AL3B2_HUMAN
ID AL3B2_HUMAN Reviewed; 385 AA.
AC P48448; Q53Y98; Q8NAL5; Q96IB2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B2;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:E9Q3E1};
DE AltName: Full=Aldehyde dehydrogenase 8;
DE Flags: Precursor;
GN Name=ALDH3B2; Synonyms=ALDH8;
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], AND VARIANTS ASN-52; ARG-203; GLY-220 AND
RP ARG-361.
RC TISSUE=Salivary gland;
RX PubMed=7484374; DOI=10.1007/978-1-4615-1965-2_21;
RA Hsu L.C., Chang W.-C., Lin S.W., Yoshida A.;
RT "Cloning and characterization of genes encoding four additional human
RT aldehyde dehydrogenase isozymes.";
RL Adv. Exp. Med. Biol. 372:159-168(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-52; ARG-203; GLY-220 AND ARG-361,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Salivary gland;
RX PubMed=8890755; DOI=10.1016/0378-1119(96)00087-x;
RA Hsu L.C., Chang W.-C.;
RT "Sequencing and expression of the human ALDH8 encoding a new member of the
RT aldehyde dehydrogenase family.";
RL Gene 174:319-322(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-203; GLY-220 AND
RP TRP-276.
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-52; ARG-203;
RP GLY-220 AND ARG-361.
RC TISSUE=Placenta;
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].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-203; GLY-220 AND
RP TRP-276.
RC TISSUE=Placenta;
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).
CC -!- FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty
CC acids. {ECO:0000250|UniProtKB:E9Q3E1}.
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:E9Q3E1};
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:E9Q3E1};
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:E9Q3E1};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:E9Q3E1}.
CC -!- TISSUE SPECIFICITY: Salivary gland. {ECO:0000269|PubMed:8890755}.
CC -!- PTM: Geranylgeranylation is important for localization to lipid
CC droplets and enzyme activity. {ECO:0000250|UniProtKB:E9Q3E1}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U37519; AAA85441.1; -; mRNA.
DR EMBL; BT006810; AAP35456.1; -; mRNA.
DR EMBL; AK092464; BAC03897.1; -; mRNA.
DR EMBL; AP003385; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC007685; AAH07685.1; -; mRNA.
DR CCDS; CCDS31622.1; -.
DR PIR; JC5019; JC5019.
DR AlphaFoldDB; P48448; -.
DR SMR; P48448; -.
DR BioGRID; 106724; 32.
DR IntAct; P48448; 1.
DR STRING; 9606.ENSP00000255084; -.
DR ChEMBL; CHEMBL3542434; -.
DR DrugBank; DB09116; Calcium carbimide.
DR DrugBank; DB00157; NADH.
DR iPTMnet; P48448; -.
DR PhosphoSitePlus; P48448; -.
DR BioMuta; ALDH3B2; -.
DR DMDM; 288558849; -.
DR jPOST; P48448; -.
DR MassIVE; P48448; -.
DR MaxQB; P48448; -.
DR PaxDb; P48448; -.
DR PeptideAtlas; P48448; -.
DR PRIDE; P48448; -.
DR ProteomicsDB; 55892; -.
DR Antibodypedia; 30491; 225 antibodies from 33 providers.
DR DNASU; 222; -.
DR Ensembl; ENST00000349015.7; ENSP00000255084.3; ENSG00000132746.15.
DR Ensembl; ENST00000530069.6; ENSP00000431595.1; ENSG00000132746.15.
DR Ensembl; ENST00000673966.1; ENSP00000501254.1; ENSG00000132746.15.
DR MANE-Select; ENST00000673966.2; ENSP00000501254.1; NM_001393402.2; NP_001380331.1.
DR UCSC; uc001omr.4; human.
DR GeneCards; ALDH3B2; -.
DR HGNC; HGNC:411; ALDH3B2.
DR HPA; ENSG00000132746; Group enriched (breast, esophagus, skin, vagina).
DR MIM; 601917; gene.
DR neXtProt; NX_P48448; -.
