ID   AL3A2_MACFA             Reviewed;         485 AA.
AC   Q60HH8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Aldehyde dehydrogenase family 3 member A2;
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:P51648};
DE            EC=1.2.1.94 {ECO:0000250|UniProtKB:P51648};
DE   AltName: Full=Fatty aldehyde dehydrogenase;
GN   Name=ALDH3A2; ORFNames=QccE-15682;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of medium and long-chain aliphatic
CC       aldehydes to fatty acids. Active on a variety of saturated and
CC       unsaturated aliphatic aldehydes between 6 and 24 carbons in length.
CC       Responsible for conversion of the sphingosine 1-phosphate (S1P)
CC       degradation product hexadecenal to hexadecenoic acid.
CC       {ECO:0000250|UniProtKB:P51648}.
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         Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2
CC         H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:72745;
CC         Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
CC         Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298,
CC         ChEBI:CHEBI:76299; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14-
CC         tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268;
CC         Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate;
CC         Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+);
CC         Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate;
CC         Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:84067; Evidence={ECO:0000250|UniProtKB:P51648};
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:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH;
CC         Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+)
CC         + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:83276; EC=1.2.1.94;
CC         Evidence={ECO:0000250|UniProtKB:P51648};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51648}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P30839}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB125149; BAD51937.1; -; mRNA.
DR   RefSeq; NP_001270311.1; NM_001283382.1.
DR   AlphaFoldDB; Q60HH8; -.
DR   SMR; Q60HH8; -.
DR   STRING; 9541.ENSMFAP00000017937; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   OrthoDB; 606537at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046458; P:hexadecanal metabolic process; ISS:UniProtKB.
DR   CDD; cd07132; ALDH_F3AB; 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; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF9; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER A2; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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   Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane;
KW   Microsome; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..485
FT                   /note="Aldehyde dehydrogenase family 3 member A2"
FT                   /id="PRO_0000056474"
FT   TOPO_DOM        1..463
FT                   /note="Cytoplasmic"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           481..484
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         185..190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51648"
SQ   SEQUENCE   485 AA;  54628 MW;  D01B965D56CBF3D6 CRC64;
     MEREVQRVRQ AFLSGRSRPL RFRLQQLEAL RRMVQEREKD ILAAIAADLC KSELNAYSQE
     VITVLGEIDF MLENLPEWVT AKPVKKNLLT MMDEAYIQPQ PLGVVLIIGA WNYPFVLIIQ
     PLIGAIAAGN AVIIKPSELS ENTAKIVAKL LPQYLDQDLY VVINGGVEET TELLKQRFDH
     IFYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDKDC DLDIVCRRIT WGKYMNCGQT
     CIAPDYILCE ASLQSQIVWK IKETVKEFYG ENIKESPDYE RIINLRHFKR ILSLLEGQKI
     ALGGETDEAT RYIAPTVLTD VDPKTKVMQE EIFGPVLPIV PVKNVDEATD FINEREKPLA
     LYVFSHNHKL IKRMIDETSS GGVTGNDVIM HFTLNSFPFG GVGSSGMGAY HGKHSFDTFS
     HQRPCLLKSL KREGANKLRY PPNSQSKVDW GKFFLLRRFN KEKLGLLVLT FLGIVAAVLV
     NAGYY
//