SMN_DROME
ID SMN_DROME Reviewed; 226 AA.
AC Q9VV74;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Survival motor neuron protein {ECO:0000312|EMBL:AAG17893.1};
GN Name=Smn; ORFNames=CG16725;
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] {ECO:0000305, ECO:0000312|EMBL:AAG17893.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=11113446; DOI=10.1016/s0014-5793(00)02243-2;
RA Miguel-Aliaga I., Chan Y.B., Davies K.E., van den Heuvel M.;
RT "Disruption of SMN function by ectopic expression of the human SMN gene in
RT Drosophila.";
RL FEBS Lett. 486:99-102(2000).
RN [2] {ECO:0000312|EMBL:AAF49446.1}
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 [3] {ECO:0000312|EMBL:AAF49446.1}
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] {ECO:0000312|EMBL:AAL13758.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569, ECO:0000312|EMBL:AAL13758.1};
RC TISSUE=Larva {ECO:0000269|PubMed:12537569}, and
RC Pupae {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF SER-201 AND GLY-202.
RX PubMed=12783845; DOI=10.1093/hmg/ddg157;
RA Chan Y.B., Miguel-Aliaga I., Franks C., Thomas N., Trulzsch B.,
RA Sattelle D.B., Davies K.E., van den Heuvel M.;
RT "Neuromuscular defects in a Drosophila survival motor neuron gene mutant.";
RL Hum. Mol. Genet. 12:1367-1376(2003).
RN [6] {ECO:0000305}
RP SUBUNIT, AND INTERACTION WITH RPP20.
RX PubMed=14715275; DOI=10.1016/j.bbrc.2003.12.084;
RA Hua Y., Zhou J.;
RT "Rpp20 interacts with SMN and is re-distributed into SMN granules in
RT response to stress.";
RL Biochem. Biophys. Res. Commun. 314:268-276(2004).
RN [7] {ECO:0000305}
RP INTERACTION WITH SMB.
RX PubMed=16753561; DOI=10.1016/j.cub.2006.04.037;
RA Gonsalvez G.B., Rajendra T.K., Tian L., Matera A.G.;
RT "The Sm-protein methyltransferase, dart5, is essential for germ-cell
RT specification and maintenance.";
RL Curr. Biol. 16:1077-1089(2006).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16533947; DOI=10.1083/jcb.200511038;
RA Liu J.L., Murphy C., Buszczak M., Clatterbuck S., Goodman R., Gall J.G.;
RT "The Drosophila melanogaster Cajal body.";
RL J. Cell Biol. 172:875-884(2006).
RN [9] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH ACTN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17353360; DOI=10.1083/jcb.200610053;
RA Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K.,
RA Matera A.G.;
RT "A Drosophila melanogaster model of spinal muscular atrophy reveals a
RT function for SMN in striated muscle.";
RL J. Cell Biol. 176:831-841(2007).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17595295; DOI=10.1073/pnas.0704977104;
RA Liu J.L., Gall J.G.;
RT "U bodies are cytoplasmic structures that contain uridine-rich small
RT nuclear ribonucleoproteins and associate with P bodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11655-11659(2007).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18791638; DOI=10.1371/journal.pone.0003209;
RA Chang H.C., Dimlich D.N., Yokokura T., Mukherjee A., Kankel M.W., Sen A.,
RA Sridhar V., Fulga T.A., Hart A.C., Van Vactor D., Artavanis-Tsakonas S.;
RT "Modeling spinal muscular atrophy in Drosophila.";
RL PLoS ONE 3:E3209-E3209(2008).
RN [12] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH THE
RP SPLICEOSOME USNRNP PROTEINS SNRNP-U1-70K, U2A, SNF/U1A AND U5-116KD,
RP INTERACTION WITH THE SNRNP SM PROTEINS, AND INTERACTION WITH GEM3.
RX PubMed=18621711; DOI=10.1073/pnas.0802287105;
RA Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.;
RT "Evolution of an RNP assembly system: a minimal SMN complex facilitates
RT formation of UsnRNPs in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2008).
