS3.
GenevestigatorO88876.
GermOnlineENSMUSG00000066026. Mus musculus.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio297657.
SOURCESearch...

Entry information

Entry nameDHRS3_MOUSE
AccessionPrimary (citable) accession number: O88876
Secondary accession number(s): Q3UAD1 expand/collapse secondary AC list , Q91WR0, Q91XC3, Q922A6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 29, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents