AL3B2_MOUSE
ID AL3B2_MOUSE Reviewed; 479 AA.
AC E9Q3E1; Q497U8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B2 {ECO:0000312|MGI:MGI:2147613};
DE EC=1.2.1.3 {ECO:0000269|PubMed:25286108};
DE AltName: Full=Aldehyde dehydrogenase 8 {ECO:0000250|UniProtKB:P48448};
DE Flags: Precursor;
GN Name=Aldh3b2 {ECO:0000312|MGI:MGI:2147613};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Ensembl:ENSMUSP00000115356};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAI00371.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-479.
RC TISSUE=Placenta {ECO:0000312|EMBL:AAI00371.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP ISOPRENYLATION AT CYS-476, AND MUTAGENESIS OF TRP-462; TRP-469 AND CYS-476.
RX PubMed=25286108; DOI=10.1042/bj20140624;
RA Kitamura T., Takagi S., Naganuma T., Kihara A.;
RT "Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via
RT two C-terminal tryptophan residues and lipid modification.";
RL Biochem. J. 465:79-87(2015).
CC -!- FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty
CC acids. {ECO:0000269|PubMed:25286108}.
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:0000269|PubMed:25286108};
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:0000269|PubMed:25286108};
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:0000269|PubMed:25286108};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2. {ECO:0000250|UniProtKB:P48448}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25286108}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, white adipose tissue, lung,
CC small intestine, kidney, spleen and liver.
CC {ECO:0000269|PubMed:25286108}.
CC -!- PTM: Geranylgeranylation is important for localization to lipid
CC droplets and enzyme activity. {ECO:0000269|PubMed:25286108}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|PIRNR:PIRNR036492}.
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DR EMBL; AC133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100370; AAI00371.1; -; mRNA.
DR CCDS; CCDS50347.1; -.
DR RefSeq; NP_001170909.1; NM_001177438.1.
DR AlphaFoldDB; E9Q3E1; -.
DR SMR; E9Q3E1; -.
DR STRING; 10090.ENSMUSP00000115356; -.
DR SwissLipids; SLP:000001743; -.
DR iPTMnet; E9Q3E1; -.
DR PhosphoSitePlus; E9Q3E1; -.
DR SwissPalm; E9Q3E1; -.
DR jPOST; E9Q3E1; -.
DR MaxQB; E9Q3E1; -.
DR PaxDb; E9Q3E1; -.
DR PeptideAtlas; E9Q3E1; -.
DR PRIDE; E9Q3E1; -.
DR ProteomicsDB; 296166; -.
DR Ensembl; ENSMUST00000143380; ENSMUSP00000115356; ENSMUSG00000075296.
DR GeneID; 621603; -.
DR KEGG; mmu:621603; -.
DR UCSC; uc008fxw.2; mouse.
DR CTD; 222; -.
DR MGI; MGI:2147613; Aldh3b2.
DR VEuPathDB; HostDB:ENSMUSG00000075296; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000155904; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; E9Q3E1; -.
DR OMA; NDCLWHL; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; E9Q3E1; -.
DR TreeFam; TF314264; -.
DR BRENDA; 1.2.1.48; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 621603; 3 hits in 75 CRISPR screens.
DR PRO; PR:E9Q3E1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; E9Q3E1; protein.
DR Bgee; ENSMUSG00000075296; Expressed in lip and 82 other tissues.
DR Genevisible; E9Q3E1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; ISO:MGI.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Lipid droplet; Lipid metabolism; Lipoprotein; Methylation; NAD;
KW Oxidoreductase; Prenylation; Reference proteome.
FT CHAIN 1..476
FT /note="Aldehyde dehydrogenase family 3 member B2"
FT /id="PRO_0000436528"
FT PROPEP 477..479
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:25286108"
FT /id="PRO_0000436529"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT MOD_RES 476
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 476
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:25286108"
FT MUTAGEN 462
FT /note="W->A: Reduces lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:25286108"
FT MUTAGEN 469
FT /note="W->A: Reduces lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:25286108"
FT MUTAGEN 476
FT /note="C->S: Reduces lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:25286108"
SQ SEQUENCE 479 AA; 52983 MW; 50D1138DCE3D9CAD CRC64;
MSAAETGSEP SQGAGPSEAT LHSLREAFNA GRTRPTEFRT AQLRSLGRFL QENKELLQDA
LAKDVGKSGF ESDMSEIILC ENEVDLALKN LQTWMKDEPV STNLLTKLSS AFIRKEPFGL
VLIIAPWNYP VNLMIIPLVG AIAAGNCVVL KPSEISKNTE KVLAELLPQY LDQSCFAVML
GGPEETRQLL EHKFDYIFFT GSPRVGKIVM TAAAKHLTPI TLELGGKNPC YVDDNCDPQT
VANRVAWFRY FNAGQTCVAP DYILCSQEMQ ERLVPALQNS ITRFYGDNPQ TSPNLGRIIN
QKHFKRLQGL LGCGRVAIGG QSDEGERYIA PTVLVDVQET EPVMQEEIFG PILPLVTVRS
LDEAIEFINR REKPLALYAF SNNNQVVNQM LERTSSGGFG GNDGFLYLTL PALPLGGVGN
SGMGRYHGKF SFDTFSHHRA CLLRSPGMEK LNDLRYPPYG PWNQQLISWA IGSRSCTLL
