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O75911 (DHRS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

Names and origin

Protein namesRecommended name:
Short-chain dehydrogenase/reductase 3

EC=1.1.1.300
Alternative name(s):
DD83.1
Retinal short-chain dehydrogenase/reductase 1
Short name=retSDR1
Gene names
Name:DHRS3
ORF Names:UNQ2424/PRO4983
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH. Ref.1

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Widely expressed with highest levels found in heart, placenta, lung, liver, kidney, pancreas, thyroid, testis, stomach, trachea and spinal cord. Lower levels found in skeletal muscle, intestine and lymph node. No expression detected in brain. In the retina, expressed in cone but not rod outer segments. Ref.1 Ref.9

Induction

By retinoic acid. Ref.9

Miscellaneous

Located in a region of chromosome 1 which is often deleted in aggressive neuroblastoma tumors.

Sequence similarities

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

Sequence caution

The sequence AAQ88460.1 differs from that shown. Reason: Frameshift at position 15.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75911-1)

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: O75911-2)

The sequence of this isoform differs from the canonical sequence as follows:
     115-167: GDITILVNNA...FLPRMLELQN → CSLGGSIPST...DSPMKLAPVT
     168-302: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Short-chain dehydrogenase/reductase 3
PRO_0000054644

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane195 – 21521Helical; Potential
Transmembrane253 – 27321Helical; Potential

Sites

Active site1881Proton acceptor By similarity
Binding site1751Substrate By similarity

Natural variations

Alternative sequence115 – 16753GDITI…LELQN → CSLGGSIPSTADHRLIPGKE NILMWPGRELCLWQNGFARG TFGDSPMKLAPVT in isoform 2.
VSP_013256
Alternative sequence168 – 302135Missing in isoform 2.
VSP_013257
Natural variant21V → A. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1128251 [ dbSNP | Ensembl ].
VAR_067443

Sequences

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

Last modified March 29, 2005. Version 2.
Checksum: 8FB4A735278E242E

FASTA30233,548
        10         20         30         40         50         60 
MVWKRLGALV MFPLQMIYLV VKAAVGLVLP AKLRDLSREN VLITGGGRGI GRQLAREFAE 

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

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

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

       250        260        270        280        290        300 
LKPETVARRT VEAVQLNQAL LLLPWTMHAL VILKSILPQA ALEEIHKFSG TYTCMNTFKG 


RT 

« Hide

Isoform 2 [UniParc].

Checksum: 803F9C15FF4F826F
Show »

FASTA16718,675

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), FUNCTION, TISSUE SPECIFICITY, VARIANT ALA-2.
Tissue: Retina.
[2]"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 [GENOMIC DNA], VARIANT ALA-2.
Tissue: Retina.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-2.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon endothelium.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Uterus.
[9]"retSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines."
Cerignoli F., Guo X., Cardinali B., Rinaldi C., Casaletto J., Frati L., Screpanti I., Gudas L.J., Gulino A., Thiele C.J., Giannini G.
Cancer Res. 62:1196-1204(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061741 mRNA. Translation: AAC63263.1.
AF179237 expand/collapse EMBL AC list , AF179234, AF179235, AF179236 Genomic DNA. Translation: AAD55402.1.
AY358093 mRNA. Translation: AAQ88460.1. Frameshift.
AK312961 mRNA. Translation: BAG35800.1.
BX648476 mRNA. Translation: CAI46033.1.
AL513016, AL645761 Genomic DNA. Translation: CAH74172.1.
AL645761, AL513016 Genomic DNA. Translation: CAI14999.1.
CH471130 Genomic DNA. Translation: EAW71743.1.
BC002730 mRNA. Translation: AAH02730.1.
RefSeqNP_004744.2. NM_004753.5.
UniGeneHs.289347.

3D structure databases

ProteinModelPortalO75911.
SMRO75911. Positions 32-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114675. 2 interactions.
IntActO75911. 1 interaction.
STRING9606.ENSP00000365397.

Chemistry

DrugBankDB00162. Vitamin A.

PTM databases

PhosphoSiteO75911.

Proteomic databases

PaxDbO75911.
PeptideAtlasO75911.
PRIDEO75911.

Protocols and materials databases

DNASU9249.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376223; ENSP00000365397; ENSG00000162496. [O75911-1]
GeneID9249.
KEGGhsa:9249.
UCSCuc001aub.3. human. [O75911-1]
uc001aud.4. human. [O75911-2]

Organism-specific databases

CTD9249.
GeneCardsGC01M012627.
HGNCHGNC:17693. DHRS3.
HPAHPA010844.
MIM612830. gene.
neXtProtNX_O75911.
PharmGKBPA134952810.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG051352.
InParanoidO75911.
KOK11146.
OMAWTMHALI.
OrthoDBEOG7Z3F50.
PhylomeDBO75911.
TreeFamTF312837.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000162496-MONOMER.
BRENDA1.1.1.105. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO75911.
BgeeO75911.
CleanExHS_DHRS3.
GenevestigatorO75911.

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.
ProtoNetSearch...

Other

GeneWikiDHRS3.
GenomeRNAi9249.
NextBio34675.
PROO75911.
SOURCESearch...

Entry information

Entry nameDHRS3_HUMAN
AccessionPrimary (citable) accession number: O75911
Secondary accession number(s): B2R7F3 expand/collapse secondary AC list , Q5VUY3, Q6UY38, Q9BUC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM