UniProt Accession

 AL1A1_MOUSE; P24549; Q7TQJ0; Q811J0 

Genbank Protein ID

 M74570; M74571; S75713; S77047; BC044729; BC054386 

Genbank Nucleotide ID

 AAA37202.1; AAA37203.1; AAB32754.2; AAH44729.1; AAH54386.1 

Protein Name

 Retinal dehydrogenase 1 

Protein Synonyms/Alias

 RALDH 1; RalDH1; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic 

Gene Name

 Aldh1a1 

Gene Synonyms/Alias

 Ahd-2; Ahd2; Aldh1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
17	PAPLADLKIQHTKIF	ubiquitination	[1]
22	DLKIQHTKIFINNEW	ubiquitination	[1]
36	WHNSVSGKKFPVLNP	ubiquitination	[1]
57	CHVEEGDKADVDKAV	acetylation	[2]
62	GDKADVDKAVKAARQ	ubiquitination	[1]
91	ERGRLLNKLADLMER	ubiquitination	[1]
128	SDLGGCIKALKYCAG	ubiquitination	[1]
131	GGCIKALKYCAGWAD	ubiquitination	[1]
139	YCAGWADKIHGQTIP	ubiquitination	[1]
193	CGNTVVVKPAEQTPL	ubiquitination	[1]
252	TGSTQVGKLIKEAAG	ubiquitination	[1]
255	TQVGKLIKEAAGKSN	ubiquitination	[1]
321	SVYDEFVKRSVERAK	ubiquitination	[1]
329	RSVERAKKYVLGNPL	ubiquitination	[1]
348	NQGPQIDKEQHDKIL	acetylation	[2]
348	NQGPQIDKEQHDKIL	ubiquitination	[1]
353	IDKEQHDKILDLIES	ubiquitination	[1]
362	LDLIESGKKEGAKLE	acetylation	[3]
362	LDLIESGKKEGAKLE	succinylation	[3]
362	LDLIESGKKEGAKLE	ubiquitination	[1]
363	DLIESGKKEGAKLEC	ubiquitination	[1]
367	SGKKEGAKLECGGGR	acetylation	[2]
378	GGGRWGNKGFFVQPT	ubiquitination	[1]
398	TDEMRIAKEEIFGPV	ubiquitination	[1]
410	GPVQQIMKFKSVDDV	acetylation	[4]
410	GPVQQIMKFKSVDDV	ubiquitination	[1]
412	VQQIMKFKSVDDVIK	acetylation	[2, 3, 4, 5]
412	VQQIMKFKSVDDVIK	succinylation	[3]
412	VQQIMKFKSVDDVIK	ubiquitination	[1]
419	KSVDDVIKRANNTTY	acetylation	[2, 4, 5, 6]
419	KSVDDVIKRANNTTY	ubiquitination	[1]
435	LAAGLFTKDLDKAIT	ubiquitination	[1]
490	LYEYTELKTVAMKIS	ubiquitination	[1]
495	ELKTVAMKISQKNS*	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599] 

Functional Description

 In addition to the activity on acetaldehyde and related substrates, is also involved in the oxidation of aldehydes derived from biogenic amines such as epinephrine and norepinephrine, as well as the aldehydes generated via lipid peroxidation. Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity). 

Sequence Annotation

 NP_BIND 246 251 NAD (By similarity).
 REGION 300 305 Antabuse binding.
 ACT_SITE 269 269 Proton acceptor (By similarity).
 ACT_SITE 303 303 Nucleophile (By similarity).
 BINDING 456 456 NAD (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 91 91 N6-acetyllysine (By similarity).
 MOD_RES 128 128 N6-acetyllysine (By similarity).
 MOD_RES 252 252 N6-acetyllysine (By similarity).
 MOD_RES 353 353 N6-acetyllysine (By similarity).
 MOD_RES 367 367 N6-acetyllysine (By similarity).
 MOD_RES 410 410 N6-acetyllysine (By similarity).
 MOD_RES 419 419 N6-acetyllysine (By similarity).
 MOD_RES 435 435 N6-acetyllysine (By similarity).
 MOD_RES 495 495 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 501 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI.
 GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:Compara.
 GO:0001758; F:retinal dehydrogenase activity; IEA:EC.
 GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI.
 GO:0060206; P:estrous cycle phase; IEA:Compara.
 GO:0001822; P:kidney development; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0007494; P:midgut development; IEA:Compara.
 GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IGI:MGI.
 GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0042493; P:response to drug; IDA:MGI.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IEA:Compara.
 GO:0032526; P:response to retinoic acid; IEA:Compara.
 GO:0042572; P:retinol metabolic process; IMP:MGI. 

Interpro

 IPR016161; Ald_DH/histidinol_DH.
 IPR016163; Ald_DH_C.
 IPR016160; Ald_DH_CS.
 IPR016162; Ald_DH_N.
 IPR015590; Aldehyde_DH_dom. 

Pfam

 PF00171; Aldedh 

SMART

  

PROSITE

 PS00070; ALDEHYDE_DEHYDR_CYS
 PS00687; ALDEHYDE_DEHYDR_GLU 

PRINTS