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Aldehyde dehydrogenase family 1 member A3 (EC 1.2.1.5) (Aldehyde dehydrogenase 6) (Retinaldehyde dehydrogenase 3) (RALDH-3) (RalDH3)

 AL1A3_MOUSE             Reviewed;         512 AA.
Q9JHW9; Q9EQP7; Q9JI72;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 135.
RecName: Full=Aldehyde dehydrogenase family 1 member A3;
EC=1.2.1.5 {ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11044606};
AltName: Full=Aldehyde dehydrogenase 6 {ECO:0000303|PubMed:11013254};
AltName: Full=Retinaldehyde dehydrogenase 3;
Short=RALDH-3 {ECO:0000303|PubMed:11044606};
Short=RalDH3 {ECO:0000303|PubMed:11025231};
Name=Aldh1a3; Synonyms=Aldh6, Raldh3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=B6/D2;
PubMed=10906479; DOI=10.1016/S0925-4773(00)00352-X;
Li H., Wagner E., McCaffery P., Smith D., Andreadis A., Drager U.C.;
"A retinoic acid synthesizing enzyme in ventral retina and
telencephalon of the embryonic mouse.";
Mech. Dev. 95:283-289(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6 X 129/SvJ; TISSUE=Kidney;
PubMed=11025231; DOI=10.1016/S0925-4773(00)00434-2;
Mic F.A., Molotkov A., Fan X., Cuenca A.E., Duester G.;
"RALDH3, a retinaldehyde dehydrogenase that generates retinoic acid,
is expressed in the ventral retina, otic vesicle and olfactory pit
during mouse development.";
Mech. Dev. 97:227-230(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, CATALYTIC
ACTIVITY, AND PATHWAY.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=11044606; DOI=10.1016/S0925-4773(00)00450-0;
Suzuki R., Shintani T., Sakuta H., Kato A., Ohkawara T., Osumi N.,
Noda M.;
"Identification of RALDH-3, a novel retinaldehyde dehydrogenase,
expressed in the ventral region of the retina.";
Mech. Dev. 98:37-50(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=11013254; DOI=10.1074/jbc.M007376200;
Grun F., Hirose Y., Kawauchi S., Ogura T., Umesono K.;
"Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase
prominently expressed in sensory neuroepithelia during development.";
J. Biol. Chem. 275:41210-41218(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND PATHWAY.
PubMed=14623956; DOI=10.1073/pnas.2336223100;
Dupe V., Matt N., Garnier J.M., Chambon P., Mark M., Ghyselinck N.B.;
"A newborn lethal defect due to inactivation of retinaldehyde
dehydrogenase type 3 is prevented by maternal retinoic acid
treatment.";
Proc. Natl. Acad. Sci. U.S.A. 100:14036-14041(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
DISRUPTION PHENOTYPE.
PubMed=23536097; DOI=10.1523/JNEUROSCI.4618-12.2013;
Romand R., Krezel W., Beraneck M., Cammas L., Fraulob V.,
Messaddeq N., Kessler P., Hashino E., Dolle P.;
"Retinoic acid deficiency impairs the vestibular function.";
J. Neurosci. 33:5856-5866(2013).
-!- FUNCTION: NAD-dependent aldehyde dehydrogenase that catalyzes the
formation of retinoic acid (PubMed:11044606, PubMed:11013254,
PubMed:14623956). Has high activity with all-trans retinal, and
has much lower in vitro activity with acetaldehyde (By
similarity). Required for the biosynthesis of normal levels of
retinoic acid in the embryonic ocular and nasal regions; retinoic
acid is required for normal embryonic development of the eye and
the nasal region (PubMed:14623956). {ECO:0000250|UniProtKB:P47895,
ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11044606,
ECO:0000269|PubMed:14623956}.