RN [13] {ECO:0000305}
RP INTERACTION WITH SMD1.
RX PubMed=18369183; DOI=10.1261/rna.940708;
RA Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.;
RT "Sm protein methylation is dispensable for snRNP assembly in Drosophila
RT melanogaster.";
RL RNA 14:878-887(2008).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19464282; DOI=10.1016/j.ydbio.2009.05.553;
RA Lee L., Davies S.E., Liu J.L.;
RT "The spinal muscular atrophy protein SMN affects Drosophila germline
RT nuclear organization through the U body-P body pathway.";
RL Dev. Biol. 332:142-155(2009).
RN [15] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=20452345; DOI=10.1016/j.yexcr.2010.05.001;
RA Cauchi R.J., Sanchez-Pulido L., Liu J.L.;
RT "Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components
RT of U bodies.";
RL Exp. Cell Res. 316:2354-2364(2010).
RN [16] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21490958; DOI=10.1371/journal.pgen.1002030;
RA Grice S.J., Liu J.L.;
RT "Survival motor neuron protein regulates stem cell division, proliferation,
RT and differentiation in Drosophila.";
RL PLoS Genet. 7:E1002030-E1002030(2011).
RN [17] {ECO:0000305}
RP FUNCTION.
RX PubMed=23103409; DOI=10.1016/j.brainres.2012.10.035;
RA Timmerman C., Sanyal S.;
RT "Behavioral and electrophysiological outcomes of tissue-specific Smn
RT knockdown in Drosophila melanogaster.";
RL Brain Res. 1489:66-80(2012).
RN [18] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23063130; DOI=10.1016/j.cell.2012.09.011;
RA Imlach W.L., Beck E.S., Choi B.J., Lotti F., Pellizzoni L., McCabe B.D.;
RT "SMN is required for sensory-motor circuit function in Drosophila.";
RL Cell 151:427-439(2012).
RN [19] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23063131; DOI=10.1016/j.cell.2012.09.012;
RA Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W.,
RA Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.;
RT "An SMN-dependent U12 splicing event essential for motor circuit
RT function.";
RL Cell 151:440-454(2012).
RN [20] {ECO:0000305}
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-20; PHE-70;
RP TYR-203; THR-205 AND GLY-206.
RX PubMed=22813737; DOI=10.1016/j.celrep.2012.05.014;
RA Praveen K., Wen Y., Matera A.G.;
RT "A Drosophila model of spinal muscular atrophy uncouples snRNP biogenesis
RT functions of survival motor neuron from locomotion and viability defects.";
RL Cell Rep. 1:624-631(2012).
RN [21] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23029159; DOI=10.1371/journal.pone.0045649;
RA Ruiz O.E., Nikolova L.S., Metzstein M.M.;
RT "Drosophila Zpr1 (Zinc finger protein 1) is required downstream of both
RT EGFR and FGFR signaling in tracheal subcellular lumen formation.";
RL PLoS ONE 7:E45649-E45649(2012).
RN [22] {ECO:0000305}
RP INTERACTION WITH MSK AND SNUP.
RX PubMed=23885126; DOI=10.1091/mbc.e13-03-0118;
RA Natalizio A.H., Matera A.G.;
RT "Identification and characterization of Drosophila Snurportin reveals a
RT role for the import receptor Moleskin/Importin7 in snRNP biogenesis.";
RL Mol. Biol. Cell 24:2932-2942(2013).
RN [23] {ECO:0000312|PDB:4V98}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-122, FUNCTION, AND SUBUNIT.
RX PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
RA Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
RA Stark H., Schindelin H., Fischer U.;
RT "Structural basis of assembly chaperone-mediated snRNP formation.";
RL Mol. Cell 49:692-703(2013).
CC -!- FUNCTION: The SMN complex plays an essential role in spliceosomal snRNP
CC assembly in the cytoplasm, is required for pre-mRNA splicing in the
CC nucleus and acts as a chaperone that discriminates target and non-
CC target RNAs of Sm proteins. Required for normal expression of
CC spliceosomal snRNAs and for U12 intron splicing. Required in
CC cholinergic neurons, but not in motor neurons, to ensure correct
CC splicing and proper levels of stas mRNA and normal neurotransmitter
CC release by motor neurons (PubMed:23063130 and PubMed:23063131).
