ID H0ZCF8_TAEGU Unreviewed; 327 AA. AC H0ZCF8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 38. DE SubName: Full=Aldo-keto reductase family 1 member A1 {ECO:0000313|Ensembl:ENSTGUP00000008268}; 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; OC Estrildidae; 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., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA 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 -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTGUP00000008268}. 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; ABQF01031098; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002194532.1; XM_002194496.3. DR STRING; 59729.ENSTGUP00000008268; -. DR Ensembl; ENSTGUT00000008355; ENSTGUP00000008268; ENSTGUG00000007993. DR GeneID; 100220342; -. DR KEGG; tgu:100220342; -. DR CTD; 10327; -. DR eggNOG; KOG1577; Eukaryota. DR eggNOG; COG0656; LUCA. DR GeneTree; ENSGT00760000119041; -. DR InParanoid; H0ZCF8; -. DR KO; K00002; -. DR OMA; IHWPYAF; -. DR OrthoDB; EOG091G0D69; -. DR TreeFam; TF106492; -. DR Reactome; R-TGU-156590; Glutathione conjugation. DR Reactome; R-TGU-5661270; Catabolism of glucuronate to xylulose-5-phosphate. DR Proteomes; UP000007754; Chromosome 8. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl. DR GO; GO:0047939; F:L-glucuronate reductase activity; IEA:Ensembl. DR GO; GO:0046185; P:aldehyde catabolic process; IEA:Ensembl. DR GO; GO:0042840; P:D-glucuronate catabolic process; IEA:Ensembl. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:Ensembl. DR CDD; cd06660; Aldo_ket_red; 1. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 19 295 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. FT ACT_SITE 52 52 Proton donor. {ECO:0000256|PIRSR: FT PIRSR000097-1}. FT BINDING 115 115 Substrate. {ECO:0000256|PIRSR: FT PIRSR000097-2}. FT SITE 82 82 Lowers pKa of active site Tyr. FT {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 //