AL1A2_TAEGU
ID AL1A2_TAEGU Reviewed; 517 AA.
AC Q9I8W8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Retinal dehydrogenase 2;
DE Short=RALDH 2;
DE Short=RalDH2;
DE EC=1.2.1.36 {ECO:0000269|PubMed:10985355};
DE AltName: Full=Aldehyde dehydrogenase family 1 member A2;
DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2;
DE Short=RALDH(II);
DE AltName: Full=zRalDH;
GN Name=ALDH1A2; Synonyms=RALDH2;
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=10985355; DOI=10.1016/s0896-6273(00)00043-x;
RA Denisenko-Nehrbass N.I., Jarvis E., Scharff C., Nottebohm F., Mello C.V.;
RT "Site-specific retinoic acid production in the brain of adult songbirds.";
RL Neuron 27:359-370(2000).
CC -!- FUNCTION: Converts retinaldehyde to retinoic acid (PubMed:10985355).
CC Recognizes as substrates free retinal and cellular retinol-binding
CC protein-bound retinal (By similarity). Has only very low activity with
CC benzaldehyde and acetaldehyde. Displays complete lack of activity with
CC citral (PubMed:10985355). It is responsible for the ability of brain
CC sites to synthesize retinoic acid. Its activity in the high vocal
CC center (HVC) is required for the song of juvenile zebra finches to
CC become stereotyped (PubMed:10985355). {ECO:0000250|UniProtKB:Q63639,
CC ECO:0000269|PubMed:10985355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate;
CC Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000269|PubMed:10985355};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.118 uM for retinal {ECO:0000269|PubMed:10985355};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:10985355}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O94788}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in the high vocal center (HVC) which
CC integrates auditory and motor activities and constitutes a nodal
CC nucleus on the song system. {ECO:0000269|PubMed:10985355}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF162770; AAF80471.1; -; mRNA.
DR RefSeq; NP_001070153.1; NM_001076685.1.
DR AlphaFoldDB; Q9I8W8; -.
DR SMR; Q9I8W8; -.
DR STRING; 59729.ENSTGUP00000031661; -.
DR GeneID; 751771; -.
DR KEGG; tgu:751771; -.
DR CTD; 8854; -.
DR InParanoid; Q9I8W8; -.
DR OrthoDB; 153834at2759; -.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000007754; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
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; IPR029510; Ald_DH_CS_GLU.
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.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..517
FT /note="Retinal dehydrogenase 2"
FT /id="PRO_0000225600"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 184..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 210..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 366..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT SITE 187
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 517 AA; 56596 MW; D842A2A1BF4DA109 CRC64;
MTSSKIEMPG EVKADPAALM ASLHLLPSPT LNLEIKYTKI FINNEWQNSE SGRIFPVYNP
ATGEQICDIQ EADKVDTDKA VRAARLAFSL GSVWRRMDAS ERGHLLDKLA DLVERDRAIL
ATMESLNSGK PFLQAFYVDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC
GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP
GFGPIVGAAI ASHVGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
LDYAVEQAHQ GVFFNQGQCC TAGSRIYVEE SIYEEFVRKS VKRAKRKIVG SPFDPTTEQG
PQIDKKQYNK ILELIQSGIT EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG
PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ
SPFGGSKSGN GREMGECGLR EYSEVKTVTI KIPQENS
