ID ASPDH_RAT Reviewed; 297 AA. AC Q5I0J9; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000305}; GN Name=Aspdh {ECO:0000312|RGD:1310111}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family. CC {ECO:0000305}. 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; BC088252; AAH88252.1; -; mRNA. DR RefSeq; NP_001009643.2; NM_001009643.2. DR AlphaFoldDB; Q5I0J9; -. DR SMR; Q5I0J9; -. DR STRING; 10116.ENSRNOP00000073291; -. DR PhosphoSitePlus; Q5I0J9; -. DR PaxDb; 10116-ENSRNOP00000063826; -. DR GeneID; 292875; -. DR KEGG; rno:292875; -. DR UCSC; RGD:1310111; rat. DR AGR; RGD:1310111; -. DR CTD; 554235; -. DR RGD; 1310111; Aspdh. DR VEuPathDB; HostDB:ENSRNOG00000019424; -. DR eggNOG; ENOG502QVGC; Eukaryota. DR InParanoid; Q5I0J9; -. DR OrthoDB; 2879851at2759; -. DR PhylomeDB; Q5I0J9; -. DR TreeFam; TF315092; -. DR PRO; PR:Q5I0J9; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000019424; Expressed in liver and 10 other cell types or tissues. DR ExpressionAtlas; Q5I0J9; baseline and differential. DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR002811; Asp_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1. DR Pfam; PF01958; Asp_DH_C; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q5I0J9; RN. PE 2: Evidence at transcript level; KW Phosphoprotein; Reference proteome. FT CHAIN 1..297 FT /note="Aspartate dehydrogenase domain-containing protein" FT /id="PRO_0000144902" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A6ND91" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A6ND91" SQ SEQUENCE 297 AA; 31260 MW; 572A02B436161734 CRC64; MDASMVPRVP HKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ LEDLTTLEER HPDLVVEVAH PKIIHESGVQ ILRHANLLVG SPSALADQTT ERQLLEASNH WGHTVFVARG ALWGCEDISR LDAAGGLQSL RVTMATHPDG FRLEGPLAAA HSSGPRTVLY EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELTGPQGPQ AAALPCTPTE RTQPSLALSL APLLLQPSGT AYWAAVSFPP DLGSASAEFP PLPLLSP //