CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014669
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 All-trans-retinol 13,14-reductase 
Protein Synonyms/Alias
 All-trans-13,14-dihydroretinol saturase; RetSat; PPAR-alpha-regulated and starvation-induced gene protein 
Gene Name
 Retsat 
Gene Synonyms/Alias
 Ppsig 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
47PEPLVTDKEARKKVLubiquitination[1]
55EARKKVLKQAFSVSRphosphoglycerylation[2]
55EARKKVLKQAFSVSRubiquitination[1]
87ASAAVLAKAGKRVLVubiquitination[1]
164LEGPNGRKEFPMYSGubiquitination[1]
173FPMYSGRKEYIQGLKubiquitination[1]
180KEYIQGLKKKFPKEEubiquitination[1]
192KEEAVIDKYMELVKVubiquitination[1]
429YVSMPKEKAPEHIPLubiquitination[1]
601DLQALGSKVKAQKKKubiquitination[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] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
 Retinol saturase carrying out the saturation of the 13- 14 double bond of all-trans-retinol to produce all-trans-13,14- dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A. 
Sequence Annotation
 NP_BIND 69 97 FAD or NAD or NADP (Potential).  
Keyword
 Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 609 AA 
Protein Sequence
MWITALLLAV LLLVILHRVY VGLYAASSPN PFAEDVKRPP EPLVTDKEAR KKVLKQAFSV 60
SRVPEKLDAV VIGSGIGGLA SAAVLAKAGK RVLVLEQHTK AGGCCHTFGE NGLEFDTGIH 120
YIGRMREGNI GRFILDQITE GQLDWAPMAS PFDLMILEGP NGRKEFPMYS GRKEYIQGLK 180
KKFPKEEAVI DKYMELVKVV ARGVSHAVLL KFLPLPLTQL LSKFGLLTRF SPFCRASTQS 240
LAEVLQQLGA SRELQAVLSY IFPTYGVTPS HTAFSLHALL VDHYIQGAYY PRGGSSEIAF 300
HTIPLIQRAG GAVLTRATVQ SVLLDSAGRA CGVSVKKGQE LVNIYCPVVI SNAGMFNTYQ 360
HLLPETVRHL PDVKKQLAMV RPGLSMLSIF ICLKGTKEDL KLQSTNYYVY FDTDMDKAME 420
RYVSMPKEKA PEHIPLLFIA FPSSKDPTWE ERFPDRSTMT ALVPMAFEWF EEWQEEPKGK 480
RGVDYETLKN AFVEASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAPR GATYGADHDL 540
ARLHPHAMAS IRAQTPIPNL YLTGQDIFTC GLMGALQGAL LCSSAILKRN LYSDLQALGS 600
KVKAQKKKM 609 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC.
 GO:0005640; C:nuclear outer membrane; IDA:HGNC.
 GO:0051786; F:all-trans-retinol 13,14-reductase activity; IDA:HGNC.
 GO:0042572; P:retinol metabolic process; IDA:HGNC. 
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