DHYS_MOUSE
ID DHYS_MOUSE Reviewed; 369 AA.
AC Q3TXU5; E9QM48;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=Dhps;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine
CC and the subsequent transfer of the butylamine moiety of spermidine to
CC the epsilon-amino group of a critical lysine residue of the eIF-5A
CC precursor protein to form the intermediate deoxyhypusine residue. This
CC is the first step of the post-translational modification of that lysine
CC into an unusual amino acid residue named hypusine. Hypusination is
CC unique to mature eIF-5A factor and is essential for its function.
CC {ECO:0000250|UniProtKB:P49366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-
CC deoxyhypusine + propane-1,3-diamine; Xref=Rhea:RHEA:33299, Rhea:RHEA-
CC COMP:10143, Rhea:RHEA-COMP:10144, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:82657; EC=2.5.1.46;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; AK159104; BAE34820.1; -; mRNA.
DR EMBL; AC163703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS22492.1; -.
DR RefSeq; NP_001034603.1; NM_001039514.1.
DR AlphaFoldDB; Q3TXU5; -.
DR SMR; Q3TXU5; -.
DR BioGRID; 237030; 16.
DR STRING; 10090.ENSMUSP00000077733; -.
DR iPTMnet; Q3TXU5; -.
DR PhosphoSitePlus; Q3TXU5; -.
DR EPD; Q3TXU5; -.
DR MaxQB; Q3TXU5; -.
DR PaxDb; Q3TXU5; -.
DR PeptideAtlas; Q3TXU5; -.
DR PRIDE; Q3TXU5; -.
DR ProteomicsDB; 279538; -.
DR Antibodypedia; 1964; 321 antibodies from 31 providers.
DR DNASU; 330817; -.
DR Ensembl; ENSMUST00000078665; ENSMUSP00000077733; ENSMUSG00000060038.
DR GeneID; 330817; -.
DR KEGG; mmu:330817; -.
DR UCSC; uc009mpf.1; mouse.
DR CTD; 1725; -.
DR MGI; MGI:2683592; Dhps.
DR VEuPathDB; HostDB:ENSMUSG00000060038; -.
DR eggNOG; KOG2924; Eukaryota.
DR GeneTree; ENSGT00390000008063; -.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; Q3TXU5; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 883558at2759; -.
DR PhylomeDB; Q3TXU5; -.
DR TreeFam; TF300625; -.
DR BRENDA; 2.5.1.46; 3474.
DR Reactome; R-MMU-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR BioGRID-ORCS; 330817; 33 hits in 77 CRISPR screens.
DR ChiTaRS; Dhps; mouse.
DR PRO; PR:Q3TXU5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TXU5; protein.
DR Bgee; ENSMUSG00000060038; Expressed in floor plate of midbrain and 244 other tissues.
DR ExpressionAtlas; Q3TXU5; baseline and differential.
DR Genevisible; Q3TXU5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0046203; P:spermidine catabolic process; ISO:MGI.
DR GO; GO:0008216; P:spermidine metabolic process; ISO:MGI.
DR Gene3D; 3.40.910.10; -; 1.
DR InterPro; IPR002773; Deoxyhypusine_synthase.
DR InterPro; IPR036982; Deoxyhypusine_synthase_sf.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR PANTHER; PTHR11703; PTHR11703; 1.
DR Pfam; PF01916; DS; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR TIGRFAMs; TIGR00321; dhys; 1.
PE 1: Evidence at protein level;
KW Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000314944"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 131..133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 136..137
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 308..309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 323..329
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 342..343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 340
FT /note="Y -> C (in Ref. 1; BAE34820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40642 MW; 22B835EEE4E9DFAC CRC64;
MEGTPPGAAP SSALAAVLKH SSALPPESAQ VQGYDFNRGV DYHALLDAYR TTGFQATNFG
RAVQQVNAMI EKKLEPLAVD EDHHADLTQS RRPLTGCTIF LGYTSNLISS GIRETIRYLV
QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE SGINRIGNLL VPNDNYCKFE
DWLMPILDQM VLEQNTEGVK WTPSKMISRL GKEINNPDSV YYWAHKNHIP VLSPALTDGS
LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKRSGMII LGGGVVKHHI ANANLMRNGA
DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RMDAQPVKVY ADASLVFPLL VAETFAQKAD
AFRAEKNED