DR OpenTargets; ENSG00000132746; -.
DR PharmGKB; PA24700; -.
DR VEuPathDB; HostDB:ENSG00000132746; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000155904; -.
DR HOGENOM; CLU_005391_3_2_1; -.
DR InParanoid; P48448; -.
DR OMA; AINIDVG; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; P48448; -.
DR TreeFam; TF314264; -.
DR PathwayCommons; P48448; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; P48448; -.
DR UniPathway; UPA00780; UER00768.
DR BioGRID-ORCS; 222; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; ALDH3B2; human.
DR GeneWiki; ALDH3B2; -.
DR GenomeRNAi; 222; -.
DR Pharos; P48448; Tbio.
DR PRO; PR:P48448; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P48448; protein.
DR Bgee; ENSG00000132746; Expressed in lower esophagus mucosa and 111 other tissues.
DR ExpressionAtlas; P48448; baseline and differential.
DR Genevisible; P48448; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
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; EXP:Reactome.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006066; P:alcohol metabolic process; TAS:ProtInc.
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; TAS:ProtInc.
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 SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW Lipid droplet; Lipid metabolism; Lipoprotein; Methylation; NAD;
KW Oxidoreductase; Prenylation; Reference proteome.
FT CHAIN 1..382
FT /note="Aldehyde dehydrogenase family 3 member B2"
FT /id="PRO_0000056484"
FT PROPEP 383..385
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:E9Q3E1"
FT /id="PRO_0000436532"
FT ACT_SITE 129
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT BINDING 107..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 382
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:E9Q3E1"
FT LIPID 382
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:E9Q3E1"
FT VARIANT 50
FT /note="A -> T (in dbSNP:rs3741178)"
FT /id="VAR_022058"
FT VARIANT 52
FT /note="S -> N (in dbSNP:rs1551888)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7484374, ECO:0000269|PubMed:8890755"
FT /id="VAR_058696"
FT VARIANT 203
FT /note="H -> R (in dbSNP:rs6591270)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7484374,
FT ECO:0000269|PubMed:8890755, ECO:0000269|Ref.3"
FT /id="VAR_058697"
FT VARIANT 220
FT /note="S -> G (in dbSNP:rs2447571)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7484374,
FT ECO:0000269|PubMed:8890755, ECO:0000269|Ref.3"
FT /id="VAR_058698"
FT VARIANT 276
FT /note="R -> W (in dbSNP:rs17856219)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_058699"
FT VARIANT 302
FT /note="S -> R (in dbSNP:rs4646826)"
FT /id="VAR_055699"
FT VARIANT 361
FT /note="H -> R (in dbSNP:rs1551886)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7484374, ECO:0000269|PubMed:8890755"
FT /id="VAR_058700"
FT CONFLICT 2
FT /note="K -> E (in Ref. 4; BAC03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..49
FT /note="ALA -> TLP (in Ref. 1; AAA85441 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="G -> V (in Ref. 4; BAC03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> R (in Ref. 1; AAA85441 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42635 MW; 418879E834C3F9C6 CRC64;
MKDEPRSTNL FMKLDSVFIW KEPFGLVLII APWNYPLNLT LVLLVGALAA GSCVVLKPSE
ISQGTEKVLA EVLPQYLDQS CFAVVLGGPQ ETGQLLEHKL DYIFFTGSPR VGKIVMTAAT
KHLTPVTLEL GGKNPCYVDD NCDPQTVANR VAWFCYFNAG QTCVAPDYVL CSPEMQERLL
PALQSTITRF YGDDPQSSPN LGHIINQKQF QRLRALLGCS RVAIGGQSNE SDRYIAPTVL
VDVQETEPVM QEEIFGPILP IVNVQSVDEA IKFINRQEKP LALYAFSNSS QVVNQMLERT
SSGSFGGNEG FTYISLLSVP FGGVGHSGMG RYHGKFTFDT FSHHRTCLLA PSGLEKLKEI
HYPPYTDWNQ QLLRWGMGSQ SCTLL
