DPH6_MOUSE
ID DPH6_MOUSE Reviewed; 267 AA.
AC Q9CQ28; Q3UL00; Q8R1W5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Diphthine--ammonia ligase;
DE EC=6.3.1.14;
DE AltName: Full=ATP-binding domain-containing protein 4;
DE AltName: Full=Diphthamide synthase;
DE AltName: Full=Diphthamide synthetase;
DE AltName: Full=Protein DPH6 homolog;
GN Name=Dph6; Synonyms=Atpbd4;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Testis, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, 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: Amidase that catalyzes the last step of diphthamide
CC biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists
CC in the conversion of an L-histidine residue in the translation
CC elongation factor 2 (EEF2) to diphthamide (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC ChEBI:CHEBI:456215; EC=6.3.1.14;
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CQ28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQ28-2; Sequence=VSP_024125;
CC Name=3;
CC IsoId=Q9CQ28-3; Sequence=VSP_024126;
CC -!- SIMILARITY: Belongs to the Diphthine--ammonia ligase 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; AK006965; BAB24811.1; -; mRNA.
DR EMBL; AK007021; BAB24832.1; -; mRNA.
DR EMBL; AK017595; BAB30829.1; -; mRNA.
DR EMBL; AK088160; BAC40182.1; -; mRNA.
DR EMBL; AK145789; BAE26651.1; -; mRNA.
DR EMBL; AL732404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022995; AAH22995.1; -; mRNA.
DR CCDS; CCDS16567.1; -. [Q9CQ28-1]
DR CCDS; CCDS89535.1; -. [Q9CQ28-3]
DR CCDS; CCDS89536.1; -. [Q9CQ28-2]
DR RefSeq; NP_079951.1; NM_025675.4. [Q9CQ28-1]
DR AlphaFoldDB; Q9CQ28; -.
DR SMR; Q9CQ28; -.
DR BioGRID; 211610; 1.
DR IntAct; Q9CQ28; 1.
DR MINT; Q9CQ28; -.
DR STRING; 10090.ENSMUSP00000099601; -.
DR iPTMnet; Q9CQ28; -.
DR PhosphoSitePlus; Q9CQ28; -.
DR EPD; Q9CQ28; -.
DR MaxQB; Q9CQ28; -.
DR PaxDb; Q9CQ28; -.
DR PeptideAtlas; Q9CQ28; -.
DR PRIDE; Q9CQ28; -.
DR ProteomicsDB; 279564; -. [Q9CQ28-1]
DR ProteomicsDB; 279565; -. [Q9CQ28-2]
DR ProteomicsDB; 279566; -. [Q9CQ28-3]
DR Antibodypedia; 51931; 59 antibodies from 16 providers.
DR Ensembl; ENSMUST00000028640; ENSMUSP00000028640; ENSMUSG00000057147. [Q9CQ28-3]
DR Ensembl; ENSMUST00000055144; ENSMUSP00000060730; ENSMUSG00000057147. [Q9CQ28-2]
DR Ensembl; ENSMUST00000102542; ENSMUSP00000099601; ENSMUSG00000057147. [Q9CQ28-1]
DR GeneID; 66632; -.
DR KEGG; mmu:66632; -.
DR UCSC; uc008lqk.1; mouse. [Q9CQ28-1]
DR UCSC; uc008lql.1; mouse. [Q9CQ28-3]
DR UCSC; uc012cbd.1; mouse. [Q9CQ28-2]
DR CTD; 89978; -.
DR MGI; MGI:1913882; Dph6.
DR VEuPathDB; HostDB:ENSMUSG00000057147; -.
DR eggNOG; KOG2316; Eukaryota.
DR GeneTree; ENSGT00420000029820; -.
DR HOGENOM; CLU_010289_0_1_1; -.
DR InParanoid; Q9CQ28; -.
DR OMA; NYALYWA; -.
DR OrthoDB; 1126213at2759; -.
DR PhylomeDB; Q9CQ28; -.
DR TreeFam; TF313566; -.
DR Reactome; R-MMU-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 66632; 25 hits in 73 CRISPR screens.
DR ChiTaRS; Dph6; mouse.
DR PRO; PR:Q9CQ28; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQ28; protein.
DR Bgee; ENSMUSG00000057147; Expressed in animal zygote and 242 other tissues.
DR Genevisible; Q9CQ28; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; ISO:MGI.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR12196; PTHR12196; 1.
DR Pfam; PF01902; Diphthami_syn_2; 1.
DR PIRSF; PIRSF039123; Diphthamide_synthase; 1.
DR TIGRFAMs; TIGR00290; MJ0570_dom; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Ligase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..267
FT /note="Diphthine--ammonia ligase"
FT /id="PRO_0000282398"
FT MOD_RES 97
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 189..267
FT /note="ELSKKYGVHVCGEGGEYETFTLDCPLFKKKIVVDSSEAVMHSADAFAPVAYL
FT RLSRLHLEEKVSSVPADDETANSIHSS -> EGLFRSSHALSGCIRTCGLSAALPAALG
FT RESVVSTCG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024126"
FT VAR_SEQ 253..267
FT /note="SVPADDETANSIHSS -> KAQMAEIPRRVRGVVSTCG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024125"
SQ SEQUENCE 267 AA; 29922 MW; D347E1AC6D537920 CRC64;
MRVAALISGG KDSCYNMMQC IAEGHQIVAL ANLRPDENQV ESDELDSYMY QTVGHHAIDL
YAEAMALPLY RRAIRGRSLE TGRVYTQCEG DEVEDLYELL KLVKEKEEIE GVSVGAILSD
YQRGRVENVC KRLNLQPLAY LWQRNQEDLL REMIASNIKA IIIKVAALGL DPDKHLGKTL
VEMEPYLLEL SKKYGVHVCG EGGEYETFTL DCPLFKKKIV VDSSEAVMHS ADAFAPVAYL
RLSRLHLEEK VSSVPADDET ANSIHSS
