Full text data of ALDH3B1
ALDH3B1
(ALDH7)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Aldehyde dehydrogenase family 3 member B1; 1.2.1.5 (Aldehyde dehydrogenase 7; Flags: Precursor)
Aldehyde dehydrogenase family 3 member B1; 1.2.1.5 (Aldehyde dehydrogenase 7; Flags: Precursor)
hRBCD
IPI00018031
IPI00018031 Aldehyde dehydrogenase 3B1 An aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H, Ethanol utilization; second step, aldehyde dehydrogenase activity, alcohol metabolism, lipid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00018031 Aldehyde dehydrogenase 3B1 An aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H, Ethanol utilization; second step, aldehyde dehydrogenase activity, alcohol metabolism, lipid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P43353
ID AL3B1_HUMAN Reviewed; 468 AA.
AC P43353; A3FMP9; Q53XL5; Q8N515; Q96CK8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B1;
DE EC=1.2.1.5;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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), AND FUNCTION.
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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, PALMITOYLATION AT CYS-463, AND
RP ISOPRENYLATION AT CYS-465.
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. Metabolizes also benzaldehyde. Low activity towards
CC acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not
CC metabolize short chain aldehydes. May use both NADP(+) and NAD(+)
CC as cofactors. May have a protective role against the cytotoxicity
CC induced by lipid peroxidation.
CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a
CC carboxylate + NAD(P)H.
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC ethanol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Primarily
CC in the plasma membrane as well as in some punctate structures in
CC the 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highest expression in kidney and lung.
CC -!- PTM: Dually lipadated in the C-terminus; prenylation occurs prior,
CC and is a prerequisite for palmitoylation, it is also required for
CC activity towards long-chain substrates.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; I38669; I38669.
DR RefSeq; NP_000685.1; NM_000694.2.
DR RefSeq; NP_001025181.1; NM_001030010.1.
DR RefSeq; NP_001154945.1; NM_001161473.1.
DR UniGene; Hs.523841; -.
DR ProteinModelPortal; P43353; -.
DR SMR; P43353; 4-448.
DR IntAct; P43353; 1.
DR STRING; 9606.ENSP00000007633; -.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; P43353; -.
DR DMDM; 1169285; -.
DR PaxDb; P43353; -.
DR PRIDE; P43353; -.
DR DNASU; 221; -.
DR GeneID; 221; -.
DR KEGG; hsa:221; -.
DR UCSC; uc001omz.3; human.
DR CTD; 221; -.
DR GeneCards; GC11P067776; -.
DR HGNC; HGNC:410; ALDH3B1.
DR MIM; 600466; gene.
DR neXtProt; NX_P43353; -.
DR PharmGKB; PA24699; -.
DR eggNOG; COG1012; -.
DR HOVERGEN; HBG050483; -.
DR InParanoid; P43353; -.
DR KO; K00129; -.
DR UniPathway; UPA00780; UER00768.
DR GeneWiki; ALDH3B1; -.
DR GenomeRNAi; 221; -.
DR NextBio; 894; -.
DR PRO; PR:P43353; -.
DR CleanEx; HS_ALDH3B1; -.
DR Genevestigator; P43353; -.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006066; P:alcohol metabolic process; TAS:ProtInc.
DR GO; GO:0046185; P:aldehyde catabolic process; IDA:MGI.
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 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.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR11699:SF15; PTHR11699:SF15; 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; Complete proteome;
KW Lipoprotein; Membrane; NAD; Oxidoreductase; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1 465 Aldehyde dehydrogenase family 3 member
FT B1.
FT /FTId=PRO_0000056481.
FT PROPEP 466 468 Removed in mature form (Probable).
FT /FTId=PRO_0000424193.
FT NP_BIND 188 193 NAD (By similarity).
FT ACT_SITE 210 210 By similarity.
FT ACT_SITE 244 244 By similarity.
FT MOD_RES 1 1 N-acetylmethionine.
FT LIPID 463 463 S-palmitoyl cysteine.
FT LIPID 465 465 S-farnesyl cysteine.
FT VAR_SEQ 55 91 Missing (in isoform 2).
FT /FTId=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
//
ID AL3B1_HUMAN Reviewed; 468 AA.
AC P43353; A3FMP9; Q53XL5; Q8N515; Q96CK8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B1;
DE EC=1.2.1.5;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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), AND FUNCTION.
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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, PALMITOYLATION AT CYS-463, AND
RP ISOPRENYLATION AT CYS-465.
