AL3B1_HUMAN
ID AL3B1_HUMAN Reviewed; 468 AA.
AC P43353; A3FMP9; Q53XL5; Q8N515; Q96CK8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B1;
DE EC=1.2.1.28 {ECO:0000269|PubMed:17382292};
DE EC=1.2.1.5 {ECO:0000269|PubMed:17382292, ECO:0000269|PubMed:23721920};
DE EC=1.2.1.7 {ECO:0000269|PubMed:17382292};
DE AltName: Full=Aldehyde dehydrogenase 7;
DE Flags: Precursor;
GN Name=ALDH3B1; Synonyms=ALDH7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=7828891; DOI=10.1016/0378-1119(94)90672-6;
RA Hsu L.C., Chang W.-C., Yoshida A.;
RT "Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde
RT dehydrogenase family.";
RL Gene 151:285-289(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Prostate;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, PALMITOYLATION AT CYS-463, ISOPRENYLATION
RP AT CYS-465, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=23721920; DOI=10.1016/j.bbalip.2013.05.007;
RA Kitamura T., Naganuma T., Abe K., Nakahara K., Ohno Y., Kihara A.;
RT "Substrate specificity, plasma membrane localization, and lipid
RT modification of the aldehyde dehydrogenase ALDH3B1.";
RL Biochim. Biophys. Acta 1831:1395-1401(2013).
CC -!- FUNCTION: Oxidizes medium and long chain saturated and unsaturated
CC aldehydes (PubMed:17382292, PubMed:23721920). Metabolizes also
CC benzaldehyde (PubMed:17382292). Low activity towards acetaldehyde and
CC 3,4-dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). May
CC not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+)
CC as electron acceptor (PubMed:17382292). May have a protective role
CC against the cytotoxicity induced by lipid peroxidation
CC (PubMed:17382292). {ECO:0000269|PubMed:17382292,
CC ECO:0000269|PubMed:23721920}.
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:0000269|PubMed:17382292};
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; Evidence={ECO:0000269|PubMed:17382292,
CC ECO:0000269|PubMed:23721920};
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:23721920};
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:23721920};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
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:0000269|PubMed:17382292};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for octanal {ECO:0000269|PubMed:23721920};
CC KM=45.6 uM for trans-2-hexadecenal {ECO:0000269|PubMed:23721920};
CC KM=4.9 uM for hexadecanal {ECO:0000269|PubMed:23721920};
CC Vmax=4.9 pmol/min/ng enzyme with trans-2-hexadecenal
CC {ECO:0000269|PubMed:23721920};
CC Vmax=5 pmol/min/ng enzyme with octanal {ECO:0000269|PubMed:23721920};
CC Vmax=9.7 pmol/min/ng enzyme with hexadecanal
CC {ECO:0000269|PubMed:23721920};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- INTERACTION:
CC P43353; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2558314, EBI-3867333;
CC P43353; Q15323: KRT31; NbExp=3; IntAct=EBI-2558314, EBI-948001;
CC P43353; O76011: KRT34; NbExp=3; IntAct=EBI-2558314, EBI-1047093;
CC P43353; Q6A162: KRT40; NbExp=3; IntAct=EBI-2558314, EBI-10171697;
CC P43353; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-2558314, EBI-11959885;
CC P43353; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2558314, EBI-11749135;
CC P43353; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-2558314, EBI-10172150;
CC P43353; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2558314, EBI-10172290;
CC P43353; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-2558314, EBI-10171774;
CC P43353; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2558314, EBI-10172052;
CC P43353; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-2558314, EBI-11953334;
CC P43353; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-2558314, EBI-3957694;
CC P43353; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-2558314, EBI-3958099;
CC P43353; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2558314, EBI-10172526;
CC P43353; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2558314, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23721920};
CC Lipid-anchor {ECO:0000269|PubMed:23721920}. Note=Primarily in the
CC plasma membrane as well as in some punctate structures in the
CC cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43353-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43353-2; Sequence=VSP_014040;
CC -!- TISSUE SPECIFICITY: Highest expression in kidney and lung.
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:23721920}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U10868; AAA83428.1; -; mRNA.
DR EMBL; EF411198; ABN58743.1; -; mRNA.
DR EMBL; BT009832; AAP88834.1; -; mRNA.
DR EMBL; AK291505; BAF84194.1; -; mRNA.
DR EMBL; CH471076; EAW74680.1; -; Genomic_DNA.
DR EMBL; BC013584; AAH13584.1; -; mRNA.
DR EMBL; BC014168; AAH14168.2; -; mRNA.
DR EMBL; BC033099; AAH33099.1; -; mRNA.
DR CCDS; CCDS73335.1; -. [P43353-1]
DR CCDS; CCDS73336.1; -. [P43353-2]
DR PIR; I38669; I38669.
DR RefSeq; NP_000685.1; NM_000694.3. [P43353-1]
DR RefSeq; NP_001025181.1; NM_001030010.2. [P43353-2]
DR RefSeq; NP_001154945.1; NM_001161473.2. [P43353-1]
DR RefSeq; NP_001276987.1; NM_001290058.1.
