AL3B1_MOUSE
ID AL3B1_MOUSE Reviewed; 468 AA.
AC Q80VQ0; Q63ZW3; Q8VHW0; Q9CW05;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B1;
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P43353};
DE EC=1.2.1.5 {ECO:0000269|PubMed:25286108};
DE EC=1.2.1.7 {ECO:0000250|UniProtKB:P43353};
DE AltName: Full=Aldehyde dehydrogenase 7;
DE Flags: Precursor;
GN Name=Aldh3b1; Synonyms=Aldh7;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-468.
RA Vasiliou V., Pappa A., Manzer R.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-468.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17382292; DOI=10.1016/j.bbrc.2007.03.046;
RA Marchitti S.A., Orlicky D.J., Vasiliou V.;
RT "Expression and initial characterization of human ALDH3B1.";
RL Biochem. Biophys. Res. Commun. 356:792-798(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ISOPRENYLATION,
RP PALMITOYLATION AT CYS-462 AND CYS-463, AND MUTAGENESIS OF CYS-462; CYS-463
RP AND 462-CYS-SER-463.
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 saturated and unsaturated
CC aldehydes (PubMed:25286108). Metabolizes also benzaldehyde (By
CC similarity). Low activity towards acetaldehyde and 3,4-
CC dihydroxyphenylacetaldehyde (By similarity). May not metabolize short
CC chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor
CC (By similarity). May have a protective role against the cytotoxicity
CC induced by lipid peroxidation (By similarity).
CC {ECO:0000250|UniProtKB:P43353, 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=1.2.1.5;
CC Evidence={ECO:0000269|PubMed:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.5;
CC Evidence={ECO:0000250|UniProtKB:P43353};
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:17382292,
CC ECO:0000269|PubMed:25286108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate;
CC Xref=Rhea:RHEA:59904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NADP(+) = benzoate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:21660, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.7;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NADP(+) = 2 H(+) + hexanoate + NADPH;
CC Xref=Rhea:RHEA:59908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NADP(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:59912, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenal + H2O + NADP(+) = (2E)-octenoate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:59916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748,
CC ChEBI:CHEBI:143526; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenal + H2O + NAD(+) = (2E)-octenoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:59920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:61748,
CC ChEBI:CHEBI:143526; Evidence={ECO:0000250|UniProtKB:P43353};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108};
CC Lipid-anchor {ECO:0000269|PubMed:25286108}. Note=Primarily in the
CC plasma membrane as well as in some punctate structures in the
CC cytoplasm. {ECO:0000269|PubMed:25286108}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and liver. In brain is
CC expressed at moderate levels in cortex, striatum and hippocampus, and
CC at lower levels in brainstem and cerebellum.
CC {ECO:0000269|PubMed:17382292}.
CC -!- PTM: Dually lipidated in the C-terminus; prenylation occurs prior to,
CC and is a prerequisite for palmitoylation. It is also required for
CC activity towards long-chain substrates. {ECO:0000269|PubMed:25286108}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC046597; AAH46597.1; -; mRNA.
DR EMBL; BC082792; AAH82792.1; -; mRNA.
DR EMBL; AF362571; AAL56246.1; -; mRNA.
DR EMBL; AK005615; BAB24152.2; -; mRNA.
DR CCDS; CCDS29403.1; -.
DR RefSeq; NP_080592.2; NM_026316.2.
DR RefSeq; XP_006531893.1; XM_006531830.3.
DR AlphaFoldDB; Q80VQ0; -.
DR SMR; Q80VQ0; -.
DR BioGRID; 212369; 1.
DR IntAct; Q80VQ0; 1.
DR STRING; 10090.ENSMUSP00000056276; -.
DR SwissLipids; SLP:000001742; -.
DR iPTMnet; Q80VQ0; -.
DR PhosphoSitePlus; Q80VQ0; -.
DR SwissPalm; Q80VQ0; -.
DR jPOST; Q80VQ0; -.
DR MaxQB; Q80VQ0; -.
DR PaxDb; Q80VQ0; -.
DR PRIDE; Q80VQ0; -.
DR ProteomicsDB; 282069; -.
DR Antibodypedia; 30512; 284 antibodies from 32 providers.
DR DNASU; 67689; -.
DR Ensembl; ENSMUST00000051803; ENSMUSP00000056276; ENSMUSG00000024885.
DR GeneID; 67689; -.
DR KEGG; mmu:67689; -.
DR UCSC; uc008fxq.1; mouse.
DR CTD; 221; -.
DR MGI; MGI:1914939; Aldh3b1.
DR VEuPathDB; HostDB:ENSMUSG00000024885; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000162915; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; Q80VQ0; -.
DR OMA; AWMKDQK; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; Q80VQ0; -.
DR TreeFam; TF314264; -.
DR BRENDA; 1.2.1.5; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 67689; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q80VQ0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80VQ0; protein.
DR Bgee; ENSMUSG00000024885; Expressed in granulocyte and 87 other tissues.
DR ExpressionAtlas; Q80VQ0; baseline and differential.
DR Genevisible; Q80VQ0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; 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:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0018477; F:benzaldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046185; P:aldehyde catabolic process; ISO:MGI.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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 Acetylation; Cell membrane; Lipid metabolism; Lipoprotein; Membrane;
KW Methylation; NAD; Oxidoreductase; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..465
FT /note="Aldehyde dehydrogenase family 3 member B1"
FT /id="PRO_0000056482"
FT PROPEP 466..468
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000424194"
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43353"
FT MOD_RES 465
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 462
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:25286108"
FT LIPID 463
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:25286108"
FT LIPID 465
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P43353"
FT MUTAGEN 462..463
FT /note="CC->SS: Abolishes palmitoylation."
FT /evidence="ECO:0000269|PubMed:25286108"
FT MUTAGEN 462
FT /note="C->S: Reduces palmitoylation."
FT /evidence="ECO:0000269|PubMed:25286108"
FT MUTAGEN 463
FT /note="C->S: Reduces palmitoylation."
FT /evidence="ECO:0000269|PubMed:25286108"
SQ SEQUENCE 468 AA; 52292 MW; 715B01070A3F7E23 CRC64;
MDSFEDKLQQ LREAFKEGRT RSAEFRAAQL QGLSHFLRDN KQQLQEALAQ DLHKSAFEAE
VSEIAISQAE VDLALRNLRS WMKDEKVSKN LATQLDSAFI RKEPFGLVLI IVPWNYPINL
TLVPLVGAIA AGNCVVLKPS EISKATEKIL AEVLPRYLDQ SCFTVVLGGR QETGQLLEHK
FDYIFFTGNA YVGKIVMAAA AKHLTPITLE LGGKNPCYVD DNCDPQIVAN RVAWFRYFNA
GQTCVAPDYI LCSQEMQERL VPALQNAITR FYGDNPQTSP NLGRIINQKH FKRLQGLLGC
GRVAIGGQSD EGERYIAPTV LVDVQETEPV MQEEIFGPIL PLVTVRSLDE AIEFMNRREK
PLALYAFSKR SQVIKQVLAR TSSGGFCGND GFMHMTLSSL PFGGVGTSGM GRYHGKFSFD
TFSNQRACLL RSPGMEKIND LRYPPYSSRN LRVLLVAMEE RCCSCTLL
