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   27-MAR-2024, entry version 193.
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}.
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; 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.ENSP00000501254; -.
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; 9606-ENSP00000255084; -.
DR   PeptideAtlas; P48448; -.
DR   ProteomicsDB; 55892; -.
DR   Pumba; P48448; -.
DR   Antibodypedia; 30491; 237 antibodies from 33 providers.
DR   DNASU; 222; -.
DR   Ensembl; ENST00000349015.7; ENSP00000255084.3; ENSG00000132746.16.
DR   Ensembl; ENST00000530069.6; ENSP00000431595.1; ENSG00000132746.16.
DR   Ensembl; ENST00000673966.2; ENSP00000501254.1; ENSG00000132746.16.
DR   MANE-Select; ENST00000673966.2; ENSP00000501254.1; NM_001393402.2; NP_001380331.1.
DR   UCSC; uc001omr.4; human.
DR   AGR; HGNC:411; -.
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; DAFSHTR; -.
DR   OrthoDB; 606537at2759; -.
DR   PhylomeDB; P48448; -.
DR   TreeFam; TF314264; -.
DR   PathwayCommons; P48448; -.
DR   Reactome; R-HSA-428157; Sphingolipid metabolism.
DR   SignaLink; P48448; -.
DR   UniPathway; UPA00780; UER00768.
DR   BioGRID-ORCS; 222; 17 hits in 1156 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 113 other cell types or tissues.
DR   ExpressionAtlas; P48448; baseline and differential.
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; IBA:GO_Central.
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:0006665; P:sphingolipid metabolic process; TAS:Reactome.
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:SF6; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER B2; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; P48448; HS.
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
//