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Showing Protein Retinol dehydrogenase 16 (HMDBP03004)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP03004
Secondary Accession Numbers
  • 8526
Name Retinol dehydrogenase 16
Synonyms
  1. Microsomal NAD+-dependent retinol dehydrogenase 4
  2. RoDH-4
  3. Sterol/retinol dehydrogenase
Gene Name RDH16
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction
Pathways
  • Retinol Metabolism
  • Vitamin A Deficiency
Reactions Not Available
GO Classification
Function
binding
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Microsome membrane
  3. Single-pass type IV membrane protein
  4. Single-pass type IV membrane protein (Potential)
Gene Properties
Chromosome Location Chromosome:1
Locus 12q13.3
SNPs RDH16
Gene Sequence 
>954 bp
ATGTGGCTCTACCTGGCGGTTTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGCTGAGCCACCTGAGAGATAAGTATGTGTTCATCACGGGCTGTGACTCTGGC
TTCGGGAAACTGCTGGCCAGACAGCTGGATGCACGAGGCTTGCGGGTGCTGGCTGCATGT
CTGACGGAGAAAGGAGCCGAGCAGCTGAGGGGCCAGACTTCAGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGACAGAGAGCGTTGCTGCAGCCGCCCAGTGGGTGAAGGAGTGC
GTGAGAGACAAAGGACTCTGGGGCCTGGTGAATAATGCTGGCATCTCCTTGCCCACGGCT
CCCAATGAGTTGCTCACCAAGCAGGACTTCGTGACCATACTGGACGTGAACTTGTTGGGG
GTGATTGATGTGACTCTGAGCCTGCTGCCCTTAGTGAGGAAGGCCAGGGGCCGTGTGGTC
AACGTCTCCAGTGTCATGGGCCGGGTGTCACTTTTTGGTGGAGGCTACTGCATCTCCAAG
TATGGCGTGGAAGCCTTCTCTGACTCCCTCAGGAGGGAACTCTCCTACTTTGGGGTGAAG
GTGGCTATGATTGAACCTGGCTATTTCAAGACTGCTGTGACCAGTAAGGAGAGATTCTTA
AAGAGCTTCCTGGAGATTTGGGACCGGTCCAGTCCAGAGGTCAAGGAGGCCTATGGCGAG
AAGTTTGTTGCAGACTATAAGAAATCAGCTGAACAAATGGAGCAGAAGTGCACACAGGAT
CTGTCGTTGGTGACCAACTGCATGGAGCATGCGCTGATTGCCTGCCACCCCCGTACTCGC
TACTCAGCTGGCTGGGATGCCAAGCTTCTCTACCTCCCCATGAGCTACATGCCCACCTTC
CTGGTGGATGCCATTATGTACTGGGTCTCTCCAAGCCCGGCCAAGGCTCTATGA
Protein Properties
Number of Residues 317
Molecular Weight 35673.1
Theoretical pI 8.77
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 289-309
Protein Sequence 
>Retinol dehydrogenase 16
MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTA
PNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGGYCISK
YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGE
KFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTF
LVDAIMYWVSPSPAKAL
GenBank ID Protein 3372592
UniProtKB/Swiss-Prot ID O75452
UniProtKB/Swiss-Prot Entry Name RDH16_HUMAN
PDB IDs Not Available
GenBank Gene ID AF057034
GeneCard ID RDH16
GenAtlas ID RDH16
HGNC ID HGNC:29674
References
General References
  1. Gough WH, VanOoteghem S, Sint T, Kedishvili NY: cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids. J Biol Chem. 1998 Jul 31;273(31):19778-85. [PubMed:9677409 ]
  2. Jurukovski V, Markova NG, Karaman-Jurukovska N, Randolph RK, Su J, Napoli JL, Simon M: Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes. Mol Genet Metab. 1999 May;67(1):62-73. [PubMed:10329026 ]
  3. Cain JM, Zaino R, Shearer D, Bennett RA, Olt G, Weisz J: Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria. Am J Obstet Gynecol. 2002 Apr;186(4):675-83. [PubMed:11967490 ]
  4. Lapshina EA, Belyaeva OV, Chumakova OV, Kedishvili NY: Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4. Biochemistry. 2003 Jan 28;42(3):776-84. [PubMed:12534290 ]