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. Metabolizes also benzaldehyde. Low activity towards
CC acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not
CC metabolize short chain aldehydes. May use both NADP(+) and NAD(+)
CC as cofactors. May have a protective role against the cytotoxicity
CC induced by lipid peroxidation.
CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a
CC carboxylate + NAD(P)H.
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC ethanol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Primarily
CC in the plasma membrane as well as in some punctate structures in
CC the 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highest expression in kidney and lung.
CC -!- PTM: Dually lipadated in the C-terminus; prenylation occurs prior,
CC and is a prerequisite for palmitoylation, it is also required for
CC activity towards long-chain substrates.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; I38669; I38669.
DR RefSeq; NP_000685.1; NM_000694.2.
DR RefSeq; NP_001025181.1; NM_001030010.1.
DR RefSeq; NP_001154945.1; NM_001161473.1.
DR UniGene; Hs.523841; -.
DR ProteinModelPortal; P43353; -.
DR SMR; P43353; 4-448.
DR IntAct; P43353; 1.
DR STRING; 9606.ENSP00000007633; -.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; P43353; -.
DR DMDM; 1169285; -.
DR PaxDb; P43353; -.
DR PRIDE; P43353; -.
DR DNASU; 221; -.
DR GeneID; 221; -.
DR KEGG; hsa:221; -.
DR UCSC; uc001omz.3; human.
DR CTD; 221; -.
DR GeneCards; GC11P067776; -.
DR HGNC; HGNC:410; ALDH3B1.
DR MIM; 600466; gene.
DR neXtProt; NX_P43353; -.
DR PharmGKB; PA24699; -.
DR eggNOG; COG1012; -.
DR HOVERGEN; HBG050483; -.
DR InParanoid; P43353; -.
DR KO; K00129; -.
DR UniPathway; UPA00780; UER00768.
DR GeneWiki; ALDH3B1; -.
DR GenomeRNAi; 221; -.
DR NextBio; 894; -.
DR PRO; PR:P43353; -.
DR CleanEx; HS_ALDH3B1; -.
DR Genevestigator; P43353; -.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006066; P:alcohol metabolic process; TAS:ProtInc.
DR GO; GO:0046185; P:aldehyde catabolic process; IDA:MGI.
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 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.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR11699:SF15; PTHR11699:SF15; 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; Complete proteome;
KW Lipoprotein; Membrane; NAD; Oxidoreductase; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1 465 Aldehyde dehydrogenase family 3 member
FT B1.
FT /FTId=PRO_0000056481.
FT PROPEP 466 468 Removed in mature form (Probable).
FT /FTId=PRO_0000424193.
FT NP_BIND 188 193 NAD (By similarity).
FT ACT_SITE 210 210 By similarity.
FT ACT_SITE 244 244 By similarity.
FT MOD_RES 1 1 N-acetylmethionine.
FT LIPID 463 463 S-palmitoyl cysteine.
FT LIPID 465 465 S-farnesyl cysteine.
FT VAR_SEQ 55 91 Missing (in isoform 2).
FT /FTId=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
//
MIM
600466
*RECORD*
*FIELD* NO
600466
*FIELD* TI
*600466 ALDEHYDE DEHYDROGENASE 3 FAMILY, MEMBER B1; ALDH3B1
;;ALDEHYDE DEHYDROGENASE 7; ALDH7;;
read moreACETALDEHYDE DEHYDROGENASE 7
*FIELD* TX
The aldehyde dehydrogenases are a family of isozymes that may play a
major role in the detoxification of aldehydes generated by alcohol
metabolism and lipid peroxidation. Hsu et al. (1994) reported the
cloning and sequencing of a cDNA encoding a new human ALDH, designated
ALDH7. Degenerate oligodeoxyribonucleotides derived from conserved
regions of known ALDH cDNAs amplified a 408-bp product from human kidney
total RNA by the reverse transcription-PCR procedure. This PCR product
was subcloned, selected, and used as a probe to screen a human kidney
cDNA library. The full-length human kidney cDNA of ALDH7 is 2,791 bp
long and contains an open reading frame encoding 468 amino acids. The
deduced sequence of ALDH7 was longer than that of human stomach ALDH3
(100660) by 15 amino acids at the C terminus. The degree of identity
between the 2 isozymes was 52% with a positional alignment of 453 amino
acids. Northern blot analysis demonstrated that lung is another major
tissue expressing ALDH7.
Hsu et al. (1997) determined the structure of the ALDH7 and ALDH8
(601917) genes. The ALDH7 gene spans about 20 kb of genomic DNA and is
composed of 9 coding exons. The ALDH8 gene is over 10 kb in length and
consists of at least 10 exons. The ALDH8 gene contains an in-frame stop
codon at the seventeenth codon position from the first initiator Met.
