ID E9QH31_DANRE Unreviewed; 490 AA. AC E9QH31; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 2. DT 19-JAN-2022, entry version 65. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; GN Name=aldh3a2b {ECO:0000313|Ensembl:ENSDARP00000103212, GN ECO:0000313|ZFIN:ZDB-GENE-040912-103}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000103212, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000103212} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000103212}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000103212, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000103212, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492, CC ECO:0000256|RuleBase:RU003345}. 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; CU463284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001315147.1; NM_001328218.1. DR STRING; 7955.ENSDARP00000103212; -. DR PaxDb; E9QH31; -. DR PeptideAtlas; E9QH31; -. DR Ensembl; ENSDART00000114885; ENSDARP00000103212; ENSDARG00000029381. DR GeneID; 447920; -. DR KEGG; dre:447920; -. DR CTD; 447920; -. DR ZFIN; ZDB-GENE-040912-103; aldh3a2b. DR eggNOG; KOG2456; Eukaryota. DR GeneTree; ENSGT00940000165264; -. DR HOGENOM; CLU_005391_3_0_1; -. DR InParanoid; E9QH31; -. DR OMA; CDPSIQD; -. DR OrthoDB; 646662at2759; -. DR PhylomeDB; E9QH31; -. DR TreeFam; TF314264; -. DR Reactome; R-DRE-1660661; Sphingolipid de novo biosynthesis. DR Reactome; R-DRE-211945; Phase I - Functionalization of compounds. DR Reactome; R-DRE-389599; Alpha-oxidation of phytanate. DR Reactome; R-DRE-9603798; Class I peroxisomal membrane protein import. DR Reactome; R-DRE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR Reactome; R-DRE-9696270; RND2 GTPase cycle. DR Reactome; R-DRE-9696273; RND1 GTPase cycle. DR Proteomes; UP000000437; Chromosome 21. DR Bgee; ENSDARG00000029381; Expressed in intestine and 24 other tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central. 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR036492}; KW Proteomics identification {ECO:0007829|PeptideAtlas:E9QH31}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 470..488 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 5..426 FT /note="Aldedh" FT /evidence="ECO:0000259|Pfam:PF00171" FT COILED 30..50 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 210 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 244 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10008" SQ SEQUENCE 490 AA; 55060 MW; 081558B1890338EF CRC64; MSREQKAVER ARKAFFTGRS KSLEYRISQL KNLQRFMQER QKEIAEALKK DLKRSEFGTS LYETLGVESE INLALKKLKE WAAPRPVNKS LMTISDQVYI QPEPLGVVLI IGAWNYPWAV TVGPLVGAIA AGNAAVIKPS EVSAHTSKVM EEFLPLYLDK ELYPVVTGGV KETQELLKQR FDHIFYTGNG MVGKIIMEAA AKHLTPTTLE LGGKSPCYID KDCDLTIACR RIAWGKYSNC GQTCIAPDYI LCDPSIQDRV IEEIKKNIKE FYTENPQKCP DYGRIINQRH FKRLMSLMEG SSIAVSGEHN EAECYIAPTV LRDVKPDAKV MQEEIFGPLL PIVTVNSVDE AIKFINQRDK PLALYIFSSD KKLIDRMIAE TSSGGLMAND CLMHFSVSSL PFGGVGDSGM GRYHGKHGFD NLSHMRGVLL KQLKMEAVNK MRYPPHTADK LGWARFFIVR HVDFGSLGRM AMLALMVVFA AVIIQKYFTD //