ID H0ZCF8_TAEGU Unreviewed; 327 AA. AC H0ZCF8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-OCT-2022, entry version 65. DE RecName: Full=Alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074}; DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074}; GN Name=AKR1A1 {ECO:0000313|Ensembl:ENSTGUP00000008268}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae; OC Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008268, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000008268, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E., RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P., RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O., RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L., RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C., RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K., RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A., RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000008268} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00023978}; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC {ECO:0000256|ARBA:ARBA00007905}. 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 RefSeq; XP_002194532.1; XM_002194496.3. DR STRING; 59729.ENSTGUP00000008268; -. DR Ensembl; ENSTGUT00000008355.2; ENSTGUP00000008268.1; ENSTGUG00000007993.2. DR GeneID; 100220342; -. DR KEGG; tgu:100220342; -. DR CTD; 10327; -. DR GeneTree; ENSGT00940000156539; -. DR HOGENOM; CLU_023205_0_0_1; -. DR InParanoid; H0ZCF8; -. DR OMA; WRHPDEP; -. DR OrthoDB; 1016440at2759; -. DR TreeFam; TF106492; -. DR Proteomes; UP000007754; Chromosome 8. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl. DR GO; GO:0047941; F:glucuronolactone reductase activity; IEA:Ensembl. DR GO; GO:0047939; F:L-glucuronate reductase activity; IEA:Ensembl. DR GO; GO:0016657; F:oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor; IEA:Ensembl. DR GO; GO:0046185; P:aldehyde catabolic process; IEA:Ensembl. DR GO; GO:0110095; P:cellular detoxification of aldehyde; IEA:Ensembl. DR GO; GO:0042840; P:D-glucuronate catabolic process; IEA:Ensembl. DR GO; GO:0044597; P:daunorubicin metabolic process; IEA:Ensembl. DR GO; GO:0044598; P:doxorubicin metabolic process; IEA:Ensembl. DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IEA:Ensembl. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:Ensembl. DR CDD; cd19106; AKR_AKR1A1-4; 1. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR020471; AKR. DR InterPro; IPR044481; AKR1A. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR InterPro; IPR036812; NADP_OxRdtase_dom_sf. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 20..295 FT /note="Aldo_ket_red" FT /evidence="ECO:0000259|Pfam:PF00248" FT ACT_SITE 52 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2" FT SITE 82 FT /note="Lowers pKa of active site Tyr" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3" SQ SEQUENCE 327 AA; 37274 MW; 9D398CB27C58967F CRC64; MPATCDFITL HTGQKMPLVG LGTWKSDRGQ VKEAVKHALS VGYRHIDCAA AYSNEAEIGD AFQECVGPNK VIKREDLFVT SKLWNTKHHP EDVEPALRKT LGDMKLDYLD LYLMHWPHAF ERGDNLFPKN PDNTMRYDYI DYKDTWKAME KLVEKGLVKA IGLSNFNSRQ IDDVLSVATV KPAVLQVECH PYLAQNELIA HCQKRGLVVT AYSPLGSPDR MWKHPDEPVL LEEPGVKKIA EKYSKSPAQI VLRWQVQRKV VVIPKSVTPA RIQQNLQVFD FSLTEEEMSH IGSLNKNWRY IVPMITVDGK LVARDAGHPH YPFNDPY //