ID   V9GXP1_MOUSE            Unreviewed;       177 AA.
AC   V9GXP1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-NOV-2024, entry version 69.
DE   RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE            EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
GN   Name=Dph5 {ECO:0000313|Ensembl:ENSMUSP00000139249.2,
GN   ECO:0000313|MGI:MGI:1916990};
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 {ECO:0000313|Ensembl:ENSMUSP00000139249.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000139249.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139249.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
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   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000139249.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139249.2};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000139249.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139249.2};
RG   Ensembl;
RL   Submitted (AUG-2024) to UniProtKB.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       catalyzes four methylations of the modified target histidine residue in
CC       translation elongation factor 2 (EF-2), to form an intermediate called
CC       diphthine methyl ester. The four successive methylation reactions
CC       represent the second step of diphthamide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC         elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl
CC         ester-[translation elongation factor 2] + 4 S-adenosyl-L-homocysteine
CC         + 3 H(+); Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA-
CC         COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314;
CC         Evidence={ECO:0000256|ARBA:ARBA00000054};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005156}.
CC   -!- SIMILARITY: Belongs to the diphthine synthase family.
CC       {ECO:0000256|ARBA:ARBA00006729}.
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DR   RefSeq; XP_006502102.1; XM_006502039.2.
DR   AlphaFoldDB; V9GXP1; -.
DR   SMR; V9GXP1; -.
DR   PeptideAtlas; V9GXP1; -.
DR   Antibodypedia; 33698; 27 antibodies from 8 providers.
DR   Ensembl; ENSMUST00000185098.8; ENSMUSP00000139249.2; ENSMUSG00000033554.18.
DR   AGR; MGI:1916990; -.
DR   MGI; MGI:1916990; Dph5.
DR   VEuPathDB; HostDB:ENSMUSG00000033554; -.
DR   GeneTree; ENSGT00390000010568; -.
DR   HOGENOM; CLU_066040_2_0_1; -.
DR   OMA; TAGDPMV; -.
DR   UniPathway; UPA00559; -.
DR   BioGRID-ORCS; 69740; 29 hits in 79 CRISPR screens.
DR   ChiTaRS; Dph5; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000033554; Expressed in paneth cell and 234 other cell types or tissues.
DR   ExpressionAtlas; V9GXP1; baseline and differential.
DR   GO; GO:0141133; F:diphthine methyl ester synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR   CDD; cd11647; DHP5_DphB; 1.
DR   FunFam; 3.40.1010.10:FF:000004; Putative diphthine synthase; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR004551; Dphthn_synthase.
DR   NCBIfam; TIGR00522; dph5; 1.
DR   PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR   PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:V9GXP1,
KW   ECO:0007829|ProteomicsDB:V9GXP1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..166
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   177 AA;  19921 MW;  B3FE40D4B6C13472 CRC64;
     MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG RKLILADREE
     VEQEADNIFK DADVSDVAFL VVGDPFGATT HSDLILRATK LGIPYQVIHN ASIMNAVGCC
     GLQLYRFGET VSIVFWTDTW RPESFFDKVK RNRANGMHTL CLLDIKVKEQ SLENLIR
//