HEMK1_MOUSE
ID HEMK1_MOUSE Reviewed; 340 AA.
AC Q921L7; B0QZU8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=MTRF1L release factor glutamine methyltransferase {ECO:0000250|UniProtKB:Q9Y5R4};
DE EC=2.1.1.297 {ECO:0000250|UniProtKB:Q9Y5R4};
DE AltName: Full=HemK methyltransferase family member 1;
GN Name=Hemk1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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: N5-glutamine methyltransferase responsible for the
CC methylation of the glutamine residue in the universally conserved GGQ
CC motif of the mitochondrial translation release factor MTRF1L.
CC {ECO:0000250|UniProtKB:Q9Y5R4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5R4};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y5R4}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AL672070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011431; AAH11431.1; -; mRNA.
DR EMBL; BC024428; AAH24428.1; -; mRNA.
DR CCDS; CCDS23488.1; -.
DR RefSeq; NP_598745.2; NM_133984.2.
DR RefSeq; XP_011241215.1; XM_011242913.1.
DR AlphaFoldDB; Q921L7; -.
DR SMR; Q921L7; -.
DR STRING; 10090.ENSMUSP00000035196; -.
DR PhosphoSitePlus; Q921L7; -.
DR EPD; Q921L7; -.
DR MaxQB; Q921L7; -.
DR PaxDb; Q921L7; -.
DR PRIDE; Q921L7; -.
DR ProteomicsDB; 269696; -.
DR TopDownProteomics; Q921L7; -.
DR Antibodypedia; 30986; 172 antibodies from 22 providers.
DR DNASU; 69536; -.
DR Ensembl; ENSMUST00000035196; ENSMUSP00000035196; ENSMUSG00000032579.
DR GeneID; 69536; -.
DR KEGG; mmu:69536; -.
DR UCSC; uc009rle.2; mouse.
DR CTD; 51409; -.
DR MGI; MGI:1916786; Hemk1.
DR VEuPathDB; HostDB:ENSMUSG00000032579; -.
DR eggNOG; KOG2904; Eukaryota.
DR GeneTree; ENSGT00390000014125; -.
DR HOGENOM; CLU_018398_4_1_1; -.
DR InParanoid; Q921L7; -.
DR OMA; FDARYWE; -.
DR OrthoDB; 1513943at2759; -.
DR PhylomeDB; Q921L7; -.
DR TreeFam; TF324423; -.
DR BioGRID-ORCS; 69536; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Hemk1; mouse.
DR PRO; PR:Q921L7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q921L7; protein.
DR Bgee; ENSMUSG00000032579; Expressed in choroid plexus epithelium and 213 other tissues.
DR ExpressionAtlas; Q921L7; baseline and differential.
DR Genevisible; Q921L7; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..340
FT /note="MTRF1L release factor glutamine methyltransferase"
FT /id="PRO_0000157179"
FT BINDING 168..172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 241..244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="R -> Q (in Ref. 2; AAH11431)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="R -> H (in Ref. 2; AAH11431)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Q -> R (in Ref. 2; AAH11431)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Q -> R (in Ref. 2; AAH11431)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="H -> C (in Ref. 2; AAH11431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 38233 MW; 379E5932CE302053 CRC64;
MKLWGQILWT LLSVPRGRRG VLQGWAFNSW KTYSSLTGPL SATGMVNHWT RVFEERGIPE
ARESSEYIVA HVLGAKTFQS LKPALWTKPL TPQQLECIQE LCGRRLQRMP VQYILGEWDF
QGLSLKMVPP VFIPRPETEE LVEWVLEEVA QRPHAVRAQD GPLILEVGCG SGAITLSLLS
QLPKSRVVAV DKEEAAVSLT HENAQRLQLQ DRIRIIHLDI TSEGCCTHLL PWSPLDLVVS
NPPYIFRKDM EQLAPEICSY EDLVALDGGD EGMDIITHIL TLAPQLLNAS GSIFLEVDPR
HPELVSSWLQ SHPDLHLSLV GVREDFCGRP RFLHVQKSAP
