ACKMT_XENLA
ID ACKMT_XENLA Reviewed; 226 AA.
AC Q5I047;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 {ECO:0000305};
GN Name=atpsckmt; Synonyms=fam173b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial protein-lysine N-methyltransferase that
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. Protein-lysine N-methyltransferase activity is
CC dependent on S-adenosyl-L-methionine. {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 -!- SIMILARITY: Belongs to the ANT/ATPSC lysine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC088716; AAH88716.1; -; mRNA.
DR RefSeq; NP_001088917.1; NM_001095448.1.
DR AlphaFoldDB; Q5I047; -.
DR SMR; Q5I047; -.
DR DNASU; 496288; -.
DR GeneID; 496288; -.
DR KEGG; xla:496288; -.
DR CTD; 496288; -.
DR Xenbase; XB-GENE-6252193; atpsckmt.S.
DR OrthoDB; 1605787at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 496288; Expressed in muscle tissue and 20 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
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; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Membrane; Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="ATP synthase subunit C lysine N-methyltransferase"
FT /id="PRO_0000321538"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 48..82
FT /note="Required for mitochondrial location"
FT /evidence="ECO:0000250|UniProtKB:Q6P4H8"
SQ SEQUENCE 226 AA; 25478 MW; 91CE7FDE1C902518 CRC64;
MSKSRKESKS LEEYSIVSST SRPKKKKWGL VATGVIGGTL VALYAVATPF VAPALRKLCL
PYVPATTTQV KNVLKMLRSR TGIVVDIGSG DGRIVIAAAK EGFQAVGYEL NPWLVWYSRF
RAWREGVHHH TRFYVSDLWK VSFSRYRNVV IFGVPQMMPQ LEKKLQTELQ DAARVIACRF
PFPNWVPDHI FGEGVDTVWT YDLGAFRKVS DLKQVASKHC ILDTTV