CARME_MOUSE
ID CARME_MOUSE Reviewed; 400 AA.
AC Q80UY1; Q9CWF3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Carnosine N-methyltransferase {ECO:0000250|UniProtKB:Q5BJZ6, ECO:0000312|MGI:MGI:1914633};
DE EC=2.1.1.22 {ECO:0000250|UniProtKB:Q5BJZ6};
GN Name=Carnmt1 {ECO:0000312|MGI:MGI:1914633};
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;
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=FVB/N; 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=Heart;
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: N-methyltransferase that catalyzes the formation of anserine
CC (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a
CC methylated derivative of carnosine (beta-alanyl-L-histidine), is an
CC abundant constituent of vertebrate skeletal muscles. Also methylates
CC other L-histidine-containing di- and tripeptides such as Gly-Gly-His,
CC Gly-His and homocarnosine (GABA-His). {ECO:0000250|UniProtKB:Q5BJZ6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:14205, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57485, ChEBI:CHEBI:57856, ChEBI:CHEBI:58445,
CC ChEBI:CHEBI:59789; EC=2.1.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q5BJZ6};
CC -!- SUBUNIT: Homodimer. Each monomer accommodates one molecule of carnosine
CC in its active pocket, precisely anchoring the histidine imidazole ring
CC such that only N1 is exposed and deprotonated for methylation.
CC {ECO:0000250|UniProtKB:Q8N4J0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5BJZ6}. Nucleus {ECO:0000250|UniProtKB:Q5BJZ6}.
CC -!- DOMAIN: The Gly-Xaa-Gly-Xaa-Gly (GXGXG) motif binds the adenosyl part
CC of S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q8N4J0}.
CC -!- DOMAIN: The carnosine-binding region forms hydrophobic and hydrogen
CC bonds with carnosine, defining a flipping orientation of the imidazole
CC ring so that N1 is present next to S-adenosyl-L-methionine for
CC methylation. {ECO:0000250|UniProtKB:Q8N4J0}.
CC -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK010784; BAB27180.1; -; mRNA.
DR EMBL; BC043335; AAH43335.1; -; mRNA.
DR EMBL; BC092281; AAH92281.1; -; mRNA.
DR CCDS; CCDS29689.1; -.
DR RefSeq; NP_080396.2; NM_026120.4.
DR AlphaFoldDB; Q80UY1; -.
DR SMR; Q80UY1; -.
DR BioGRID; 212149; 6.
DR IntAct; Q80UY1; 1.
DR MINT; Q80UY1; -.
DR STRING; 10090.ENSMUSP00000025632; -.
DR iPTMnet; Q80UY1; -.
DR PhosphoSitePlus; Q80UY1; -.
DR EPD; Q80UY1; -.
DR MaxQB; Q80UY1; -.
DR PaxDb; Q80UY1; -.
DR PeptideAtlas; Q80UY1; -.
DR PRIDE; Q80UY1; -.
DR ProteomicsDB; 283674; -.
DR Antibodypedia; 12742; 172 antibodies from 20 providers.
DR DNASU; 67383; -.
DR Ensembl; ENSMUST00000025632; ENSMUSP00000025632; ENSMUSG00000024726.
DR GeneID; 67383; -.
DR KEGG; mmu:67383; -.
DR UCSC; uc008gxv.1; mouse.
DR CTD; 138199; -.
DR MGI; MGI:1914633; Carnmt1.
DR VEuPathDB; HostDB:ENSMUSG00000024726; -.
DR eggNOG; KOG2798; Eukaryota.
DR GeneTree; ENSGT00390000005323; -.
DR HOGENOM; CLU_030612_0_0_1; -.
DR InParanoid; Q80UY1; -.
DR OMA; PNGLWIN; -.
DR OrthoDB; 1437030at2759; -.
DR PhylomeDB; Q80UY1; -.
DR TreeFam; TF313564; -.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR BioGRID-ORCS; 67383; 8 hits in 41 CRISPR screens.
DR ChiTaRS; Carnmt1; mouse.
DR PRO; PR:Q80UY1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80UY1; protein.
DR Bgee; ENSMUSG00000024726; Expressed in quadriceps femoris and 63 other tissues.
DR ExpressionAtlas; Q80UY1; baseline and differential.
DR Genevisible; Q80UY1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030735; F:carnosine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035498; P:carnosine metabolic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR012901; CARME.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12303; PTHR12303; 1.
DR Pfam; PF07942; N2227; 1.
DR SMART; SM01296; N2227; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..400
FT /note="Carnosine N-methyltransferase"
FT /id="PRO_0000089686"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 286
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 307
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 315
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 338
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 389
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT CONFLICT 20..21
FT /note="SE -> TR (in Ref. 1; BAB27180)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="H -> D (in Ref. 1; BAB27180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 46339 MW; BF5FCC07EEB71F6D CRC64;
MQRRQRAPPA SQPAQDGGRS EDVEVQFSAG RLGSAAPAGP PARGTAEDEE RLEREHFWKV
INAFRYYGTS MHERVNRTER QFRSLPENQQ KLLPQFPLHL DKIRKCIDHN QEILLTIVND
CIHMFENKEY GEDANGKIMP ASTFDMDKLK STLKQFVRDW SETGKAERDA CYKPIIKEII
KNFPKERWDP SKVNILVPGA GLGRLAWEVA MLGYACQGNE WSFFMLFSSN FVLNRCSEIN
KYKLYPWIHQ FSNNRRSADQ IRPILFPDVD PHSLPPGSNF SMTAGDFQEI YSECNAWDCI
ATCFFIDTAH NVIDYIDTIW RILKPGGIWI NLGPLLYHFE NLANELSIEL SYEDIKNVVL
QYGFQLEVEK ESVLSTYTVN DLSMMKYYYE CVLFVVRKPQ
