ID   ALDH2_MACPR             Reviewed;         240 AA.
AC   Q29491;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Aldehyde dehydrogenase, cytosolic 2;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 1;
DE   AltName: Full=ALDH1-NL;
DE   AltName: Full=Non-lens ALDH1;
DE   Flags: Fragment;
OS   Macroscelides proboscideus (Short-eared elephant shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Macroscelides.
OX   NCBI_TaxID=29082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8663049; DOI=10.1074/jbc.271.26.15623;
RA   Graham C., Hodin J., Wistow G.;
RT   "A retinaldehyde dehydrogenase as a structural protein in a mammalian eye
RT   lens. Gene recruitment of eta-crystallin.";
RL   J. Biol. Chem. 271:15623-15628(1996).
CC   -!- FUNCTION: Elephant shrews, in contrast to other mammals, possess both a
CC       lens- and a non-lens specific class-1 aldehyde dehydrogenase. Can
CC       convert/oxidize retinaldehyde to retinoic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Non-lens specific, predominant form expressed in
CC       the liver.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U40486; AAC48589.1; -; mRNA.
DR   AlphaFoldDB; Q29491; -.
DR   SMR; Q29491; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046185; P:aldehyde catabolic process; ISS:UniProtKB.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR11699:SF140; ALDEHYDE DEHYDROGENASE 1A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           <1..240
FT                   /note="Aldehyde dehydrogenase, cytosolic 2"
FT                   /id="PRO_0000056429"
FT   ACT_SITE        8
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000255"
FT   MOD_RES         106
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         149
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         151
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47738"
FT   NON_TER         1
SQ   SEQUENCE   240 AA;  26515 MW;  9E34DC9B4D5153A9 CRC64;
     NLKRVTLELG GKSPCIVFAD ADLDNAVEFA HRGLFFHQGQ CCVAASRLFV EESIYDEFVR
     RSVERAKKYV LGNPLTPGVS QGPQIDKEQY DKIIDLIESG KKEGAKLECG GGPWGNKGYF
     IQPTVFSNVT DEMRIAKEEI FGPVQQIMKF KSLDEVIKRA NNTFYGLAAG VFTKDLDKAV
     TVSAALQAGT VWVNCYMANS VQCPFGGFKM SGNGRELGEY GLHEYTEVKT VTMKISKKNS
//