-!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a
carboxylate + NAD(P)H. {ECO:0000269|PubMed:11013254,
ECO:0000269|PubMed:11044606}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.33 uM for all-trans retinal {ECO:0000269|PubMed:11013254};
Vmax=58 nmol/min/mg enzyme for all-trans retinal
{ECO:0000269|PubMed:11013254};
-!- PATHWAY: Cofactor metabolism; retinol metabolism.
{ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11044606,
ECO:0000269|PubMed:14623956}.
-!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P47895}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11013254}.
-!- TISSUE SPECIFICITY: Detected in embryonic head (at protein level)
(PubMed:14623956). Ventral retina. {ECO:0000269|PubMed:10906479,
ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11025231,
ECO:0000269|PubMed:11044606, ECO:0000269|PubMed:14623956}.
-!- DEVELOPMENTAL STAGE: In mouse embryos, RALDH3 expression is first
noticed in the ventral optic eminence at E8.75, then in the optic
vesicle/cup, otic vesicle and olfactory placode/pit from E9.5 to
E11.5. {ECO:0000269|PubMed:11025231}.
-!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
Mendelian rate, but all die within 10 hours after birth
(PubMed:14623956, PubMed:23536097). Lethality is due to
respiratory distress, caused by choanal atresia, i.e. the lack of
communication between the nasal and oral cavities. Mutant embryos
at 11.5 dpc lack detectable retinoic acid in the ventral retina,
nasal epithelium and in the nasolacrimal groove. At 14.5 dpc
mutant embryos display shortening of the ventral retina associated
with lens rotation and persistence of the retrolenticular
membrane, indicative of retinoic acid deficiency. Still, at 18.5
dpc the ventral retina appears normal. Embryos at 18.5 dpc lack
Harderian glands, and display multiple malformations in the nasal
region, including choanal atresia, lack of maxillary sinuses and
nasolacrimal ducts (PubMed:14623956). Oral gavage of pregnant
females with retinoic acid prevents choanal atresia and other
malformations of the nasal region (PubMed:14623956,
PubMed:23536097). Females that were fed retinoic acid give birth
to pups with malformations of the inner ear vestibular organ,
causing repetitive circling behavior with head tilting
(PubMed:23536097). Likewise, mice display impaired ability in
crossing a beam without slipping and an impaired ability to swim
(PubMed:23536097). {ECO:0000269|PubMed:14623956,
ECO:0000269|PubMed:23536097}.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF253409; AAF67736.1; -; mRNA.
EMBL; AF280404; AAF86980.1; -; mRNA.
EMBL; AF246711; AAG38488.1; -; mRNA.
EMBL; AF152359; AAG33935.1; -; mRNA.
EMBL; BC058277; AAH58277.1; -; mRNA.
CCDS; CCDS21345.1; -.
RefSeq; NP_444310.3; NM_053080.3.
UniGene; Mm.140988; -.
ProteinModelPortal; Q9JHW9; -.
SMR; Q9JHW9; -.
BioGrid; 208193; 1.
STRING; 10090.ENSMUSP00000015278; -.
iPTMnet; Q9JHW9; -.
PhosphoSitePlus; Q9JHW9; -.
MaxQB; Q9JHW9; -.
PaxDb; Q9JHW9; -.
PRIDE; Q9JHW9; -.
Ensembl; ENSMUST00000015278; ENSMUSP00000015278; ENSMUSG00000015134.
GeneID; 56847; -.
KEGG; mmu:56847; -.
UCSC; uc009hhi.2; mouse.
CTD; 220; -.
MGI; MGI:1861722; Aldh1a3.
eggNOG; KOG2450; Eukaryota.
eggNOG; COG1012; LUCA.
GeneTree; ENSGT00760000118999; -.
HOGENOM; HOG000271505; -.
HOVERGEN; HBG000097; -.
InParanoid; Q9JHW9; -.
KO; K00129; -.
OMA; NEWHESK; -.
OrthoDB; EOG091G05E8; -.
PhylomeDB; Q9JHW9; -.
TreeFam; TF300455; -.
BRENDA; 1.2.1.36; 3474.
BRENDA; 1.2.1.5; 3474.
