AL3B3_MOUSE
ID AL3B3_MOUSE Reviewed; 479 AA.
AC J3QMK6; Q9D9K6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Aldehyde dehydrogenase family 3 member B3 {ECO:0000312|MGI:MGI:1920708};
DE EC=1.2.1.3 {ECO:0000269|PubMed:25286108};
DE Flags: Precursor;
GN Name=Aldh3b3 {ECO:0000312|MGI:MGI:1920708};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:BAB24748.1}
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB24748.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAB24748.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF 462-ARG-ARG-463, AND ISOPRENYLATION AT CYS-476.
RX PubMed=25286108; DOI=10.1042/bj20140624;
RA Kitamura T., Takagi S., Naganuma T., Kihara A.;
RT "Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via
RT two C-terminal tryptophan residues and lipid modification.";
RL Biochem. J. 465:79-87(2015).
CC -!- FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty
CC acids. {ECO:0000269|PubMed:25286108}.
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:0000269|PubMed:25286108};
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:25286108};
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:25286108};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108};
CC Lipid-anchor {ECO:0000305|PubMed:25286108}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, kidney, small intestine,
CC spleen, white adipose tissue, liver and lung.
CC {ECO:0000269|PubMed:25286108}.
CC -!- PTM: Geranylgeranylation is important for membrane localization and
CC enzyme activity. {ECO:0000269|PubMed:25286108}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|PIRNR:PIRNR036492}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24748.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK006803; BAB24748.1; ALT_SEQ; mRNA.
DR CCDS; CCDS57128.1; -.
DR RefSeq; NP_082821.2; NM_028545.2.
DR AlphaFoldDB; J3QMK6; -.
DR SMR; J3QMK6; -.
DR IntAct; J3QMK6; 1.
DR STRING; 10090.ENSMUSP00000136334; -.
DR SwissLipids; SLP:000001744; -.
DR iPTMnet; J3QMK6; -.
DR PhosphoSitePlus; J3QMK6; -.
DR jPOST; J3QMK6; -.
DR MaxQB; J3QMK6; -.
DR PaxDb; J3QMK6; -.
DR PeptideAtlas; J3QMK6; -.
DR PRIDE; J3QMK6; -.
DR DNASU; 73458; -.
DR Ensembl; ENSMUST00000179433; ENSMUSP00000136334; ENSMUSG00000037263.
DR GeneID; 73458; -.
DR KEGG; mmu:73458; -.
DR UCSC; uc029tql.1; mouse.
DR CTD; 73458; -.
DR MGI; MGI:1920708; Aldh3b3.
DR VEuPathDB; HostDB:ENSMUSG00000037263; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000155904; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; J3QMK6; -.
DR OMA; RWAMRSH; -.
DR OrthoDB; 646662at2759; -.
DR PhylomeDB; J3QMK6; -.
DR TreeFam; TF314264; -.
DR BRENDA; 1.2.1.48; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 73458; 3 hits in 77 CRISPR screens.
DR PRO; PR:J3QMK6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; J3QMK6; protein.
DR Bgee; ENSMUSG00000037263; Expressed in granulocyte and 40 other tissues.
DR ExpressionAtlas; J3QMK6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
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 Cell membrane; Lipoprotein; Membrane; NAD; Oxidoreductase; Prenylation;
KW Reference proteome.
FT CHAIN 1..479
FT /note="Aldehyde dehydrogenase family 3 member B3"
FT /id="PRO_0000436530"
FT PROPEP 477..479
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:25286108"
FT /id="PRO_0000436531"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT LIPID 476
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:25286108"
FT MUTAGEN 462..463
FT /note="RR->AA: Reduces membrane localization."
FT /evidence="ECO:0000269|PubMed:25286108"
SQ SEQUENCE 479 AA; 53120 MW; B8C2D0C2652B4F5D CRC64;
MSTKGKHPRA DQGTDPFEEK LQRLKEAFNT GKTKTAKFRA EQLQSLGRFL QDNSKQLHDA
LDGDLGKSGF ESDMSEIILC ENEVDLALKN LQTWMKDEPV STNLLTKLST AFIRKEPFGL
VLIIAPWNYP VNLMIIPLVG AIAAGNCVVL KPSEISKNTE KVLAELLPQY LDQSCFAVML
GGPEETGQLL EHKFDYIFFT GSPRVGKIVM TAAAKHLTPI TLELGGKNPC YVDDNCDPQT
VANRVAWFRY FNAGQTCVAP DYILCSQEMQ EQLVPALQNA ITRFYGDNPQ TSPNLGRIIN
QKHFKRLQGL LGCGRVAIGG QSDEGERYIA PTVLVDVQET EPVMQEEIFG PILPLVTVRS
LDEAIEFMNQ REKPLALYAY SNNAEVIKQV LARTSSGGFC GNDGFMYMTL SSLPFGGVGS
SGMGRYHGKF SFDTFSNQRA CLLSCPGMEK LNGLRYPPYS PRRQQLLRWA IGSESCTLL
