Overview
| Uniprot ID | P47895 |
|---|
| Protein Name | Retinaldehyde dehydrogenase 3 |
|---|
| Gene Name | ALDH1A3 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 373 |
LELIESGKKEGAKLE |
| 374 |
ELIESGKKEGAKLEC |
Function
Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (By similarity) (PubMed:27759097). High specificity for all-trans-retinal as substrate, can also accept acetaldehyde as substrate in vitro but with lower affinity (PubMed:27759097). Required for the biosynthesis of normal levels of retinoate in the embryonic ocular and nasal regions; a critical lipid in the embryonic development of the eye and the nasal region (By similarity)
Protein Sequence
10
MATANGAVEN
20
GQPDRKPPAL
30
PRPIRNLEVK
40
FTKIFINNEW
50
HESKSGKKFA
60
TCNPSTREQI
70
CEVEEGDKPD
80
VDKAVEAAQV
90
AFQRGSPWRR
100
LDALSRGRLL
110
HQLADLVERD
120
RATLAALETM
130
DTGKPFLHAF
140
FIDLEGCIRT
150
LRYFAGWADK
160
IQGKTIPTDD
170
NVVCFTRHEP
180
IGVCGAITPW
190
NFPLLMLVWK
200
LAPALCCGNT
210
MVLKPAEQTP
220
LTALYLGSLI
230
KEAGFPPGVV
240
NIVPGFGPTV
250
GAAISSHPQI
260
NKIAFTGSTE
270
VGKLVKEAAS
280
RSNLKRVTLE
290
LGGKNPCIVC
300
ADADLDLAVE
310
CAHQGVFFNQ
320
GQCCTAASRV
330
FVEEQVYSEF
340
VRRSVEYAKK
350
RPVGDPFDVK
360
TEQGPQIDQK
370
QFDKILELIE
380
SGKKEGAKLE
390
CGGSAMEDKG
400
LFIKPTVFSE
410
VTDNMRIAKE
420
EIFGPVQPIL
430
KFKSIEEVIK
440
RANSTDYGLT
450
AAVFTKNLDK
460
ALKLASALES
470
GTVWINCYNA
480
LYAQAPFGGF
490
KMSGNGRELG
500
EYALAEYTEV
510
KTVTIKLGDK
NP
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Molecular Function |
GO:0004029 |
aldehyde dehydrogenase (NAD+) activity |
| Molecular Function |
GO:0004030 |
aldehyde dehydrogenase [NAD(P)+] activity |
| Molecular Function |
GO:0070403 |
NAD+ binding |
| Molecular Function |
GO:0042803 |
protein homodimerization activity |
| Molecular Function |
GO:0001758 |
retinal dehydrogenase (NAD+) activity |
| Molecular Function |
GO:0070324 |
thyroid hormone binding |
| Biological Process |
GO:0006081 |
aldehyde metabolic process |
| Biological Process |
GO:0031076 |
embryonic camera-type eye development |
| Biological Process |
GO:0048048 |
embryonic eye morphogenesis |
| Biological Process |
GO:0070384 |
Harderian gland development |
| Biological Process |
GO:0043584 |
nose development |
| Biological Process |
GO:0051289 |
protein homotetramerization |
| Biological Process |
GO:0042574 |
retinal metabolic process |
| Biological Process |
GO:0002138 |
retinoic acid biosynthetic process |
| Biological Process |
GO:0042573 |
retinoic acid metabolic process |
| Biological Process |
GO:0042572 |
retinol metabolic process |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.