CC However, Smn is required in motor neurons, but not in cholinergic
CC neurons, for normal motor behavior but plays no role in synaptic
CC transmission according to PubMed:23103409. In both muscle and neurons,
CC required for the formation of a normal neuromuscular junction (NMJ)
CC structure. Plays a neuron-specific role in long-term homeostatic
CC compensation at the larval NMJ. In the thorax of adult flies, required
CC for Act88F, an indirect flight muscle (IFM)-specific actin, expression
CC and for proper IFM myofibril formation. In nurse cells, oocytes and
CC follicle cells, required to maintain normal organization of nuclear
CC compartments including chromosomes, nucleoli, Cajal bodies, histone
CC locus bodies and heterochromatin. Required for the functional integrity
CC of the cytoplasmic U snRNP body (U body) and P body. Required in
CC dividing postembryonic neuroblasts (pNBs) for the correct basal
CC localization of mira. The tight regulation of its expression is
CC critical for stem cell division, proliferation and differentiation in
CC male germline and developing central nervous system (CNS). Required for
CC tracheal terminal cell lumen formation. {ECO:0000269|PubMed:12783845,
CC ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:18621711,
CC ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
CC ECO:0000269|PubMed:21490958, ECO:0000269|PubMed:22813737,
CC ECO:0000269|PubMed:23029159, ECO:0000269|PubMed:23063130,
CC ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:23103409,
CC ECO:0000269|PubMed:23333303}.
CC -!- SUBUNIT: Homodimer (via C-terminal region) (PubMed:11113446,
CC PubMed:12783845, PubMed:22813737). Part of the core SMN complex, which
CC seems to be composed of Smn and Gem2 only (PubMed:18621711,
CC PubMed:23333303). The SMN complex associates with the entire set of
CC spliceosomal snRNP Sm proteins, SmB, SmD1, SmD2, SmD3, SmE, SmF and
CC SmG, and with the snRNP-specific proteins snRNP-U1-70K, U2A, snf/U1A
CC and U5-116KD (PubMed:18621711, PubMed:23333303). Associates weakly with
CC Gem3 (PubMed:18621711). Interacts with SmB and SmD1; the interaction is
CC favored by methylation of the Sm proteins (PubMed:16753561,
CC PubMed:18369183). Interacts with Actn; the interaction occurs in
CC thoracic tissues and in adult flies (PubMed:17353360). Interacts with
CC Rpp20 (PubMed:14715275). Interacts with msk and Snup; these
CC interactions are RNA-dependent (PubMed:23885126).
CC {ECO:0000269|PubMed:11113446, ECO:0000269|PubMed:12783845,
CC ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:16753561,
CC ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:18369183,
CC ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:22813737,
CC ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:23885126}.
CC -!- INTERACTION:
CC Q9VV74; Q9VVX0: Gem2; NbExp=5; IntAct=EBI-185315, EBI-108834;
CC Q9VV74; Q2MGL3: Rpp20; NbExp=3; IntAct=EBI-185315, EBI-1151669;
CC Q9VV74; Q9VV74: Smn; NbExp=4; IntAct=EBI-185315, EBI-185315;
CC Q9VV74; Q16637: SMN2; Xeno; NbExp=2; IntAct=EBI-185315, EBI-395421;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16533947,
CC ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:17595295,
CC ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
CC ECO:0000269|PubMed:20452345, ECO:0000269|PubMed:21490958}. Nucleus, gem
CC {ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
CC ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
CC ECO:0000269|PubMed:21490958}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
CC ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
CC ECO:0000269|PubMed:21490958}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
CC ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
CC ECO:0000269|PubMed:21490958}. Note=Component of U bodies. High
CC expression detected in the cytoplasm of female germline stem cells and
CC cystoblast which persists up to stage 10 egg chambers. Accumulates in
CC the cytoplasm of dividing pNBs. Colocalizes with Actn at the Z-line of
CC IFMs. Expression concentrates at the post-synaptic region of NMJs in
CC larval brain. {ECO:0000269|PubMed:16533947,
CC ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:17595295,
CC ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
CC ECO:0000269|PubMed:20452345, ECO:0000269|PubMed:21490958}.
