Identification |
HMDB Protein ID
| HMDBP03004 |
Secondary Accession Numbers
| |
Name
| Retinol dehydrogenase 16 |
Synonyms
|
- Microsomal NAD+-dependent retinol dehydrogenase 4
- RoDH-4
- 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
|
- Endoplasmic reticulum membrane
- Microsome membrane
- Single-pass type IV membrane protein
- 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
|
|
Transmembrane Regions
|
|
Protein Sequence
|
>Retinol dehydrogenase 16
MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTA
PNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRRARGRVVNVSSVMGRVSLFGGGYCISK
YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGE
KFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTF
LVDAIMYWVSPSPAKAL
|
External Links |
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
| - 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 ]
- 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 ]
- 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 ]
- 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 ]
|