ID ALDH1_ELEED Reviewed; 501 AA. AC Q28399; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 113. 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 Elephantulus edwardii (Cape long-eared elephant shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Elephantulus. OX NCBI_TaxID=28737; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lens; 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). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, AND RP HOMOTETRAMERIZATION. RX PubMed=12693930; DOI=10.1021/bi027367w; RA Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., RA Wistow G.; RT "Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde RT dehydrogenase for a new role in the eye lens."; RL Biochemistry 42:4349-4356(2003). 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 class- CC 1 aldehyde dehydrogenase 1. This eye-specific form is a structural CC protein of the lens and, in other part of the eye, serves as the major CC form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. CC {ECO:0000269|PubMed:12693930}. 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:0000269|PubMed:12693930}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Eye specific, with very high expression in the CC lens. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U02483; AAB60268.1; -; mRNA. DR RefSeq; NP_001277088.1; NM_001290159.1. DR PDB; 1O9J; X-ray; 2.40 A; A/B/C/D=1-501. DR PDBsum; 1O9J; -. DR AlphaFoldDB; Q28399; -. DR SMR; Q28399; -. DR MoonProt; Q28399; -. DR GeneID; 102867337; -. DR CTD; 102867337; -. DR OrthoDB; 2291791at2759; -. DR BRENDA; 1.2.1.36; 7360. DR UniPathway; UPA00780; UER00768. DR EvolutionaryTrace; Q28399; -. DR Proteomes; UP000694952; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IPI:CAFA. DR GO; GO:0051287; F:NAD binding; IDA:CAFA. DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:CAFA. DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0042574; P:retinal metabolic process; IDA:CAFA. DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. 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. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; NAD; Oxidoreductase. FT CHAIN 1..501 FT /note="Aldehyde dehydrogenase, cytosolic 1" FT /id="PRO_0000056427" FT ACT_SITE 269 FT /note="Proton acceptor" FT ACT_SITE 303 FT /note="Nucleophile" FT BINDING 246..251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12693930" FT SITE 170 FT /note="Transition state stabilizer" FT STRAND 22..25 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:1O9J" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 57..71 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 82..98 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 100..111 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 115..120 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 122..136 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 148..159 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 200..212 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:1O9J" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 229..234 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 241..246 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 284..296 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 306..312 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 313..326 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 348..364 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 395..398 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 403..411 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 414..422 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 428..433 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 437..446 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 449..455 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 479..483 FT /evidence="ECO:0007829|PDB:1O9J" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:1O9J" FT STRAND 487..495 FT /evidence="ECO:0007829|PDB:1O9J" SQ SEQUENCE 501 AA; 54538 MW; 9E3D5BBE083ACAD7 CRC64; MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC EVEEADKEDV DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKVFASAYL MDLDYCIKAL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGLIFPWN APMILLACKI GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE YGIHEYTEVK TVTMKISEKN S //