Reactome; R-MMU-5365859; RA biosynthesis pathway.
SABIO-RK; Q9JHW9; -.
UniPathway; UPA00912; -.
PRO; PR:Q9JHW9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000015134; -.
CleanEx; MM_ALDH1A3; -.
ExpressionAtlas; Q9JHW9; baseline and differential.
Genevisible; Q9JHW9; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:MGI.
GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:MGI.
GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:MGI.
GO; GO:0070403; F:NAD+ binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
GO; GO:0070324; F:thyroid hormone binding; IPI:MGI.
GO; GO:0031076; P:embryonic camera-type eye development; IMP:UniProtKB.
GO; GO:0048048; P:embryonic eye morphogenesis; IMP:MGI.
GO; GO:0060324; P:face development; IGI:MGI.
GO; GO:0070384; P:Harderian gland development; IMP:UniProtKB.
GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0043584; P:nose development; IMP:UniProtKB.
GO; GO:0021768; P:nucleus accumbens development; IMP:MGI.
GO; GO:0060166; P:olfactory pit development; IMP:MGI.
GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IGI:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0042574; P:retinal metabolic process; ISO:MGI.
GO; GO:0002138; P:retinoic acid biosynthetic process; IDA:MGI.
GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0060013; P:righting reflex; IMP:MGI.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016163; Ald_DH_C.
InterPro; IPR016160; Ald_DH_CS_CYS.
InterPro; IPR029510; Ald_DH_CS_GLU.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
InterPro; IPR012394; Aldehyde_DH_NAD(P).
Pfam; PF00171; Aldedh; 1.
PIRSF; PIRSF036492; ALDH; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; NAD; Oxidoreductase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P47895}.
CHAIN 2 512 Aldehyde dehydrogenase family 1 member
A3.
/FTId=PRO_0000056479.
NP_BIND 257 262 NAD. {ECO:0000250|UniProtKB:P47895}.
ACT_SITE 280 280 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10007, ECO:0000255|PROSITE-
ProRule:PRU10008}.
ACT_SITE 314 314 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10007, ECO:0000255|PROSITE-
ProRule:PRU10008}.
BINDING 204 204 NAD. {ECO:0000250|UniProtKB:P47895}.
BINDING 207 207 NAD. {ECO:0000250|UniProtKB:P47895}.
BINDING 361 361 NAD. {ECO:0000250|UniProtKB:P47895}.
BINDING 411 411 NAD. {ECO:0000250|UniProtKB:P47895}.
SITE 181 181 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P47895}.
CONFLICT 91 91 L -> V (in Ref. 1; AAF67736).
{ECO:0000305}.
CONFLICT 208 208 Q -> R (in Ref. 4; AAG33935).
{ECO:0000305}.
CONFLICT 223 223 V -> E (in Ref. 1; AAF67736).
{ECO:0000305}.
CONFLICT 341 341 R -> S (in Ref. 4; AAG33935).
{ECO:0000305}.
CONFLICT 407 407 I -> R (in Ref. 1; AAF67736).
{ECO:0000305}.
SEQUENCE 512 AA; 56157 MW; 5BBC6DEE41E58CFE CRC64;
MATTNGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HESKSGRKFA TYNPSTLEKI
CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL HQLADLVERD RAILATLETM
DTGKPFLHAF FVDLEGCIKT FRYFAGWADK IQGRTIPTDD NVVCFTRHEP IGVCGAITPW
NFPLLMLAWK LAPALCCGNT VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV
GAAISSHPQI NKIAFTGSTE VGKLVREAAS RSNLKRVTLE LGGKNPCIVC ADADLDLAVE
CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK TEQGPQIDQK
QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD VTDNMRIAKE EIFGPVQPIL
KFKNLEEVIK RANSTDYGLT AAVFTKNLDK ALKLAAALES GTVWINCYNA FYAQAPFGGF
KMSGNGRELG EYALAEYTEV KTVTIKLEEK NP


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