O75911 (DHRS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	DHRS3
ORF Names:	UNQ2424/PRO4983

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	retinol metabolic process Traceable author statement Ref.1. Source: UniProtKB visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	NADP-retinol dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Traceable author statement Ref.1. Source: UniProtKB nucleotide binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Short-chain dehydrogenase/reductase 3		PRO_0000054644
Regions
	Transmembrane	9 – 29	21	Helical; Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Transmembrane	195 – 215	21	Helical; Potential
	Transmembrane	253 – 273	21	Helical; Potential
Sites
	Active site	188	1	Proton acceptor By similarity
	Binding site	175	1	Substrate By similarity
Natural variations
	Alternative sequence	115 – 167	53	GDITI…LELQN → CSLGGSIPSTADHRLIPGKE NILMWPGRELCLWQNGFARG TFGDSPMKLAPVT in isoform 2.		VSP_013256
	Alternative sequence	168 – 302	135	Missing in isoform 2.		VSP_013257
	Natural variant	2	1	V → A. Ref.1 Ref.2 Ref.4 Corresponds to variant rs1128251 [ dbSNP | Ensembl ].		VAR_067443

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 8FB4A735278E242E	FASTA	302	33,548
	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
	Isoform 2 [UniParc]. Checksum: 803F9C15FF4F826F	FASTA	167	18,675
	10 20 30 40 50 60 MVWKRLGALV MFPLQMIYLV VKAAVGLVLP AKLRDLSREN VLITGGGRGI GRQLAREFAE 70 80 90 100 110 120 RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQTAKAV REKVCSLGGS 130 140 150 160 IPSTADHRLI PGKENILMWP GRELCLWQNG FARGTFGDSP MKLAPVT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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 , 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.
IPI	IPI00006250. IPI00432717.
RefSeq	NP_004744.2. NM_004753.4.
UniGene	Hs.289347.
3D structure databases
ProteinModelPortal	O75911.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75911. 1 interaction.
STRING	9606.ENSP00000365397.
PTM databases
PhosphoSite	O75911.
Proteomic databases
PaxDb	O75911.
PeptideAtlas	O75911.
PRIDE	O75911.
Protocols and materials databases
DNASU	9249.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376223; ENSP00000365397; ENSG00000162496.
GeneID	9249.
KEGG	hsa:9249.
UCSC	uc001aub.3. human. uc001aud.4. human.
Organism-specific databases
CTD	9249.
GeneCards	GC01M012627.
HGNC	HGNC:17693. DHRS3.
HPA	HPA010844.
MIM	612830. gene.
neXtProt	NX_O75911.
PharmGKB	PA134952810.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG051352.
InParanoid	O75911.
KO	K11146.
OMA	IHRFSGT.
OrthoDB	EOG4GQQ5C.
PhylomeDB	O75911.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000162496-MONOMER.
BRENDA	1.1.1.105. 2681.
Gene expression databases
ArrayExpress	O75911.
Bgee	O75911.
CleanEx	HS_DHRS3.
Genevestigator	O75911.
GermOnline	ENSG00000162496. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PIRSF	PIRSF000126. 11-beta-HSD1. 1 hit.
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00162. Vitamin A.
GenomeRNAi	9249.
NextBio	34675.
SOURCE	Search...

Entry information

Entry name

DHRS3_HUMAN

Accession

Primary (citable) accession number: O75911
Secondary accession number(s): B2R7F3 , Q5VUY3, Q6UY38, Q9BUC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.