The coding region of the ALDH7 gene shows about 86% nucleotide identity
with the corresponding region of the ALDH8 gene. The numbers and
positions of the introns of the 2 genes are conserved, suggesting that
gene duplication is involved in the expansion of the ALDH gene family.
The human ALDH7 and ALDH8 genes have a close evolutionary relationship
with human ALDH3.
The International Radiation Hybrid Mapping Consortium mapped the ALDH7
gene to chromosome 11 (TMAP RH69713).
*FIELD* RF
1. Hsu, L. C.; Chang, W.-C.; Yoshida, A.: Human aldehyde dehydrogenase
genes, ALDH7 and ALDH8: genomic organization and gene structure comparison. Gene 189:
89-94, 1997.
2. Hsu, L. C.; Chang, W.-C.; Yoshida, A.: Cloning of a cDNA encoding
human ALDH7, a new member of the aldehyde dehydrogenase family. Gene 151:
285-289, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/2/2001
Victor A. McKusick - updated: 7/2/1997
*FIELD* CD
Victor A. McKusick: 3/23/1995
*FIELD* ED
carol: 04/03/2001
joanna: 4/2/2001
dkim: 7/17/1998
dkim: 6/30/1998
terry: 6/4/1998
mark: 7/2/1997
jenny: 7/1/1997
jamie: 5/29/1997
mark: 3/24/1995
mark: 3/23/1995
*RECORD*
*FIELD* NO
600466
*FIELD* TI
*600466 ALDEHYDE DEHYDROGENASE 3 FAMILY, MEMBER B1; ALDH3B1
;;ALDEHYDE DEHYDROGENASE 7; ALDH7;;
read moreACETALDEHYDE DEHYDROGENASE 7
*FIELD* TX
The aldehyde dehydrogenases are a family of isozymes that may play a
major role in the detoxification of aldehydes generated by alcohol
metabolism and lipid peroxidation. Hsu et al. (1994) reported the
cloning and sequencing of a cDNA encoding a new human ALDH, designated
ALDH7. Degenerate oligodeoxyribonucleotides derived from conserved
regions of known ALDH cDNAs amplified a 408-bp product from human kidney
total RNA by the reverse transcription-PCR procedure. This PCR product
was subcloned, selected, and used as a probe to screen a human kidney
cDNA library. The full-length human kidney cDNA of ALDH7 is 2,791 bp
long and contains an open reading frame encoding 468 amino acids. The
deduced sequence of ALDH7 was longer than that of human stomach ALDH3
(100660) by 15 amino acids at the C terminus. The degree of identity
between the 2 isozymes was 52% with a positional alignment of 453 amino
acids. Northern blot analysis demonstrated that lung is another major
tissue expressing ALDH7.
Hsu et al. (1997) determined the structure of the ALDH7 and ALDH8
(601917) genes. The ALDH7 gene spans about 20 kb of genomic DNA and is
composed of 9 coding exons. The ALDH8 gene is over 10 kb in length and
consists of at least 10 exons. The ALDH8 gene contains an in-frame stop
codon at the seventeenth codon position from the first initiator Met.
The coding region of the ALDH7 gene shows about 86% nucleotide identity
with the corresponding region of the ALDH8 gene. The numbers and
positions of the introns of the 2 genes are conserved, suggesting that
gene duplication is involved in the expansion of the ALDH gene family.
The human ALDH7 and ALDH8 genes have a close evolutionary relationship
with human ALDH3.
The International Radiation Hybrid Mapping Consortium mapped the ALDH7
gene to chromosome 11 (TMAP RH69713).
*FIELD* RF
1. Hsu, L. C.; Chang, W.-C.; Yoshida, A.: Human aldehyde dehydrogenase
genes, ALDH7 and ALDH8: genomic organization and gene structure comparison. Gene 189:
89-94, 1997.
2. Hsu, L. C.; Chang, W.-C.; Yoshida, A.: Cloning of a cDNA encoding
human ALDH7, a new member of the aldehyde dehydrogenase family. Gene 151:
285-289, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/2/2001
Victor A. McKusick - updated: 7/2/1997
*FIELD* CD
Victor A. McKusick: 3/23/1995
*FIELD* ED
carol: 04/03/2001
joanna: 4/2/2001
dkim: 7/17/1998
dkim: 6/30/1998
terry: 6/4/1998
mark: 7/2/1997
jenny: 7/1/1997
jamie: 5/29/1997
mark: 3/24/1995
mark: 3/23/1995