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 02-SEP-2026, entry version 207. 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 AltName: Full=Long-chain fatty aldehyde dehydrogenase; DE EC=1.2.1.48 {ECO:0000269|PubMed:23721920}; DE AltName: Full=Medium-chain fatty aldehyde dehydrogenase; 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 fatty aldehydes generated in the plasma membrane into non-toxic fatty CC acids (PubMed:17382292, PubMed:23721920). May have a protective role CC against the cytotoxicity induced by lipid peroxidation CC (PubMed:17382292). Short-chain fatty aldehydes are not good substrates CC (PubMed:17382292). Can use both NADP(+) and NAD(+) as electron acceptor CC in vitro, however in vivo preference will depend on their tissue levels CC (PubMed:17382292). Low activity towards acetaldehyde and 3,4- CC dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). Able to CC metabolize aromatic aldehydes such as benzaldehyde to their acid form CC (PubMed:17382292). {ECO:0000269|PubMed:17382292, CC ECO:0000269|PubMed:23721920}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + NADP(+) + H2O = a carboxylate + NADPH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11889; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186; CC Evidence={ECO:0000269|PubMed:23721920, ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a long-chain fatty aldehyde + NAD(+) + H2O = a long-chain CC fatty acid + NADH + 2 H(+); Xref=Rhea:RHEA:10652, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17176, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57560, ChEBI:CHEBI:57945; EC=1.2.1.48; CC Evidence={ECO:0000269|PubMed:23721920}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10653; CC Evidence={ECO:0000269|PubMed:23721920}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a medium-chain fatty aldehyde + NAD(+) + H2O = a medium-chain CC fatty acid + NADH + 2 H(+); Xref=Rhea:RHEA:69763, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:59558, ChEBI:CHEBI:142621; CC Evidence={ECO:0000269|PubMed:17382292, ECO:0000269|PubMed:23721920}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69764; CC Evidence={ECO:0000269|PubMed:23721920, ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octanal + NAD(+) + H2O = octanoate + NADH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44101; CC Evidence={ECO:0000269|PubMed:23721920, ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=nonanal + NAD(+) + H2O = nonanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:69759, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32361, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:84268; Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69760; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoate + NADH + 2 H(+) = hexadecanal + NAD(+) + H2O; 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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33741; CC Evidence={ECO:0000269|PubMed:23721920}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-octenal + NAD(+) + H2O = (2E)-octenoate + NADH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59921; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-non-2-enal + NAD(+) + H2O = (E)-non-2-enoate + NADH + 2 CC H(+); Xref=Rhea:RHEA:69767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:142592, CC ChEBI:CHEBI:143908; Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69768; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-hydroxynon-2-enal + NAD(+) + H2O = (E)-4-hydroxynon-2- CC enoate + NADH + 2 H(+); Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920; CC Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexadecenal + NAD(+) + H2O = (E)-hexadec-2-enoate + NADH CC + 2 H(+); Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17585, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:72745; Evidence={ECO:0000269|PubMed:23721920}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36136; CC Evidence={ECO:0000269|PubMed:23721920}; CC -!- CATALYTIC ACTIVITY: CC Reaction=benzaldehyde + NAD(+) + H2O = benzoate + NADH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a medium-chain fatty aldehyde + NADP(+) + H2O = a medium-chain CC fatty acid + NADPH + 2 H(+); Xref=Rhea:RHEA:80815, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:59558, ChEBI:CHEBI:142621; CC Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80816; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexanal + NADP(+) + H2O = hexanoate + NADPH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59909; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octanal + NADP(+) + H2O = octanoate + NADPH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59905; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=nonanal + NADP(+) + H2O = nonanoate + NADPH + 2 H(+); CC Xref=Rhea:RHEA:80819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32361, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:84268; Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80820; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-octenal + NADP(+) + H2O = (2E)-octenoate + NADPH + 2 CC H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59917; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-non-2-enal + NADP(+) + H2O = (E)-non-2-enoate + NADPH + 2 CC H(+); Xref=Rhea:RHEA:60692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142592, CC ChEBI:CHEBI:143908; Evidence={ECO:0000269|PubMed:17382292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60693; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-hydroxynon-2-enal + NADP(+) + H2O = (E)-4-hydroxynon-2- CC enoate + NADPH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59913; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- CATALYTIC ACTIVITY: CC Reaction=benzaldehyde + NADP(+) + H2O = benzoate + NADPH + 2 H(+); 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21661; CC Evidence={ECO:0000305|PubMed:17382292}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for octanal {ECO:0000269|PubMed:23721920}; CC KM=45.6 uM for hexadecanal {ECO:0000269|PubMed:23721920}; CC KM=4.9 uM for trans-2-hexadecenal {ECO:0000269|PubMed:23721920}; CC Vmax=4.8 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; P48448: ALDH3B2; NbExp=3; IntAct=EBI-2558314, EBI-21868861; 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}. 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; 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_000694.4. [P43353-1] DR RefSeq; NP_001025181.1; NM_001030010.3. [P43353-2] DR RefSeq; NP_001154945.1; NM_001161473.3. [P43353-1] DR RefSeq; NP_001276987.1; NM_001290058.2. DR RefSeq; NP_001276988.1; NM_001290059.2. DR AlphaFoldDB; P43353; -. DR SMR; P43353; -. DR BioGRID; 106723; 154. DR FunCoup; P43353; 768. DR IntAct; P43353; 117. 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 jPOST; P43353; -. DR MassIVE; P43353; -. DR PaxDb; 9606-ENSP00000473990; -. DR PeptideAtlas; P43353; -. DR ProteomicsDB; 55614; -. [P43353-1] DR ProteomicsDB; 55615; -. [P43353-2] DR Pumba; P43353; -. DR Antibodypedia; 30512; 278 antibodies from 32 providers. DR DNASU; 221; -. DR Ensembl; ENST00000342456.11; ENSP00000473990.2; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000614849.4; ENSP00000478486.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000617288.4; ENSP00000481604.1; ENSG00000006534.18. [P43353-2] DR Ensembl; ENST00000894326.1; ENSP00000564385.1; ENSG00000006534.18. [P43353-2] DR Ensembl; ENST00000894327.1; ENSP00000564386.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894329.1; ENSP00000564388.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894331.1; ENSP00000564390.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894332.1; ENSP00000564391.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894333.1; ENSP00000564392.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894334.1; ENSP00000564393.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894335.1; ENSP00000564394.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894336.1; ENSP00000564395.1; ENSG00000006534.18. [P43353-1] DR Ensembl; ENST00000894337.1; ENSP00000564396.1; ENSG00000006534.18. [P43353-1] 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 AGR; HGNC:410; -. DR ClinPGx; PA24699; -. DR CTD; 221; -. DR DisGeNET; 221; -. DR GeneCards; ALDH3B1; -. DR HGNC; HGNC:410; ALDH3B1. DR HPA; ENSG00000006534; Low tissue specificity. DR MIM; 600466; gene. DR OpenTargets; ENSG00000006534; -. DR VEuPathDB; HostDB:ENSG00000006534; -. DR eggNOG; KOG2456; Eukaryota. DR GeneTree; ENSGT00940000162915; -. DR HOGENOM; CLU_005391_3_1_1; -. DR InParanoid; P43353; -. DR OMA; MKDQKVP; -. DR OrthoDB; 440325at2759; -. DR PAN-GO; P43353; 4 GO annotations based on evolutionary models. DR PhylomeDB; P43353; -. DR BRENDA; 1.2.1.5; 2681. DR PathwayCommons; P43353; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9845614; Sphingolipid catabolism. DR SignaLink; P43353; -. DR SIGNOR; P43353; -. DR UniPathway; UPA00780; UER00768. DR Agora; ENSG00000006534; -. DR BioGRID-ORCS; 221; 7 hits in 322 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 196 other cell types or tissues. DR ExpressionAtlas; P43353; baseline and differential. 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; IBA:GO_Central. 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: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:0050061; F:long-chain fatty aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0052814; F:medium-chain fatty aldehyde dehydrogenase (NAD+) activity; IEA:RHEA. 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: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:0030149; P:sphingolipid catabolic process; TAS:Reactome. DR CDD; cd07132; ALDH_F3AB; 1. DR FunFam; 3.40.309.10:FF:000003; Aldehyde dehydrogenase; 1. DR FunFam; 3.40.605.10:FF:000004; Aldehyde dehydrogenase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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:SF2; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER B1; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 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; Proteomics identification; 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 //