ACKMT_MOUSE
ID ACKMT_MOUSE Reviewed; 247 AA.
AC Q9D1Z3; Q8K2S1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP synthase subunit C lysine N-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:30530489};
DE AltName: Full=Protein N-lysine methyltransferase FAM173B {ECO:0000305};
DE Short=mFam173b {ECO:0000303|PubMed:29444090};
GN Name=Atpsckmt {ECO:0000250|UniProtKB:Q6P4H8};
GN Synonyms=Fam173b {ECO:0000312|MGI:MGI:1915323};
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; TISSUE=Retina;
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 MRNA].
RC STRAIN=Czech II; TISSUE=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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=29444090; DOI=10.1371/journal.pbio.2003452;
RA Willemen H.L.D.M., Kavelaars A., Prado J., Maas M., Versteeg S.,
RA Nellissen L.J.J., Tromp J., Gonzalez Cano R., Zhou W., Jakobsson M.E.,
RA Malecki J., Posthuma G., Habib A.M., Heijnen C.J., Falnes P.O.,
RA Eijkelkamp N.;
RT "Identification of FAM173B as a protein methyltransferase promoting chronic
RT pain.";
RL PLoS Biol. 16:E2003452-E2003452(2018).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30530489; DOI=10.1074/jbc.ra118.005473;
RA Malecki J.M., Willemen H.L.D.M., Pinto R., Ho A.Y.Y., Moen A.,
RA Kjoenstad I.F., Burgering B.M.T., Zwartkruis F., Eijkelkamp N.,
RA Falnes P.O.;
RT "Lysine methylation by the mitochondrial methyltransferase FAM173B
RT optimizes the function of mitochondrial ATP synthase.";
RL J. Biol. Chem. 294:1128-1141(2019).
CC -!- FUNCTION: Mitochondrial protein-lysine N-methyltransferase that
CC trimethylates ATP synthase subunit C, ATP5MC1 and ATP5MC2.
CC Trimethylation is required for proper incorporation of the C subunit
CC into the ATP synthase complex and mitochondrial respiration
CC (PubMed:29444090, PubMed:30530489). Promotes chronic pain
CC (PubMed:29444090). Involved in persistent inflammatory and neuropathic
CC pain: methyltransferase activity in the mitochondria of sensory neurons
CC promotes chronic pain via a pathway that depends on the production of
CC reactive oxygen species (ROS) and on the engagement of spinal cord
CC microglia (PubMed:29444090). {ECO:0000269|PubMed:29444090,
CC ECO:0000269|PubMed:30530489}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000269|PubMed:30530489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000269|PubMed:30530489};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q6P4H8}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to mitochondrial cristae.
CC {ECO:0000250|UniProtKB:Q6P4H8}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:29444090}.
CC -!- INDUCTION: Expression is up-regulated in dorsal root ganglia (DRG)
CC during chronic inflammatory pain. {ECO:0000269|PubMed:29444090}.
CC -!- DOMAIN: Contains an atypical, non-cleavable mitochondrial targeting
CC sequence responsible for its localization to mitochondria.
CC {ECO:0000250|UniProtKB:Q6P4H8}.
CC -!- SIMILARITY: Belongs to the ANT/ATPSC lysine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK020868; BAB32234.1; -; mRNA.
DR EMBL; BC030179; AAH30179.1; -; mRNA.
DR CCDS; CCDS27412.1; -.
DR RefSeq; NP_080822.1; NM_026546.3.
DR AlphaFoldDB; Q9D1Z3; -.
DR SMR; Q9D1Z3; -.
DR BioGRID; 212640; 1.
DR STRING; 10090.ENSMUSP00000039094; -.
DR PhosphoSitePlus; Q9D1Z3; -.
DR EPD; Q9D1Z3; -.
DR MaxQB; Q9D1Z3; -.
DR PaxDb; Q9D1Z3; -.
DR PeptideAtlas; Q9D1Z3; -.
DR PRIDE; Q9D1Z3; -.
DR ProteomicsDB; 275974; -.
DR Antibodypedia; 22448; 69 antibodies from 21 providers.
DR DNASU; 68073; -.
DR Ensembl; ENSMUST00000042702; ENSMUSP00000039094; ENSMUSG00000039065.
DR GeneID; 68073; -.
DR KEGG; mmu:68073; -.
DR UCSC; uc007vkk.1; mouse.
DR CTD; 134145; -.
DR MGI; MGI:1915323; Atpsckmt.
DR VEuPathDB; HostDB:ENSMUSG00000039065; -.
DR eggNOG; KOG4058; Eukaryota.
DR GeneTree; ENSGT00390000014771; -.
DR HOGENOM; CLU_068443_4_0_1; -.
DR InParanoid; Q9D1Z3; -.
DR OMA; GVNTVWF; -.
DR OrthoDB; 1605787at2759; -.
DR PhylomeDB; Q9D1Z3; -.
DR TreeFam; TF314984; -.
DR BioGRID-ORCS; 68073; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Fam173b; mouse.
DR PRO; PR:Q9D1Z3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D1Z3; protein.
DR Bgee; ENSMUSG00000039065; Expressed in ear vesicle and 189 other tissues.
DR ExpressionAtlas; Q9D1Z3; baseline and differential.
DR Genevisible; Q9D1Z3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030061; C:mitochondrial crista; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:UniProtKB.
DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026170; FAM173A/B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13610; PTHR13610; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Methyltransferase; Mitochondrion;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..247
FT /note="ATP synthase subunit C lysine N-methyltransferase"
FT /id="PRO_0000321537"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..85
FT /note="Required for mitochondrial location"
FT /evidence="ECO:0000250|UniProtKB:Q6P4H8"
FT REGION 209..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4H8"
FT CONFLICT 229
FT /note="T -> I (in Ref. 2; AAH30179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27397 MW; 30566F3CBAAF5B20 CRC64;
MERVGTPEEE RQAGPVLPTS LESDSSKRTS WGFLITGVVG GALLTVYAVA TPFITPALRK
VCLPFVPATS KQVENVVRML RHRRGPLVDI GSGDGRIVIA AAKEGFPAVG YELNPWLVWY
SRYRAWRAGV HGSAKFYISD LWKVTFAQYS NVVIFGVPQM MPQLEKKLEL ELEDGARVIA
CRFPFPRWTP DHTTGEGIDT VWAYDMSAQR GRGGRPNQEW VGQKNLSETA GLQASSSETR
SKLLDVE
