ID   ALDH1_MACPR             Reviewed;         501 AA.
AC   Q29490;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Aldehyde dehydrogenase, cytosolic 1;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 1;
DE   AltName: Full=ETA-crystallin;
GN   Name=ALDH1;
OS   Macroscelides proboscideus (Short-eared elephant shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Afrotheria; Macroscelidea; Macroscelididae;
OC   Macroscelides.
OX   NCBI_TaxID=29082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   MEDLINE=96279083; 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
RT   eye lens. Gene recruitment of eta-crystallin.";
RL   J. Biol. Chem. 271:15623-15628(1996).
CC   -!- FUNCTION: Major component of the eye of elephant shrews, which in
CC       contrast to other mammals, possesses both a lens- and a non-lens
CC       class-1 aldehyde dehydrogenase 1. This eye-specific form is a
CC       structural protein of the lens and, in other part of the eye,
CC       serves as the major form of ALDH1. Can convert/oxidize
CC       retinaldehyde to retinoic acid.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Eye specific, with very high expression in the
CC       lens.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; U03906; AAC48588.1; -; mRNA.
DR   HSSP; Q28399; 1O9J.
DR   HOVERGEN; Q29490; -.
DR   BRENDA; 1.2.1.3; 317919.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) 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; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    501       Aldehyde dehydrogenase, cytosolic 1.
FT                                /FTId=PRO_0000056428.
FT   NP_BIND     246    251       NAD (By similarity).
FT   ACT_SITE    269    269       Proton acceptor (By similarity).
FT   ACT_SITE    303    303       Nucleophile (By similarity).
FT   SITE        170    170       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   501 AA;  54625 MW;  48C15C682665D0C0 CRC64;
     MSSSGMPDLP APLTNIKIQH TKLFINNEWH DSVSGKTFPV FNPATEEKIC EVEEADKEDV
     DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKIFASAYL
     MDLDYCIKVL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGQIFPWN APMILLACKI
     GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
     KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG
     QSCIAASKLF VEETIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES
     GKKEGAKLEC GGGPWGNKGY FIQPTIFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR
     ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE
     YGIHEYTEVK TVTMKISEKN S
//