ACKMT_RAT
ID ACKMT_RAT Reviewed; 216 AA.
AC D3ZLY0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=ATP synthase subunit C lysine N-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q6P4H8};
DE AltName: Full=Protein N-lysine methyltransferase FAM173B;
GN Name=Atpsckmt; Synonyms=Fam173b {ECO:0000312|RGD:1560629};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
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 (Probable).
CC Promotes chronic pain. Involved in persistent inflammatory and
CC neuropathic pain: methyltransferase activity in the mitochondria of
CC sensory neurons promotes chronic pain via a pathway that depends on the
CC production of reactive oxygen species (ROS) and on the engagement of
CC spinal cord microglia (By similarity). {ECO:0000250|UniProtKB:Q6P4H8,
CC ECO:0000250|UniProtKB:Q9D1Z3, ECO:0000305|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:0000250|UniProtKB:Q6P4H8};
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 -!- 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; AABR07009034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473992; EDL82650.1; -; Genomic_DNA.
DR RefSeq; NP_001102648.1; NM_001109178.1.
DR AlphaFoldDB; D3ZLY0; -.
DR SMR; D3ZLY0; -.
DR STRING; 10116.ENSRNOP00000041476; -.
DR PaxDb; D3ZLY0; -.
DR Ensembl; ENSRNOT00000046325; ENSRNOP00000041476; ENSRNOG00000022347.
DR GeneID; 499561; -.
DR KEGG; rno:499561; -.
DR UCSC; RGD:1560629; rat.
DR CTD; 134145; -.
DR RGD; 1560629; Atpsckmt.
DR eggNOG; KOG4058; Eukaryota.
DR GeneTree; ENSGT00390000014771; -.
DR HOGENOM; CLU_068443_4_0_1; -.
DR InParanoid; D3ZLY0; -.
DR OMA; GVNTVWF; -.
DR OrthoDB; 1605787at2759; -.
DR PhylomeDB; D3ZLY0; -.
DR TreeFam; TF314984; -.
DR PRO; PR:D3ZLY0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000022347; Expressed in quadriceps femoris and 20 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030061; C:mitochondrial crista; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISO:RGD.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; ISS:UniProtKB.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; ISO:RGD.
DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; ISS: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 3: Inferred from homology;
KW Acetylation; Membrane; Methyltransferase; Mitochondrion;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..216
FT /note="ATP synthase subunit C lysine N-methyltransferase"
FT /id="PRO_0000446889"
FT TRANSMEM 31..50
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4H8"
SQ SEQUENCE 216 AA; 24053 MW; 20127BA3A1283DD2 CRC64;
MERGETPEEE RQSGCVLPTS PESDSLKTSN WGFLITGVIG GALVTVYAVT TPFIAPALRK
VCLPFVPATS RQVENVVKML QHRRGPLVDI GSGDGRIVIA AAKAGFPAVG YELNPWLVWY
SRYRAWREGV HGSAKFYISD LWKVTFAQYS NVVIFGVPQM MPQLEKKLEF ELEDGARVIA
CRFPFPHWTP DHTTGEGIDT VWAYDMSACR TQGKRA