DR RefSeq; NP_001276988.1; NM_001290059.1.
DR AlphaFoldDB; P43353; -.
DR SMR; P43353; -.
DR BioGRID; 106723; 152.
DR IntAct; P43353; 37.
DR MINT; P43353; -.
DR STRING; 9606.ENSP00000473990; -.
DR ChEMBL; CHEMBL3542434; -.
DR DrugBank; DB00157; NADH.
DR GlyGen; P43353; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P43353; -.
DR PhosphoSitePlus; P43353; -.
DR SwissPalm; P43353; -.
DR BioMuta; ALDH3B1; -.
DR DMDM; 1169285; -.
DR EPD; P43353; -.
DR jPOST; P43353; -.
DR MassIVE; P43353; -.
DR MaxQB; P43353; -.
DR PeptideAtlas; P43353; -.
DR PRIDE; P43353; -.
DR ProteomicsDB; 55614; -. [P43353-1]
DR ProteomicsDB; 55615; -. [P43353-2]
DR Antibodypedia; 30512; 284 antibodies from 32 providers.
DR DNASU; 221; -.
DR Ensembl; ENST00000342456.11; ENSP00000473990.2; ENSG00000006534.17. [P43353-1]
DR Ensembl; ENST00000614849.4; ENSP00000478486.1; ENSG00000006534.17. [P43353-1]
DR Ensembl; ENST00000617288.4; ENSP00000481604.1; ENSG00000006534.17. [P43353-2]
DR GeneID; 221; -.
DR KEGG; hsa:221; -.
DR MANE-Select; ENST00000342456.11; ENSP00000473990.2; NM_000694.4; NP_000685.1.
DR UCSC; uc031xti.2; human. [P43353-1]
DR CTD; 221; -.
DR DisGeNET; 221; -.
DR GeneCards; ALDH3B1; -.
DR HGNC; HGNC:410; ALDH3B1.
DR HPA; ENSG00000006534; Tissue enhanced (bone).
DR MIM; 600466; gene.
DR neXtProt; NX_P43353; -.
DR OpenTargets; ENSG00000006534; -.
DR PharmGKB; PA24699; -.
DR VEuPathDB; HostDB:ENSG00000006534; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000162915; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; P43353; -.
DR OMA; AWMKDQK; -.
DR PhylomeDB; P43353; -.
DR BRENDA; 1.2.1.5; 2681.
DR PathwayCommons; P43353; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P43353; -.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 221; 7 hits in 268 CRISPR screens.
DR ChiTaRS; ALDH3B1; human.
DR GeneWiki; ALDH3B1; -.
DR GenomeRNAi; 221; -.
DR Pharos; P43353; Tbio.
DR PRO; PR:P43353; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P43353; protein.
DR Bgee; ENSG00000006534; Expressed in bronchial epithelial cell and 195 other tissues.
DR ExpressionAtlas; P43353; baseline and differential.
DR Genevisible; P43353; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:ProtInc.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA: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:0006066; P:alcohol metabolic process; TAS:ProtInc.
DR GO; GO:0046185; P:aldehyde catabolic process; IDA:MGI.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
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; Alternative splicing; Cell membrane; Lipid metabolism;
KW Lipoprotein; Membrane; Methylation; NAD; Oxidoreductase; Palmitate;
KW Prenylation; Reference proteome.
FT CHAIN 1..465
FT /note="Aldehyde dehydrogenase family 3 member B1"
FT /id="PRO_0000056481"
FT PROPEP 466..468
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000424193"
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:0007744|PubMed:22814378"
FT MOD_RES 465
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 463
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23721920"
FT LIPID 465
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:23721920"
FT VAR_SEQ 55..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014040"
SQ SEQUENCE 468 AA; 51840 MW; 30BEEB982395D2F7 CRC64;
MDPLGDTLRR LREAFHAGRT RPAEFRAAQL QGLGRFLQEN KQLLHDALAQ DLHKSAFESE
VSEVAISQGE VTLALRNLRA WMKDERVPKN LATQLDSAFI RKEPFGLVLI IAPWNYPLNL
TLVPLVGALA AGNCVVLKPS EISKNVEKIL AEVLPQYVDQ SCFAVVLGGP QETGQLLEHR
FDYIFFTGSP RVGKIVMTAA AKHLTPVTLE LGGKNPCYVD DNCDPQTVAN RVAWFRYFNA
GQTCVAPDYV LCSPEMQERL LPALQSTITR FYGDDPQSSP NLGRIINQKQ FQRLRALLGC
GRVAIGGQSD ESDRYIAPTV LVDVQEMEPV MQEEIFGPIL PIVNVQSLDE AIEFINRREK
PLALYAFSNS SQVVKRVLTQ TSSGGFCGND GFMHMTLASL PFGGVGASGM GRYHGKFSFD
TFSHHRACLL RSPGMEKLNA LRYPPQSPRR LRMLLVAMEA QGCSCTLL
