MLP2_DROME
ID MLP2_DROME Reviewed; 495 AA.
AC Q24400; A4V2J1; Q9VI62;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Muscle LIM protein Mlp84B {ECO:0000303|PubMed:8794860};
GN Name=Mlp84B {ECO:0000303|PubMed:8794860, ECO:0000312|FlyBase:FBgn0014863};
GN Synonyms=LIM3 {ECO:0000312|FlyBase:FBgn0014863};
GN ORFNames=CG1019 {ECO:0000312|FlyBase:FBgn0014863};
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, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8794860; DOI=10.1083/jcb.134.5.1179;
RA Stronach B.E., Siegrist S.E., Beckerle M.C.;
RT "Two muscle-specific LIM proteins in Drosophila.";
RL J. Cell Biol. 134:1179-1195(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10397768; DOI=10.1091/mbc.10.7.2329;
RA Stronach B.E., Renfranz P.J., Lilly B., Beckerle M.C.;
RT "Muscle LIM proteins are associated with muscle sarcomeres and require
RT dMEF2 for their expression during Drosophila myogenesis.";
RL Mol. Biol. Cell 10:2329-2342(1999).
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; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:ALI30537.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Qian G., Yu M.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in cell differentiation late in myogenesis.
CC Transcription factor Mef2 is essential for expression.
CC {ECO:0000269|PubMed:10397768, ECO:0000269|PubMed:8794860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8794860}. Nucleus
CC {ECO:0000269|PubMed:8794860}.
CC -!- TISSUE SPECIFICITY: In the embryo, expression is restricted to the
CC somatic, visceral, and pharyngeal muscles. Within the somatic
CC musculature, expression is localized at the ends of muscles fibers at
CC the point of attachment to the epidermis (at protein level). There is
CC no expression in cardiac mesoderm or in fat body.
CC {ECO:0000269|PubMed:10397768, ECO:0000269|PubMed:8794860}.
CC -!- DEVELOPMENTAL STAGE: Expression is biphasic, peaking late in
CC embryogenesis (16-24 hours embryos) and during the larval to pupal
CC transition, when the musculature is differentiating. Found in
CC developing muscles of the visceral and somatic mesoderm subsequent to
CC the formation of the muscle precursor cells. Decreased levels are still
CC detectable in adults. {ECO:0000269|PubMed:8794860}.
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DR EMBL; X91245; CAA62627.1; -; mRNA.
DR EMBL; AF090832; AAC61591.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54063.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54064.1; -; Genomic_DNA.
DR EMBL; AE014297; ALI30537.1; -; Genomic_DNA.
DR EMBL; BT003202; AAO24957.1; -; mRNA.
DR RefSeq; NP_001303418.1; NM_001316489.1.
DR RefSeq; NP_477122.1; NM_057774.5.
DR RefSeq; NP_731134.1; NM_169173.3.
DR AlphaFoldDB; Q24400; -.
DR BioGRID; 66046; 32.
DR DIP; DIP-17587N; -.
DR IntAct; Q24400; 7.
DR STRING; 7227.FBpp0081133; -.
DR PaxDb; Q24400; -.
DR PRIDE; Q24400; -.
DR DNASU; 40849; -.
DR EnsemblMetazoa; FBtr0081616; FBpp0081133; FBgn0014863.
DR EnsemblMetazoa; FBtr0081617; FBpp0081134; FBgn0014863.
DR EnsemblMetazoa; FBtr0346967; FBpp0312428; FBgn0014863.
DR GeneID; 40849; -.
DR KEGG; dme:Dmel_CG1019; -.
DR UCSC; CG1019-RB; d. melanogaster.
DR CTD; 40849; -.
DR FlyBase; FBgn0014863; Mlp84B.
DR VEuPathDB; VectorBase:FBgn0014863; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000171011; -.
DR HOGENOM; CLU_037060_0_0_1; -.
DR InParanoid; Q24400; -.
DR OMA; EIHCRAC; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; Q24400; -.
DR SignaLink; Q24400; -.
DR BioGRID-ORCS; 40849; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40849; -.
DR PRO; PR:Q24400; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0014863; Expressed in oviduct (Drosophila) and 23 other tissues.
DR Genevisible; Q24400; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0060537; P:muscle tissue development; IEP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:FlyBase.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 5.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 5.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; LIM domain;
KW Metal-binding; Myogenesis; Nucleus; Reference proteome; Repeat; Zinc.
FT CHAIN 1..495
FT /note="Muscle LIM protein Mlp84B"
FT /id="PRO_0000075852"
FT DOMAIN 12..63
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 120..172
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 222..274
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 325..377
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 421..473
FT /note="LIM zinc-binding 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOTIF 66..71
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 175..180
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 53526 MW; 2E559B9178E54C0E CRC64;
MPSFQPIEAP KCPRCGKSVY AAEERLAGGY VFHKNCFKCG MCNKSLDSTN CTEHERELYC
KTCHGRKFGP KGYGFGTGAG TLSMDNGSQF LRENGDVPSV RNGARLEPRA IARAPEGEGC
PRCGGYVYAA EQMLARGRSW HKECFKCGTC KKGLDSILCC EAPDKNIYCK GCYAKKFGPK
GYGYGQGGGA LQSDCYAHDD GAPQIRAAID VDKIQARPGE GCPRCGGVVY AAEQKLSKGR
EWHKKCFNCK DCHKTLDSIN ASDGPDRDVY CRTCYGKKWG PHGYGFACGS GFLQTDGLTE
DQISANRPFY NPDTTSIKAR DGEGCPRCGG AVFAAEQQLS KGKVWHKKCY NCADCHRPLD
SVLACDGPDG DIHCRACYGK LFGPKGFGYG HAPTLVSTSG ESTIQFPDGR PLAGPKTSGG
CPRCGFAVFA AEQMISKTRI WHKRCFYCSD CRKSLDSTNL NDGPDGDIYC RACYGRNFGP
KGVGYGLGAG ALTTF
