ID   AL3A2_RAT               Reviewed;         484 AA.
AC   P30839;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-NOV-2008, entry version 70.
DE   RecName: Full=Fatty aldehyde dehydrogenase;
DE            EC=1.2.1.3;
DE   AltName: Full=Aldehyde dehydrogenase family 3 member A2;
DE   AltName: Full=Aldehyde dehydrogenase 4;
DE   AltName: Full=Microsomal aldehyde dehydrogenase;
DE            Short=msALDH;
GN   Name=Aldh3a2; Synonyms=Aldh4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 93-110; 236-255
RP   AND 408-427.
RC   TISSUE=Liver;
RX   MEDLINE=92011753; PubMed=1717467;
RA   Miyauchi K., Masaki R., Taketani S., Yamamoto A., Akayama M.,
RA   Tashiro Y.;
RT   "Molecular cloning, sequencing, and expression of cDNA for rat liver
RT   microsomal aldehyde dehydrogenase.";
RL   J. Biol. Chem. 266:19536-19542(1991).
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein; Cytoplasmic side.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; M73714; AAA41555.1; -; mRNA.
DR   PIR; A41028; A41028.
DR   RefSeq; NP_113919.2; -.
DR   UniGene; Rn.9113; -.
DR   HSSP; P11883; 1AD3.
DR   Ensembl; ENSRNOG00000002342; Rattus norvegicus.
DR   GeneID; 65183; -.
DR   KEGG; rno:65183; -.
DR   RGD; 61866; Aldh3a2.
DR   HOVERGEN; P30839; -.
DR   NextBio; 614089; -.
DR   ArrayExpress; P30839; -.
DR   GermOnline; ENSRNOG00000002342; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR012394; Ald_DHase_NAD(P).
DR   InterPro; IPR015590; Aldehyde_DHase.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   PANTHER; PTHR11699:SF15; ALDH; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane; NAD;
KW   Oxidoreductase; Transmembrane.
FT   CHAIN         1    484       Fatty aldehyde dehydrogenase.
FT                                /FTId=PRO_0000056476.
FT   TOPO_DOM      1    463       Cytoplasmic.
FT   TRANSMEM    464    480       Potential.
FT   NP_BIND     185    190       NAD (Potential).
FT   MOTIF       481    484       Prevents secretion from ER (By
FT                                similarity).
FT   ACT_SITE    207    207       By similarity.
FT   ACT_SITE    241    241       By similarity.
SQ   SEQUENCE   484 AA;  54082 MW;  9F50CB34AB64C31D CRC64;
     MERQVQRLRQ TFRSGRSRPL RFRLQQLEAL RRMVQEREKD ILAAIAADLS KSELNAYSHE
     VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTLQ
     PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY MIVNGGVEET TELLRQRFDH
     ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIT WGKYMNCGQT
     CIAPDYILCE ASSQDQIVQK IKDTVKDFYG ENVKASPDYE RIINLRHFKR IKSLLEGQKI
     AFGGETDEAT RYIAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVEEAIN FINDREKPLA
     LYIFSHNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS
     HQRPCLLKGL KGESVNKLRY PPNSESKVSW SKFFLLKQFN KGRLQLLLLV CLVAVAAVIV
     KDQL
//