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ANKMT_MOUSE
ID   ANKMT_MOUSE             Reviewed;         229 AA.
AC   Q501J2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Adenine nucleotide translocase lysine N-methyltransferase {ECO:0000250|UniProtKB:Q9BQD7};
DE            Short=ANT-KMT {ECO:0000250|UniProtKB:Q9BQD7};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9BQD7};
GN   Name=Antkmt {ECO:0000312|MGI:MGI:2384888};
GN   Synonyms=Fam173a {ECO:0000312|MGI:MGI:2384888};
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=BALB/cJ, and C57BL/6J; TISSUE=Cecum;
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=Lung;
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=Heart, Kidney, Lung, and Testis;
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).
CC   -!- FUNCTION: Mitochondrial protein-lysine N-methyltransferase that
CC       trimethylates adenine nucleotide translocases ANT2/SLC25A5 and
CC       ANT3/SLC25A6, thereby regulating mitochondrial respiration. Probably
CC       also trimethylates ANT1/SLC25A4. {ECO:0000250|UniProtKB:Q9BQD7}.
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:Q9BQD7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQD7};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q9BQD7}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The pre-methyltransferase (preMT) region is responsible for
CC       mitochondrial localization. {ECO:0000250|UniProtKB:Q9BQD7}.
CC   -!- SIMILARITY: Belongs to the ANT/ATPSC lysine N-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK146214; BAE26983.1; -; mRNA.
DR   EMBL; AK162337; BAE36860.1; -; mRNA.
DR   EMBL; BC096050; AAH96050.1; -; mRNA.
DR   CCDS; CCDS28528.1; -.
DR   RefSeq; NP_663385.2; NM_145410.4.
DR   AlphaFoldDB; Q501J2; -.
DR   SMR; Q501J2; -.
DR   STRING; 10090.ENSMUSP00000072518; -.
DR   PhosphoSitePlus; Q501J2; -.
DR   SwissPalm; Q501J2; -.
DR   EPD; Q501J2; -.
DR   MaxQB; Q501J2; -.
DR   PaxDb; Q501J2; -.
DR   PeptideAtlas; Q501J2; -.
DR   PRIDE; Q501J2; -.
DR   ProteomicsDB; 267685; -.
DR   Ensembl; ENSMUST00000072735; ENSMUSP00000072518; ENSMUSG00000057411.
DR   GeneID; 214917; -.
DR   KEGG; mmu:214917; -.
DR   UCSC; uc008bbw.2; mouse.
DR   CTD; 65990; -.
DR   MGI; MGI:2384888; Antkmt.
DR   VEuPathDB; HostDB:ENSMUSG00000057411; -.
DR   eggNOG; KOG4058; Eukaryota.
DR   GeneTree; ENSGT00390000014771; -.
DR   HOGENOM; CLU_068443_4_2_1; -.
DR   InParanoid; Q501J2; -.
DR   OMA; HEFRIPG; -.
DR   OrthoDB; 1605787at2759; -.
DR   PhylomeDB; Q501J2; -.
DR   TreeFam; TF314984; -.
DR   BioGRID-ORCS; 214917; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Fam173a; mouse.
DR   PRO; PR:Q501J2; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q501J2; protein.
DR   Bgee; ENSMUSG00000057411; Expressed in choroid plexus and 105 other tissues.
DR   ExpressionAtlas; Q501J2; baseline and differential.
DR   Genevisible; Q501J2; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; 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; IBA:GO_Central.
DR   GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; IBA:GO_Central.
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   Membrane; Methyltransferase; Mitochondrion; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..229
FT                   /note="Adenine nucleotide translocase lysine N-
FT                   methyltransferase"
FT                   /id="PRO_0000263722"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="N-terminal sequence (NTS)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQD7"
FT   REGION          43..77
FT                   /note="Methyltransferase (MTase)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQD7"
FT   REGION          43..77
FT                   /note="Pre-methyltransferase (preMT)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQD7"
SQ   SEQUENCE   229 AA;  24740 MW;  2123E2BADCAA9C10 CRC64;
     MDQDDPAEAL TELREKRLGL LEIVQAAAGS GLAVYTIWAL LLQPGFRRVP LRLQVPYVGA
     SARQVENVLS LLRGRPGKMV DLGSGDGRIV LAAHQCGLRP AMGYELNPWL VGLARLHAWR
     AGCSASVCYH RKDLWKVSLR DCHNVSVFLA PSVLQLLEDK LQAELPVGAR VVSGRFPLPT
     WQPVAVVGEG TDRVWAYDVH GSGPTVSSCG VPIKAIPESS STLVPRAPV
 
 
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