CMTR2_DROME
ID CMTR2_DROME Reviewed; 700 AA.
AC Q9UAS6; A1ZB00; O96839; Q961S3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
DE EC=2.1.1.296 {ECO:0000250|UniProtKB:Q8IYT2};
DE AltName: Full=Cap methyltransferase 2 homolog;
DE AltName: Full=Cap2 2'O-ribose methyltransferase 2 homolog;
DE Short=MTr2;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 1 homolog;
DE AltName: Full=Protein Adrift;
GN Name=cmtr2; Synonyms=aft; ORFNames=CG5032;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10068643; DOI=10.1242/dev.126.7.1505;
RA Englund C., Uv A.E., Cantera R., Mathies L.D., Krasnow M.A., Samakovlis C.;
RT "adrift, a novel bnl-induced Drosophila gene, required for tracheal
RT pathfinding into the CNS.";
RL Development 126:1505-1514(1999).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure
CC of mRNAs. May methylate the ribose of the second nucleotide of a
CC m(7)GpppG-capped mRNA (cap0) to produce m(7)GpppRmpNm (cap2) (By
CC similarity). Regulates expression of tracheal genes required for
CC pathfinding on the segmental nerve (PubMed:10068643).
CC {ECO:0000250|UniProtKB:Q8IYT2, ECO:0000269|PubMed:10068643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC EC=2.1.1.296; Evidence={ECO:0000250|UniProtKB:Q8IYT2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10068643}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed and distributed during the
CC syncytial blastoderm stage. In zygote first detected in mid-
CC embryogenesis in the developing tracheal system and later in the
CC developing gonad. Tracheal expression is highly dynamic. At stage 11,
CC weakly expressed in all tracheal cells. During stages 12 and 13,
CC preferential expression in the leading cells of the ganglionic branch
CC and other growing primary branches. During stages 14 and 15, expression
CC becomes further restricted to just the GB1 terminal cell and other
CC terminal cells. {ECO:0000269|PubMed:10068643}.
CC -!- INDUCTION: Induced by the branchless FGF pathway in migrating tracheal
CC cells, resulting of the switch from the intersegmental to the segmental
CC nerve. {ECO:0000269|PubMed:10068643}.
CC -!- DISRUPTION PHENOTYPE: Ganglionic branches migrate normally along the
CC intersegmental nerve, but sporadically fail to switch to the segmental
CC nerve and enter the CNS; they wind up meandering along the ventral
CC epidermis instead. {ECO:0000269|PubMed:10068643}.
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DR EMBL; AF117649; AAD22030.1; -; mRNA.
DR EMBL; AE013599; AAF57788.1; -; Genomic_DNA.
DR EMBL; AL035311; CAA22952.1; -; Genomic_DNA.
DR EMBL; AY050236; AAK84935.1; -; mRNA.
DR PIR; T13577; T13577.
DR RefSeq; NP_477413.1; NM_058065.3.
DR AlphaFoldDB; Q9UAS6; -.
DR SMR; Q9UAS6; -.
DR STRING; 7227.FBpp0088518; -.
DR PaxDb; Q9UAS6; -.
DR PRIDE; Q9UAS6; -.
DR DNASU; 37034; -.
DR EnsemblMetazoa; FBtr0089549; FBpp0088518; FBgn0026309.
DR GeneID; 37034; -.
DR KEGG; dme:Dmel_CG5032; -.
DR UCSC; CG5032-RA; d. melanogaster.
DR CTD; 109861; -.
DR FlyBase; FBgn0026309; aft.
DR VEuPathDB; VectorBase:FBgn0026309; -.
DR eggNOG; KOG3674; Eukaryota.
DR HOGENOM; CLU_019427_0_0_1; -.
DR OMA; EFVTVAW; -.
DR OrthoDB; 1327262at2759; -.
DR PhylomeDB; Q9UAS6; -.
DR BioGRID-ORCS; 37034; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37034; -.
DR PRO; PR:Q9UAS6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026309; Expressed in open tracheal system and 23 other tissues.
DR ExpressionAtlas; Q9UAS6; baseline and differential.
DR Genevisible; Q9UAS6; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IMP:FlyBase.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0097309; P:cap1 mRNA methylation; IMP:FlyBase.
DR GO; GO:0097310; P:cap2 mRNA methylation; IBA:GO_Central.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..700
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 2"
FT /id="PRO_0000388728"
FT DOMAIN 109..321
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 234
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT CONFLICT 325
FT /note="D -> N (in Ref. 5; AAK84935)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="F -> S (in Ref. 5; AAK84935)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="E -> K (in Ref. 1; AAD22030)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="K -> E (in Ref. 4; CAA22952)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="Q -> R (in Ref. 4; CAA22952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 80503 MW; 3A445D5CE34587E1 CRC64;
MSFRSSPQGK PHPMTDYQSI RPSEVEQLFE KKFHYQKPKG NKSWQLPPPD QALFSEFYQF
EALQGLREQL NAVKSKLNDY GVQEWSAHTN RRDPSGEVSW RLKNDTKAEF VTVAWCKLFE
CLHRYPLVTK PAVNSMHLCE APGAFIASLN HYLHSKYEKD EIKWRWRSTT LNPYYEGNAI
NQMISDDRFI VHTLDNWFFH KDLTGNLLDV ANIDHLVERC EVEFQGQVDL VTADGSIDCA
AQPDCQEEIV VRLFFAEVLS ALRILSSGGN FLVKMFTLFE ACSVSLLYTL NCIFEEVHIF
KPATSKRGNS EVYVICLNYN KDHPDLPRLL EEIKSKLAQP NDTLVMPLFA KFQIPHDFLM
QHEIACRMYM KLQTDAIEGS IYAYESNDRH YLRHLHHLRS LVANTYYSLY KVKPLEDSLC
IVDKEATSKA LGFQVPVYGG SYTERESLKH GDLLKQIYCL RREFNQLEKC LNNRTPYSYV
KNRTAPLNLH ISRGAPVQSL QSSMFASEPI LILRLRILDT FELDPVWQSA PKCQLESKTL
CYLPPTEDEA FHTAQQRFFI DLLEEVKKLK PDSIVFHKFL FLTHYAASLL LFLIESVYQD
CCFNSNQAQT LTLSKLKDTA NSALEQVLEL LKDEQAGAIH SLLDIKELQK NQFSKALIQH
NNSIVMTCFR SMLGEESFPM PVAPTSNSDV GSIQESAAVF
