AL3A2_RAT
ID AL3A2_RAT Reviewed; 484 AA.
AC P30839;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aldehyde dehydrogenase family 3 member A2;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P47740};
DE EC=1.2.1.94 {ECO:0000250|UniProtKB:P51648};
DE AltName: Full=Aldehyde dehydrogenase 4;
DE AltName: Full=Fatty aldehyde dehydrogenase;
DE AltName: Full=Microsomal aldehyde dehydrogenase;
DE Short=msALDH;
GN Name=Aldh3a2; Synonyms=Aldh4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-110; 236-255 AND
RP 408-427, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Liver;
RX PubMed=1717467; DOI=10.1016/s0021-9258(18)55028-6;
RA Miyauchi K., Masaki R., Taketani S., Yamamoto A., Akayama M., Tashiro Y.;
RT "Molecular cloning, sequencing, and expression of cDNA for rat liver
RT microsomal aldehyde dehydrogenase.";
RL J. Biol. Chem. 266:19536-19542(1991).
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 (By similarity).
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 {ECO:0000269|PubMed:1717467}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:1717467}; Single-
CC pass membrane protein {ECO:0000305|PubMed:1717467}; Cytoplasmic side
CC {ECO:0000269|PubMed:1717467}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:1717467}.
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; M73714; AAA41555.1; -; mRNA.
DR PIR; A41028; A41028.
DR RefSeq; NP_113919.2; NM_031731.2.
DR AlphaFoldDB; P30839; -.
DR SMR; P30839; -.
DR IntAct; P30839; 1.
DR STRING; 10116.ENSRNOP00000061762; -.
DR CarbonylDB; P30839; -.
DR iPTMnet; P30839; -.
DR PhosphoSitePlus; P30839; -.
DR jPOST; P30839; -.
DR PaxDb; P30839; -.
DR PRIDE; P30839; -.
DR GeneID; 65183; -.
DR KEGG; rno:65183; -.
DR UCSC; RGD:61866; rat.
DR CTD; 224; -.
DR RGD; 61866; Aldh3a2.
DR eggNOG; KOG2456; Eukaryota.
DR InParanoid; P30839; -.
DR PhylomeDB; P30839; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-RNO-389599; Alpha-oxidation of phytanate.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:P30839; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:RGD.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; ISO:RGD.
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:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046292; P:formaldehyde metabolic process; IDA:RGD.
DR GO; GO:0046458; P:hexadecanal metabolic process; ISS:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR GO; GO:0033306; P:phytol metabolic process; ISO:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Microsome; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Aldehyde dehydrogenase family 3 member A2"
FT /id="PRO_0000056476"
FT TOPO_DOM 1..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1717467"
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 484 AA; 54082 MW; 9F50CB34AB64C31D CRC64;
MERQVQRLRQ TFRSGRSRPL RFRLQQLEAL RRMVQEREKD ILAAIAADLS KSELNAYSHE
VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTLQ
PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY MIVNGGVEET TELLRQRFDH
ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIT WGKYMNCGQT
CIAPDYILCE ASSQDQIVQK IKDTVKDFYG ENVKASPDYE RIINLRHFKR IKSLLEGQKI
AFGGETDEAT RYIAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVEEAIN FINDREKPLA
LYIFSHNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS
HQRPCLLKGL KGESVNKLRY PPNSESKVSW SKFFLLKQFN KGRLQLLLLV CLVAVAAVIV
KDQL