CC -!- TISSUE SPECIFICITY: In late first instar larvae, expressed in pNBs.
CC Expression increases as the pNBs enlarge, with the highest accumulation
CC observed in dividing pNBs of second and third instar larvae. Enriched
CC in type ID (thoracic and brain lobe), type IA and all the mira-
CC expressing NBs of the brain lobes. In larvae, also expressed in muscle
CC fibers. In larval and adult testis, expressed in germline stem cells
CC and gonialblast, expression decreases as cells differentiate into cysts
CC and spermatocytes. In adult fly thorax, expressed in the IFMs. In adult
CC ovary, expressed in germline stem cells, cystoblasts, follicle cells,
CC nurse cells and oocyte (at protein level). Also expressed in larval
CC salivary glands. {ECO:0000269|PubMed:12783845,
CC ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:19464282,
CC ECO:0000269|PubMed:21490958}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed ubiquitously throughout development. Expression is high
CC during embryogenesis but decreases 30-fold in adult flies (at protein
CC level). {ECO:0000269|PubMed:11113446, ECO:0000269|PubMed:12783845,
CC ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:18791638}.
CC -!- DISRUPTION PHENOTYPE: Embryos lacking maternal and zygotic Smn die
CC between 0 and 4 hours after egg laying. Zygotic mutants never initiate
CC pupation but instead persist as third instar larvae, often surviving at
CC this stage for several days. Mutant larvae exhibit reduced CNS, testes
CC and muscle size, decreased locomotion and altered rhythmic motor
CC activity. At the NMJ, mutant larvae show an overall decrease in the
CC number of synaptic boutons, but an increase in enlarged ones, loss of
CC large glutamate receptor clusters and an aberrant increase in evoked
CC excitatory postsynaptic potential (eEPSP) amplitude and in miniature
CC EPSP frequency. Mutant larvae also show defective mira subcellular
CC localization in pNBs. Mutant larvae show a decrease of spliceosomal
CC snRNA levels and splicing defects in U12 intron-containing genes
CC (PubMed:23063131). But appreciable splicing defects in U12 intron-
CC containing genes are not observed in mutant larvae, although a decrease
CC in spliceosomal snRNA levels is detected, in PubMed:22813737. RNAi-
CC mediated knockdown in tracheal cells results in defective gas-filling
CC lumen in terminal branches (PubMed:23029159).
CC {ECO:0000269|PubMed:12783845, ECO:0000269|PubMed:17353360,
CC ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
CC ECO:0000269|PubMed:21490958, ECO:0000269|PubMed:22813737,
CC ECO:0000269|PubMed:23029159, ECO:0000269|PubMed:23063130,
CC ECO:0000269|PubMed:23063131}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF296281; AAG17893.1; -; mRNA.
DR EMBL; AE014296; AAF49446.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94647.1; -; Genomic_DNA.
DR EMBL; AY058529; AAL13758.1; -; mRNA.
DR RefSeq; NP_001261954.1; NM_001275025.1.
DR RefSeq; NP_524112.1; NM_079388.4.
DR PDB; 4V98; X-ray; 3.10 A; A1/AE/AM/AU/Ac/Ak/As/B1/BE/BM/BU/Bc/Bk/Bs/CE/CM/CU/Cc/Ck/Cs=1-122.
DR PDBsum; 4V98; -.
DR AlphaFoldDB; Q9VV74; -.
DR SASBDB; Q9VV74; -.
DR SMR; Q9VV74; -.
DR BioGRID; 65147; 58.
DR DIP; DIP-18223N; -.
DR IntAct; Q9VV74; 8.
DR STRING; 7227.FBpp0302954; -.
DR PaxDb; Q9VV74; -.
DR PRIDE; Q9VV74; -.
DR ABCD; Q9VV74; 1 sequenced antibody.
DR DNASU; 39844; -.
