AL1A3_RAT
ID AL1A3_RAT Reviewed; 512 AA.
AC Q8K4D8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aldehyde dehydrogenase family 1 member A3;
DE EC=1.2.1.36 {ECO:0000250|UniProtKB:P47895};
DE AltName: Full=Aldehyde dehydrogenase 6;
DE AltName: Full=Retinaldehyde dehydrogenase 3;
DE Short=RALDH-3;
DE Short=RalDH3;
GN Name=Aldh1a3; Synonyms=Aldh6, Raldh3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12390888; DOI=10.1095/biolreprod.102.007021;
RA Rexer B.N., Ong D.E.;
RT "A novel short-chain alcohol dehydrogenase from rats with retinol
RT dehydrogenase activity, cyclically expressed in uterine epithelium.";
RL Biol. Reprod. 67:1555-1564(2002).
CC -!- FUNCTION: NAD-dependent aldehyde dehydrogenase that catalyzes the
CC formation of retinoic acid (By similarity). Has high activity with all-
CC trans retinal, and has much lower in vitro activity with acetaldehyde
CC (By similarity). Required for the biosynthesis of normal levels of
CC retinoic acid in the embryonic ocular and nasal regions; retinoic acid
CC is required for normal embryonic development of the eye and the nasal
CC region (By similarity). {ECO:0000250|UniProtKB:P47895,
CC ECO:0000250|UniProtKB:Q9JHW9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000250|UniProtKB:P47895};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P47895}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P47895}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JHW9}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF434845; AAN03711.1; -; mRNA.
DR RefSeq; NP_695212.1; NM_153300.1.
DR AlphaFoldDB; Q8K4D8; -.
DR SMR; Q8K4D8; -.
DR STRING; 10116.ENSRNOP00000045261; -.
DR jPOST; Q8K4D8; -.
DR PaxDb; Q8K4D8; -.
DR PRIDE; Q8K4D8; -.
DR GeneID; 266603; -.
DR KEGG; rno:266603; -.
DR UCSC; RGD:628662; rat.
DR CTD; 220; -.
DR RGD; 628662; Aldh1a3.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q8K4D8; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q8K4D8; -.
DR BRENDA; 1.2.1.36; 5301.
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR PRO; PR:Q8K4D8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; NAS:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:RGD.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:RGD.
DR GO; GO:0070403; F:NAD+ binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; ISO:RGD.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0048048; P:embryonic eye morphogenesis; ISO:RGD.
DR GO; GO:0060324; P:face development; ISO:RGD.
DR GO; GO:0070384; P:Harderian gland development; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0043584; P:nose development; ISO:RGD.
DR GO; GO:0021768; P:nucleus accumbens development; ISO:RGD.
DR GO; GO:0060166; P:olfactory pit development; ISO:RGD.
DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; ISO:RGD.
DR GO; GO:0021983; P:pituitary gland development; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042574; P:retinal metabolic process; ISO:RGD.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IMP:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0060013; P:righting reflex; ISO:RGD.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT CHAIN 2..512
FT /note="Aldehyde dehydrogenase family 1 member A3"
FT /id="PRO_0000056480"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 314
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 257..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 411
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P47895"
SQ SEQUENCE 512 AA; 56171 MW; 2A818D7472F67A5E CRC64;
MATANGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HEPKSGRKFA TYNPSTLEKI
CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL HQLADLIERD RAILATLETM
DTGKPFLHAF FVDLEGCIKT FRYFAGWADK IQGRTIPTDD NVMCFTRHEP IGVCGAITPW
NFPLLMLAWK LAPALCCGNT VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV
GAAISSHPQI NKIAFTGSTE VGKLVKEAAS RSNLKRVTLE LGGRNPCIVC ADADLDLAVE
CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK TEQGPQIDQK
QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD VTDNMRIAKE EIFGPVQPIL
KFKNLEEVIK RANSTDYGLT AAVFTKNLDK ALKLASALES GTVWVNCYNA FYAQAPFGGF
KMSGNGRELG EYALAEYTEV KTVTIKLDEK NP
