GenomeNet

Database: UniProt
Entry: F7C1D1_MACMU
LinkDB: F7C1D1_MACMU
Original site: F7C1D1_MACMU 
ID   F7C1D1_MACMU            Unreviewed;       584 AA.
AC   F7C1D1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Aldehyde dehydrogenase family 3 member A2 {ECO:0000256|ARBA:ARBA00039622};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.94 {ECO:0000256|ARBA:ARBA00039117};
DE   AltName: Full=Fatty aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00042336};
GN   Name=ALDH3A2 {ECO:0000313|Ensembl:ENSMMUP00000018565.4,
GN   ECO:0000313|VGNC:VGNC:69785};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000018565.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000018565.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000018565.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00035777};
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:0000256|ARBA:ARBA00036228};
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:0000256|ARBA:ARBA00035953};
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:0000256|ARBA:ARBA00035974};
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:0000256|ARBA:ARBA00036932};
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:0000256|ARBA:ARBA00035984};
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:0000256|ARBA:ARBA00000589};
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:0000256|ARBA:ARBA00035786};
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:0000256|ARBA:ARBA00036881};
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:0000256|ARBA:ARBA00036717};
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:0000256|ARBA:ARBA00024149};
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:0000256|ARBA:ARBA00036332};
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:0000256|ARBA:ARBA00036265};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004131}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   AlphaFoldDB; F7C1D1; -.
DR   SMR; F7C1D1; -.
DR   STRING; 9544.ENSMMUP00000018565; -.
DR   Ensembl; ENSMMUT00000019831.4; ENSMMUP00000018565.4; ENSMMUG00000014130.4.
DR   VEuPathDB; HostDB:ENSMMUG00000014130; -.
DR   VGNC; VGNC:69785; ALDH3A2.
DR   eggNOG; KOG2456; Eukaryota.
DR   GeneTree; ENSGT00940000157944; -.
DR   HOGENOM; CLU_005391_3_2_1; -.
DR   InParanoid; F7C1D1; -.
DR   OMA; EIDWCKQ; -.
DR   Proteomes; UP000006718; Chromosome 16.
DR   Bgee; ENSMMUG00000014130; Expressed in liver and 21 other cell types or tissues.
DR   ExpressionAtlas; F7C1D1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:Ensembl.
DR   GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046458; P:hexadecanal metabolic process; IEA:Ensembl.
DR   GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR   GO; GO:0033306; P:phytol metabolic process; IEA:Ensembl.
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   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        540..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..497
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   584 AA;  66491 MW;  BB375A2839486CA6 CRC64;
     MWWKKVYVDT WGGWTRECFQ EWGSYICLVI PSMFMVCIER WTFEIGNFLA GLIDMTELGA
     QGIIYELALV AYMDQAMERE VQRVRQAFLS GRSRPLRFRL QQLEALRRMV QEREKDILAA
     IAADLCKSEL NAYSQEVITV LGEIDFMLEN LPEWVTAKPV KKNLLTMMDE AYIQPQPLGV
     VLIIGAWNYP FVLIIQPLIG AIAAGNAVII KPSELSENTA KIVAKLLPQY LDQDLYVVIN
     GGVEETTELL KQRFDHIFYT GNTAVGKIVM EAAAKHLTPV TLELGGKSPC YIDKDCDLDI
     VCRRITWGKY MNCGQTCIAP DYILCEASLQ SQIVWKIKET VKEFYGENIK ESPDYERIIN
     LRHFKRILSL LEGQKIALGG ETDEATRYIA PTVLTDVDPK TKVMQEEIFG PVLPIVPVKN
     VDEAIDFINE REKPLALYVF SHNHKLIKRM IDETSSGGVT GNDVIMHFTL NSFPFGGVGS
     SGMGAYHGKH SFDTFSHQRP CLLKSLKREG ANKLRYPPNS QSKVDWGKFF LLRRFNKEKL
     GLLVFTFLGI VAAVLVKKYQ AVLRRKALLI FLVVHRLRWS SKQR
//
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