AL3A1_CANLF
ID AL3A1_CANLF Reviewed; 453 AA.
AC A3RF36;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
DE EC=1.2.1.5 {ECO:0000250|UniProtKB:P47739};
DE AltName: Full=ALDHIII;
DE AltName: Full=Aldehyde dehydrogenase 3;
DE AltName: Full=Aldehyde dehydrogenase family 3 member A1;
GN Name=ALDH3A1; Synonyms=ALDH3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea;
RA Wistow G.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC derived acetaldehyde (Probable). They are involved in the metabolism of
CC corticosteroids, biogenic amines, neurotransmitters, and lipid
CC peroxidation (Probable). Oxidizes medium and long chain aldehydes into
CC non-toxic fatty acids (By similarity). Preferentially oxidizes aromatic
CC aldehyde substrates (By similarity). Comprises about 50 percent of
CC corneal epithelial soluble proteins (By similarity). May play a role in
CC preventing corneal damage caused by ultraviolet light (By similarity).
CC {ECO:0000250|UniProtKB:P30838, ECO:0000250|UniProtKB:P47739,
CC ECO:0000305}.
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=1.2.1.5;
CC Evidence={ECO:0000250|UniProtKB:P47739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P47739};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; EF382362; ABN70935.1; -; mRNA.
DR RefSeq; NP_001075889.1; NM_001082420.1.
DR AlphaFoldDB; A3RF36; -.
DR SMR; A3RF36; -.
DR STRING; 9612.ENSCAFP00000026805; -.
DR PaxDb; A3RF36; -.
DR PRIDE; A3RF36; -.
DR Ensembl; ENSCAFT00000028823; ENSCAFP00000026805; ENSCAFG00000018146.
DR Ensembl; ENSCAFT00845029400; ENSCAFP00845023106; ENSCAFG00845016394.
DR GeneID; 489526; -.
DR KEGG; cfa:489526; -.
DR CTD; 218; -.
DR VEuPathDB; HostDB:ENSCAFG00845016394; -.
DR VGNC; VGNC:37786; ALDH3A1.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000162101; -.
DR InParanoid; A3RF36; -.
DR OrthoDB; 646662at2759; -.
DR Proteomes; UP000002254; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid metabolism; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30838"
FT CHAIN 2..453
FT /note="Aldehyde dehydrogenase, dimeric NADP-preferring"
FT /id="PRO_0000289586"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P30838"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30838"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30838"
SQ SEQUENCE 453 AA; 50713 MW; E986E2EF8D8AE46A CRC64;
MSKISEVVQR ARAAFNSGKT RPLQFRIQQL EALRRMIKEH EKDLAGALTA DLHKNEWNAY
YEEVVYVLEE IEYMIKKLPE WAADEPVEKT PQTQQDECYI HSEPLGVVLI IGTWNYPFTV
TIQPMVGAIA AGNAVVIKPS ELSENMANLL ATIIPQYLDR DLYPVISGGI PETTELLKER
FDHILYTGNT AVGKVIMMAA AKHLTPVTLE LGGKNPCYVD KDCDLDIACR RIAWGKFMNS
GQTCVAPDYI LCDPSIQNQI VEKLKKALKE FYGEDAKKSR DYGRIINSRH FQRVMGLMEG
QKVAYGGTGD AATRYIAPTI LIDVDTQSQV MQEEIFGPVM PIVCVRSLEE AIQFINQREK
PLALYVFSLN DKMIKKMIAE TSSGGVTAND VIVHVSVHSL PYGGVGNSGM GSYHGKKSFE
TFSHCRSCLV RPLLNDESLK TRYPPSLAKM TRH
