DPH7_MOUSE
ID DPH7_MOUSE Reviewed; 477 AA.
AC Q9CYU6; A2AJ86; Q5RJV7; Q8BIT9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Diphthine methyltransferase;
DE EC=3.1.1.97;
DE AltName: Full=Diphthamide biosynthesis protein 7;
DE Short=DPH7;
DE AltName: Full=WD repeat-containing protein 85;
GN Name=Dph7; Synonyms=Wdr85;
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, Thymus, and Wolffian duct;
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 1).
RC TISSUE=Olfactory epithelium;
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 -!- FUNCTION: Catalyzes the demethylation of diphthine methyl ester to form
CC diphthine, an intermediate diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in translation
CC elongation factor 2 (EEF2). {ECO:0000250|UniProtKB:Q9BTV6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphthine methyl ester-[translation elongation factor 2] + H2O
CC = diphthine-[translation elongation factor 2] + H(+) + methanol;
CC Xref=Rhea:RHEA:42656, Rhea:RHEA-COMP:10172, Rhea:RHEA-COMP:10173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:79005, ChEBI:CHEBI:82696; EC=3.1.1.97;
CC Evidence={ECO:0000250|UniProtKB:P38332};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBUNIT: Interacts with INCA1. {ECO:0000250|UniProtKB:Q9BTV6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CYU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CYU6-2; Sequence=VSP_014526, VSP_014528;
CC -!- SIMILARITY: Belongs to the DPH7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC086486; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK013297; BAB28775.1; -; mRNA.
DR EMBL; AK078448; BAC37279.1; -; mRNA.
DR EMBL; AK087998; BAC40084.1; -; mRNA.
DR EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086486; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15743.1; -. [Q9CYU6-1]
DR RefSeq; NP_080320.1; NM_026044.3. [Q9CYU6-1]
DR AlphaFoldDB; Q9CYU6; -.
DR STRING; 10090.ENSMUSP00000028351; -.
DR iPTMnet; Q9CYU6; -.
DR PhosphoSitePlus; Q9CYU6; -.
DR EPD; Q9CYU6; -.
DR MaxQB; Q9CYU6; -.
DR PaxDb; Q9CYU6; -.
DR PeptideAtlas; Q9CYU6; -.
DR PRIDE; Q9CYU6; -.
DR ProteomicsDB; 277383; -. [Q9CYU6-1]
DR ProteomicsDB; 277384; -. [Q9CYU6-2]
DR Antibodypedia; 19075; 107 antibodies from 18 providers.
DR DNASU; 67228; -.
DR Ensembl; ENSMUST00000028351; ENSMUSP00000028351; ENSMUSG00000026975. [Q9CYU6-1]
DR GeneID; 67228; -.
DR KEGG; mmu:67228; -.
DR UCSC; uc008ipq.2; mouse. [Q9CYU6-1]
DR UCSC; uc008ips.2; mouse. [Q9CYU6-2]
DR CTD; 92715; -.
DR MGI; MGI:1914478; Dph7.
DR VEuPathDB; HostDB:ENSMUSG00000026975; -.
DR eggNOG; KOG0280; Eukaryota.
DR GeneTree; ENSGT00390000018644; -.
DR HOGENOM; CLU_036100_2_1_1; -.
DR InParanoid; Q9CYU6; -.
DR OMA; LDMKWLP; -.
DR OrthoDB; 960224at2759; -.
DR PhylomeDB; Q9CYU6; -.
DR TreeFam; TF324407; -.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 67228; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Dph7; mouse.
DR PRO; PR:Q9CYU6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CYU6; protein.
DR Bgee; ENSMUSG00000026975; Expressed in dentate gyrus of hippocampal formation granule cell and 209 other tissues.
DR ExpressionAtlas; Q9CYU6; baseline and differential.
DR Genevisible; Q9CYU6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061685; F:diphthine methylesterase activity; IBA:GO_Central.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..477
FT /note="Diphthine methyltransferase"
FT /id="PRO_0000050907"
FT REPEAT 194..232
FT /note="WD 1"
FT REPEAT 236..276
FT /note="WD 2"
FT REPEAT 422..464
FT /note="WD 3"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014526"
FT VAR_SEQ 123
FT /note="E -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014528"
FT CONFLICT 235
FT /note="K -> N (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="D -> H (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> Y (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="G -> R (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="G -> V (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="A -> P (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> R (in Ref. 1; BAC40084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 53201 MW; 2655573524A4BA9C CRC64;
MAGSHAGTLR VLQAVDTELT ADSVEWCPVE GYQHLLACGT YQLRAPRDQP ALDGSEPQVR
LGRLYLFSFS EHNTAKPLLE VQRRDSSAVL DMKWCHIPVS GHVLLGLANA SGSIGLLRLM
ECENNSYTLQ PISSLALDEN CLSLSMDWST GKSVRAREQP LKIISSDSKG QLHLLMVNEG
TAELQLVASW PAHHFEAWIA AFNYWQTELV YSGGDDCLLR GWDTRMLGTP VFTSKRHCMG
VCSIQSSPHQ EHILATGSYD EHVLLWDTRN IRQPLADVPV QGGVWRLKWH PVHHHLLLAA
CMHNGFKILN CQKAIEEKQD ITVLTSHEMP NSLVYGADWS WLFHSMKPTP TWFFDQNDMG
VKAADHSSLK VTEEPPIHSQ EQTMDRQVEG PANAHTRAEL KASLLPLTED MKNSKDCSSS
SVKTRDLSHC SGGQSFDNSL LATCSFYDHV LHLWKWETNQ ARTLCSGTGC DLGSADH
