UniProt Accession

 RDH11_HUMAN; Q8TC12; A6NDK3; A8K062; B2RB26; B4DDW0; Q6IAH5; Q9NRW0; Q9Y391 

Genbank Protein ID

 AF167438; AF395068; AF151840; CR457180; AK289427; AK293355; AK314465; AK074749; AL049779; CH471061; BC000112; BC011727; BC026274; BC037302; BC051291 

Genbank Nucleotide ID

 AAF89632.1; AAK72049.1; AAD34077.1; CAG33461.1; BAF82116.1; BAG56871.1; BAG37073.1; BAG51997.1; EAW80950.1; AAH00112.1; AAH11727.1; AAH26274.1; AAH37302.1; AAH51291.1 

Protein Name

 Retinol dehydrogenase 11 

Protein Synonyms/Alias

 Androgen-regulated short-chain dehydrogenase/reductase 1; HCV core-binding protein HCBP12; Prostate short-chain dehydrogenase/reductase 1; Retinal reductase 1; RalR1 

Gene Name

 RDH11 

Gene Synonyms/Alias

 ARSDR1; PSDR1; CGI-82 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
26	MAAPQIRKMLSSGVC	ubiquitination	[1, 2]
55	GANTGIGKETAKELA	ubiquitination	[2, 3]
77	LACRDVEKGELVAKE	ubiquitination	[2, 4]
83	EKGELVAKEIQTTTG	ubiquitination	[1, 2, 3, 5, 6]
98	NQQVLVRKLDLSDTK	ubiquitination	[2]
105	KLDLSDTKSIRAFAK	ubiquitination	[1, 2, 3, 5, 6, 7, 8, 9, 10]
112	KSIRAFAKGFLAEEK	acetylation	[11]
112	KSIRAFAKGFLAEEK	ubiquitination	[1, 2, 3, 5, 7, 8, 9]
194	FHNLQGEKFYNAGLA	ubiquitination	[1, 2]
206	GLAYCHSKLANILFT	ubiquitination	[2]
221	QELARRLKGSGVTTY	ubiquitination	[3]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [11] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. 

Sequence Annotation

 NP_BIND 48 54 NADP (By similarity).
 ACT_SITE 202 202 Proton acceptor (By similarity).
 BINDING 177 177 Substrate (By similarity).
 MOD_RES 112 112 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 318 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0001917; C:photoreceptor inner segment; IEA:Compara.
 GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:MGI.
 GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB.
 GO:0016062; P:adaptation of rhodopsin mediated signaling; IEA:Compara.
 GO:0007603; P:phototransduction, visible light; TAS:Reactome.
 GO:0042574; P:retinal metabolic process; IDA:MGI.
 GO:0042572; P:retinol metabolic process; ISS:UniProtKB. 

Interpro

 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00106; adh_short 

SMART

  

PROSITE

 PS00061; ADH_SHORT 

PRINTS

 PR00081; GDHRDH.
 PR00080; SDRFAMILY.