CARME_DROME
ID CARME_DROME Reviewed; 439 AA.
AC Q9I7X6; O46078; Q7KW04; Q9W540;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Carnosine N-methyltransferase {ECO:0000250|UniProtKB:Q5BJZ6};
DE EC=2.1.1.22 {ECO:0000250|UniProtKB:Q5BJZ6};
GN ORFNames=CG11596;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-403, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: N-methyltransferase that mediates the formation of anserine
CC (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
CC {ECO:0000250|UniProtKB:Q8N4J0}.
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:Q8N4J0};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9I7X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9I7X6-2; Sequence=VSP_037165;
CC Name=3;
CC IsoId=Q9I7X6-3; Sequence=VSP_037164, VSP_037165;
CC -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAF45697.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45698.1; -; Genomic_DNA.
DR EMBL; AE014298; AAG22387.1; -; Genomic_DNA.
DR EMBL; AL009191; CAA15684.1; -; Genomic_DNA.
DR EMBL; AY051951; AAK93375.1; -; mRNA.
DR RefSeq; NP_001259154.1; NM_001272225.1. [Q9I7X6-3]
DR RefSeq; NP_001259155.1; NM_001272226.1. [Q9I7X6-3]
DR RefSeq; NP_569963.1; NM_130607.3. [Q9I7X6-1]
DR RefSeq; NP_726779.1; NM_166916.2. [Q9I7X6-2]
DR RefSeq; NP_726780.1; NM_166917.2. [Q9I7X6-3]
DR AlphaFoldDB; Q9I7X6; -.
DR SMR; Q9I7X6; -.
DR BioGRID; 57704; 18.
DR IntAct; Q9I7X6; 4.
DR STRING; 7227.FBpp0070305; -.
DR iPTMnet; Q9I7X6; -.
DR PaxDb; Q9I7X6; -.
DR DNASU; 31158; -.
DR EnsemblMetazoa; FBtr0070318; FBpp0070305; FBgn0023522. [Q9I7X6-2]
DR EnsemblMetazoa; FBtr0070319; FBpp0070306; FBgn0023522. [Q9I7X6-1]
DR EnsemblMetazoa; FBtr0070320; FBpp0070307; FBgn0023522. [Q9I7X6-3]
DR EnsemblMetazoa; FBtr0332587; FBpp0304838; FBgn0023522. [Q9I7X6-3]
DR EnsemblMetazoa; FBtr0332588; FBpp0304839; FBgn0023522. [Q9I7X6-3]
DR GeneID; 31158; -.
DR KEGG; dme:Dmel_CG11596; -.
DR UCSC; CG11596-RA; d. melanogaster. [Q9I7X6-1]
DR UCSC; CG11596-RB; d. melanogaster.
DR UCSC; CG11596-RC; d. melanogaster.
DR FlyBase; FBgn0023522; CG11596.
DR VEuPathDB; VectorBase:FBgn0023522; -.
DR eggNOG; KOG2798; Eukaryota.
DR GeneTree; ENSGT00390000005323; -.
DR InParanoid; Q9I7X6; -.
DR PhylomeDB; Q9I7X6; -.
DR Reactome; R-DME-70921; Histidine catabolism.
DR BioGRID-ORCS; 31158; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31158; -.
DR PRO; PR:Q9I7X6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0023522; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; Q9I7X6; baseline and differential.
DR Genevisible; Q9I7X6; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030735; F:carnosine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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 Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..439
FT /note="Carnosine N-methyltransferase"
FT /id="PRO_0000372646"
FT REGION 385..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 178
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 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 286
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 317
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 368
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037164"
FT VAR_SEQ 127
FT /note="Q -> QIDIPFDEADVEPLKILK (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037165"
SQ SEQUENCE 439 AA; 50504 MW; 883DE54CC8D8B5F7 CRC64;
MSSMDCATFP MHPKMDEQLA RTFVINEEEE EKHIQKVQNA FLYYGPYACQ RLKRSMDYLN
SLSGEDQIML AKYRGHLECV RTCIDRNQAV IREILRGRVL YPTDEATGDP SEFDEPPPNV
RHGDMDQAQS TLKLIARDWS TEGALEREQS YKPIIDSIVA YFKHSDFELK DIKILVPGAG
LGRLTYELAC LGYSCEGNEF SYFMLIASNF VLNLCDNENK YVLYPWVHQY VNNLRREDQV
APVRFPDVCP LKNPPKGHFE IAAGDFLEVY KTPNAYNCVA TCFFIDCANN VIDFIRTIYK
ILVPGGIWVN LGPLLYHFSD VSGQNSIEPA FEDLCIIMES VGFVIEKSRT GIRTKYAQNP
SSMKQSEYQS LFWVCRKPDL FEEQRGKRKA SREPHDLIVR EDSEEEGEQQ PERNETEEKQ
QLKPLATANC ETEIKEQPS