DR EnsemblMetazoa; FBtr0075395; FBpp0075153; FBgn0036641.
DR EnsemblMetazoa; FBtr0329921; FBpp0302954; FBgn0036641.
DR GeneID; 39844; -.
DR KEGG; dme:Dmel_CG16725; -.
DR UCSC; CG16725-RA; d. melanogaster.
DR CTD; 39844; -.
DR FlyBase; FBgn0036641; Smn.
DR VEuPathDB; VectorBase:FBgn0036641; -.
DR eggNOG; KOG4327; Eukaryota.
DR GeneTree; ENSGT00940000153352; -.
DR HOGENOM; CLU_077852_0_0_1; -.
DR InParanoid; Q9VV74; -.
DR OMA; LMAWYMS; -.
DR OrthoDB; 1316275at2759; -.
DR PhylomeDB; Q9VV74; -.
DR SignaLink; Q9VV74; -.
DR BioGRID-ORCS; 39844; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39844; -.
DR PRO; PR:Q9VV74; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036641; Expressed in eye disc (Drosophila) and 33 other tissues.
DR Genevisible; Q9VV74; DM.
DR GO; GO:0015030; C:Cajal body; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071254; C:cytoplasmic U snRNP body; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
DR GO; GO:0031674; C:I band; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0034730; C:SmD-containing SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IDA:FlyBase.
DR GO; GO:0034718; C:SMN-Gemin2 complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:UniProtKB.
DR GO; GO:0045175; P:basal protein localization; IMP:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
DR GO; GO:1990194; P:cytoplasmic U snRNP body assembly; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0002164; P:larval development; IMP:UniProtKB.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:UniProtKB.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:0048601; P:oocyte morphogenesis; IMP:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IMP:UniProtKB.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:UniProtKB.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IMP:FlyBase.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0017145; P:stem cell division; IMP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0072553; P:terminal button organization; IMP:UniProtKB.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF06003; SMN; 2.
DR SMART; SM00333; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..226
FT /note="Survival motor neuron protein"
FT /id="PRO_0000424374"
FT DOMAIN 69..128
FT /note="Tudor"
FT /evidence="ECO:0000255"
FT REGION 35..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..226
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:11113446"
FT MUTAGEN 20
FT /note="D->V: Does not affect homodimer formation."
FT /evidence="ECO:0000269|PubMed:22813737"
FT MUTAGEN 70
FT /note="F->S: Does not affect homodimer formation."
FT /evidence="ECO:0000269|PubMed:22813737"
FT MUTAGEN 201
FT /note="S->F: In allele Smn-B; homozygous lethal at late
FT larval stages and abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:12783845"
FT MUTAGEN 202
FT /note="G->S: In allele Smn-73Ao; homozygous lethal at late
FT larval stages and abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:12783845"
FT MUTAGEN 203
FT /note="Y->C: Weakly inhibits homodimer formation."
FT /evidence="ECO:0000269|PubMed:22813737"
FT MUTAGEN 205
FT /note="T->I: Rescues larval viability and locomotion
FT defects and only partially restores U5 and U12 snRNA levels
FT in the null mutant. Weakly inhibits homodimer formation.
FT Does not affect protein stability."
FT /evidence="ECO:0000269|PubMed:22813737"
FT MUTAGEN 206
FT /note="G->S: Inhibits homodimer formation."
FT /evidence="ECO:0000269|PubMed:22813737"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:4V98"
SQ SEQUENCE 226 AA; 24622 MW; 9F00D85A3E9614C7 CRC64;
MSDETNAAVW DDSLLVKTYD ESVGLAREAL ARRLADSTNK REEENAAAAE EEAGEISATG
GATSPEPVSF KVGDYARATY VDGVDYEGAV VSINEEKGTC VLRYLGYENE QEVLLVDLLP
SWGKRVRREQ FLIAKKDEDE QLSRPKASAG SHSKTPKSSR RSRISGGLVM PPMPPVPPMI
VGQGDGAEQD FVAMLTAWYM SGYYTGLYQG KKEASTTSGK KKTPKK
