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Protein

Short-chain dehydrogenase/reductase 3

Gene

DHRS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751SubstrateBy similarity
Active sitei188 – 1881Proton acceptorBy similarity

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. NADP-retinol dehydrogenase activity Source: UniProtKB-EC
  3. nucleotide binding Source: ProtInc
  4. retinol dehydrogenase activity Source: Ensembl

GO - Biological processi

  1. bone morphogenesis Source: Ensembl
  2. cardiac septum morphogenesis Source: Ensembl
  3. negative regulation of retinoic acid receptor signaling pathway Source: Ensembl
  4. outflow tract morphogenesis Source: Ensembl
  5. palate development Source: Ensembl
  6. phototransduction, visible light Source: Reactome
  7. regulation of ossification Source: Ensembl
  8. retinoid metabolic process Source: Reactome
  9. retinol metabolic process Source: UniProtKB
  10. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000162496-MONOMER.
BRENDAi1.1.1.300. 2681.
ReactomeiREACT_160083. The retinoid cycle in cones (daylight vision).
REACT_268561. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended 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
Retinol dehydrogenase 17
Short chain dehydrogenase/reductase family 16C member 1
Gene namesi
Name:DHRS3
Synonyms:RDH17, SDR16C1
ORF Names:UNQ2424/PRO4983
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17693. DHRS3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Transmembranei195 – 21521HelicalSequence AnalysisAdd
BLAST
Transmembranei253 – 27321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. photoreceptor outer segment membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134952810.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Short-chain dehydrogenase/reductase 3PRO_0000054644Add
BLAST

Proteomic databases

MaxQBiO75911.
PaxDbiO75911.
PeptideAtlasiO75911.
PRIDEiO75911.

PTM databases

PhosphoSiteiO75911.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

By retinoic acid.1 Publication

Gene expression databases

BgeeiO75911.
CleanExiHS_DHRS3.
ExpressionAtlasiO75911. baseline and differential.
GenevestigatoriO75911.

Organism-specific databases

HPAiHPA010844.

Interactioni

Protein-protein interaction databases

BioGridi114675. 2 interactions.
IntActiO75911. 1 interaction.
STRINGi9606.ENSP00000365397.

Structurei

3D structure databases

ProteinModelPortaliO75911.
SMRiO75911. Positions 32-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00540000069900.
HOVERGENiHBG051352.
InParanoidiO75911.
KOiK11146.
OMAiWTMHALI.
OrthoDBiEOG7Z3F50.
PhylomeDBiO75911.
TreeFamiTF312837.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75911-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVWKRLGALV MFPLQMIYLV VKAAVGLVLP AKLRDLSREN VLITGGGRGI
60 70 80 90 100
GRQLAREFAE RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR
110 120 130 140 150
EEVYQTAKAV REKVGDITIL VNNAAVVHGK SLMDSDDDAL LKSQHINTLG
160 170 180 190 200
QFWTTKAFLP RMLELQNGHI VCLNSVLALS AIPGAIDYCT SKASAFAFME
210 220 230 240 250
SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP LKPETVARRT
260 270 280 290 300
VEAVQLNQAL LLLPWTMHAL VILKSILPQA ALEEIHKFSG TYTCMNTFKG

RT
Length:302
Mass (Da):33,548
Last modified:March 29, 2005 - v2
Checksum:i8FB4A735278E242E
GO
Isoform 2 (identifier: O75911-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:167
Mass (Da):18,675
Checksum:i803F9C15FF4F826F
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21V → A.3 Publications
Corresponds to variant rs1128251 [ dbSNP | Ensembl ].
VAR_067443

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei115 – 16753GDITI…LELQN → CSLGGSIPSTADHRLIPGKE NILMWPGRELCLWQNGFARG TFGDSPMKLAPVT in isoform 2. 1 PublicationVSP_013256Add
BLAST
Alternative sequencei168 – 302135Missing in isoform 2. 1 PublicationVSP_013257Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061741 mRNA. Translation: AAC63263.1.
AF179237
, 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.
CCDSiCCDS146.1. [O75911-1]
RefSeqiNP_004744.2. NM_004753.6. [O75911-1]
UniGeneiHs.289347.

Genome annotation databases

EnsembliENST00000616661; ENSP00000480439; ENSG00000162496. [O75911-1]
GeneIDi9249.
KEGGihsa:9249.
UCSCiuc001aub.3. human. [O75911-1]
uc001aud.4. human. [O75911-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061741 mRNA. Translation: AAC63263.1.
AF179237
, 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.
CCDSiCCDS146.1. [O75911-1]
RefSeqiNP_004744.2. NM_004753.6. [O75911-1]
UniGeneiHs.289347.

3D structure databases

ProteinModelPortaliO75911.
SMRiO75911. Positions 32-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114675. 2 interactions.
IntActiO75911. 1 interaction.
STRINGi9606.ENSP00000365397.

Chemistry

DrugBankiDB00162. Vitamin A.

PTM databases

PhosphoSiteiO75911.

Proteomic databases

MaxQBiO75911.
PaxDbiO75911.
PeptideAtlasiO75911.
PRIDEiO75911.

Protocols and materials databases

DNASUi9249.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000616661; ENSP00000480439; ENSG00000162496. [O75911-1]
GeneIDi9249.
KEGGihsa:9249.
UCSCiuc001aub.3. human. [O75911-1]
uc001aud.4. human. [O75911-2]

Organism-specific databases

CTDi9249.
GeneCardsiGC01M012627.
HGNCiHGNC:17693. DHRS3.
HPAiHPA010844.
MIMi612830. gene.
neXtProtiNX_O75911.
PharmGKBiPA134952810.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00540000069900.
HOVERGENiHBG051352.
InParanoidiO75911.
KOiK11146.
OMAiWTMHALI.
OrthoDBiEOG7Z3F50.
PhylomeDBiO75911.
TreeFamiTF312837.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000162496-MONOMER.
BRENDAi1.1.1.300. 2681.
ReactomeiREACT_160083. The retinoid cycle in cones (daylight vision).
REACT_268561. RA biosynthesis pathway.

Miscellaneous databases

GeneWikiiDHRS3.
GenomeRNAii9249.
NextBioi34675.
PROiO75911.
SOURCEiSearch...

Gene expression databases

BgeeiO75911.
CleanExiHS_DHRS3.
ExpressionAtlasiO75911. baseline and differential.
GenevestigatoriO75911.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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 (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-2.
    Tissue: Retina.
  3. 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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-2.
  5. 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.
    , 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2003) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHRS3_HUMAN
AccessioniPrimary (citable) accession number: O75911
Secondary accession number(s): B2R7F3
, Q5VUY3, Q6UY38, Q9BUC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 29, 2005
Last modified: April 1, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.