AL1A2_CHICK
ID AL1A2_CHICK Reviewed; 518 AA.
AC O93344; Q549A6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Retinal dehydrogenase 2;
DE Short=RALDH 2;
DE Short=RalDH2;
DE EC=1.2.1.36 {ECO:0000250|UniProtKB:Q63639};
DE AltName: Full=Aldehyde dehydrogenase family 1 member A2;
DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2;
DE Short=RALDH(II);
GN Name=ALDH1A2; Synonyms=RALDH2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9727493; DOI=10.1016/s0092-8674(00)81591-3;
RA Sockanathan S., Jessell T.M.;
RT "Motor neuron-derived retinoid signaling specifies the subtype identity of
RT spinal motor neurons.";
RL Cell 94:503-514(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-518.
RA Capdevila J.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts retinaldehyde to retinoic acid. Recognizes as
CC substrates free retinal and cellular retinol-binding protein-bound
CC retinal. Can metabolize octanal and decanal, but has only very low
CC activity with benzaldehyde, acetaldehyde and propanal. Displays
CC complete lack of activity with citral. {ECO:0000250|UniProtKB:Q63639}.
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:0000250|UniProtKB:Q63639};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:Q63639}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O94788}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF064253; AAC34299.1; ALT_INIT; mRNA.
DR EMBL; AF181680; AAF00485.2; -; mRNA.
DR RefSeq; NP_990326.1; NM_204995.1.
DR AlphaFoldDB; O93344; -.
DR SMR; O93344; -.
DR STRING; 9031.ENSGALP00000033786; -.
DR BindingDB; O93344; -.
DR ChEMBL; CHEMBL4295683; -.
DR PaxDb; O93344; -.
DR GeneID; 395844; -.
DR KEGG; gga:395844; -.
DR CTD; 8854; -.
DR VEuPathDB; HostDB:geneid_395844; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; O93344; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; O93344; -.
DR UniPathway; UPA00912; -.
DR PRO; PR:O93344; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:AgBase.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; IMP:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IEP:AgBase.
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 GO; GO:0021522; P:spinal cord motor neuron differentiation; IEP:AgBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..518
FT /note="Retinal dehydrogenase 2"
FT /id="PRO_0000056425"
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 518 AA; 56732 MW; B79FBA3124592460 CRC64;
MTSSKIEMPG EVKADPAALM ASLHLLPSPT LNLEIKHTKI FINNEWQNSE SGRVFPVYNP
ATGEQICEIQ EADKVDTDKA VRAARLAFSL GSVWRRMDAS ERGQLLDKLA DLVERDRAVL
ATMESLNSGK PFLQAFYVDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC
GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP
GFGPIVGAAI ASHVGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
LDYAVEQAHQ GVFFNQGQCC TAGSRIYVEE SIYEEFVRRS VERAKRRVVG SPFDPTTEQG
PQIDKKQYNK ILELIQSGIT EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG
PVQEILRFKT VDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ
SPFGGFKMSG NGREMGESGL REYSEVKTVT IKIPQKNS
