MT2_DROME
ID MT2_DROME Reviewed; 43 AA.
AC P11956; Q1ECC1; Q9VDM2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Metallothionein-2;
DE Short=MT-2;
DE AltName: Full=Metallothionein B;
GN Name=MtnB; Synonyms=Mto; ORFNames=CG4312;
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].
RC STRAIN=Oregon-R;
RX PubMed=3106973; DOI=10.1073/pnas.84.9.2658;
RA Mokdad R., Debec A., Wegnez M.;
RT "Metallothionein genes in Drosophila melanogaster constitute a dual
RT system.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2658-2662(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], BLOCKAGE OF N-TERMINUS, AND PROTEIN
RP SEQUENCE OF 3-27.
RC STRAIN=Oregon-R;
RX PubMed=1976815; DOI=10.1016/s0022-2836(05)80340-7;
RA Silar P., Theodore L., Mokdad R., Erraiss N.-E., Cadic A., Wegnez M.;
RT "Metallothionein Mto gene of Drosophila melanogaster: structure and
RT regulation.";
RL J. Mol. Biol. 215:217-224(1990).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein binds cations of several transition elements.
CC Thought to be involved in metal ion homeostasis.
CC -!- INTERACTION:
CC P11956; Q1WWB7: betaG; NbExp=2; IntAct=EBI-88468, EBI-130849;
CC P11956; Q9V3P0: Jafrac1; NbExp=2; IntAct=EBI-88468, EBI-82319;
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly in embryonic and larval
CC stages.
CC -!- INDUCTION: Strongly induced by cadmium, copper and mercury.
CC -!- DOMAIN: All cysteine residues are arranged in C-X-C groups. These are
CC thought to be the metal-binding sites in other metallothioneins.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 5 family.
CC {ECO:0000305}.
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DR EMBL; M16250; AAA28683.1; -; mRNA.
DR EMBL; X52098; CAA36318.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55768.1; -; Genomic_DNA.
DR EMBL; BT025813; ABF85713.1; -; mRNA.
DR PIR; S14706; SMFF2.
DR RefSeq; NP_001287425.1; NM_001300496.1.
DR RefSeq; NP_001287426.1; NM_001300497.1.
DR RefSeq; NP_524413.1; NM_079689.3.
DR AlphaFoldDB; P11956; -.
DR BioGRID; 67404; 8.
DR DIP; DIP-20926N; -.
DR IntAct; P11956; 3.
DR STRING; 7227.FBpp0083298; -.
DR PaxDb; P11956; -.
DR DNASU; 42424; -.
DR EnsemblMetazoa; FBtr0083890; FBpp0083298; FBgn0002869.
DR EnsemblMetazoa; FBtr0346152; FBpp0311980; FBgn0002869.
DR EnsemblMetazoa; FBtr0346153; FBpp0311981; FBgn0002869.
DR GeneID; 42424; -.
DR KEGG; dme:Dmel_CG4312; -.
DR CTD; 42424; -.
DR FlyBase; FBgn0002869; MtnB.
DR VEuPathDB; VectorBase:FBgn0002869; -.
DR eggNOG; KOG4738; Eukaryota.
DR HOGENOM; CLU_217426_0_0_1; -.
DR InParanoid; P11956; -.
DR OrthoDB; 1625823at2759; -.
DR PhylomeDB; P11956; -.
DR BioGRID-ORCS; 42424; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42424; -.
DR PRO; PR:P11956; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002869; Expressed in midgut and 23 other tissues.
DR ExpressionAtlas; P11956; differential.
DR Genevisible; P11956; DM.
DR GO; GO:0005507; F:copper ion binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IDA:FlyBase.
DR GO; GO:0055065; P:metal ion homeostasis; IMP:FlyBase.
DR GO; GO:0010038; P:response to metal ion; IDA:FlyBase.
DR InterPro; IPR000966; Metalthion_5.
DR Pfam; PF02067; Metallothio_5; 1.
DR PRINTS; PR00872; MTDIPTERA.
PE 1: Evidence at protein level;
KW Cadmium; Copper; Direct protein sequencing; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..43
FT /note="Metallothionein-2"
FT /id="PRO_0000197355"
FT MOD_RES 1
FT /note="Blocked amino end (Met)"
SQ SEQUENCE 43 AA; 4525 MW; 5EE0CF9171BD9A97 CRC64;
MVCKGCGTNC QCSAQKCGDN CACNKDCQCV CKNGPKDQCC SNK
