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   16-JUN-2009, entry version 57.
DE   RecName: Full=Retinal dehydrogenase 2;
DE            Short=RALDH 2;
DE            Short=RalDH2;
DE            EC=1.2.1.36;
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   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98394476; 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
RT   identity of 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: Recognizes as substrates free retinal and cellular
CC       retinol-binding protein-bound retinal. Does metabolize octanal and
CC       decanal but does not metabolize citral, benzaldehyde, acetaldehyde
CC       and propanal efficiently (By similarity).
CC   -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AF064253; AAC34299.1; ALT_INIT; mRNA.
DR   EMBL; AF181680; AAF00485.2; -; mRNA.
DR   IPI; IPI00575967; -.
DR   RefSeq; NP_990326.1; -.
DR   UniGene; Gga.2996; -.
DR   HSSP; Q63639; 1BI9.
DR   Ensembl; ENSGALG00000004270; Gallus gallus.
DR   GeneID; 395844; -.
DR   KEGG; gga:395844; -.
DR   HOGENOM; O93344; -.
DR   HOVERGEN; O93344; -.
DR   BRENDA; 1.2.1.36; 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    518       Retinal dehydrogenase 2.
FT                                /FTId=PRO_0000056425.
FT   NP_BIND     263    268       NAD (By similarity).
FT   ACT_SITE    286    286       Proton acceptor (By similarity).
FT   ACT_SITE    320    320       Nucleophile (By similarity).
FT   SITE        187    187       Transition state stabilizer (By
FT                                similarity).
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
//