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Survival motor neuron protein

 SMN_DROME               Reviewed;         226 AA.
Q9VV74;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 154.
RecName: Full=Survival motor neuron protein {ECO:0000312|EMBL:AAG17893.1};
Name=Smn; ORFNames=CG16725;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG17893.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND DEVELOPMENTAL STAGE.
PubMed=11113446; DOI=10.1016/S0014-5793(00)02243-2;
Miguel-Aliaga I., Chan Y.B., Davies K.E., van den Heuvel M.;
"Disruption of SMN function by ectopic expression of the human SMN
gene in Drosophila.";
FEBS Lett. 486:99-102(2000).
[2] {ECO:0000312|EMBL:AAF49446.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000312|EMBL:AAF49446.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAL13758.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569,
ECO:0000312|EMBL:AAL13758.1};
TISSUE=Larva {ECO:0000269|PubMed:12537569}, and
Pupae {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF SER-201 AND GLY-202.
PubMed=12783845; DOI=10.1093/hmg/ddg157;
Chan Y.B., Miguel-Aliaga I., Franks C., Thomas N., Trulzsch B.,
Sattelle D.B., Davies K.E., van den Heuvel M.;
"Neuromuscular defects in a Drosophila survival motor neuron gene
mutant.";
Hum. Mol. Genet. 12:1367-1376(2003).
[6] {ECO:0000305}
SUBUNIT, AND INTERACTION WITH RPP20.
PubMed=14715275; DOI=10.1016/j.bbrc.2003.12.084;
Hua Y., Zhou J.;
"Rpp20 interacts with SMN and is re-distributed into SMN granules in
response to stress.";
Biochem. Biophys. Res. Commun. 314:268-276(2004).
[7] {ECO:0000305}
INTERACTION WITH SMB.
PubMed=16753561; DOI=10.1016/j.cub.2006.04.037;
Gonsalvez G.B., Rajendra T.K., Tian L., Matera A.G.;
"The Sm-protein methyltransferase, dart5, is essential for germ-cell
specification and maintenance.";
Curr. Biol. 16:1077-1089(2006).
[8] {ECO:0000305}
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16533947; DOI=10.1083/jcb.200511038;
Liu J.L., Murphy C., Buszczak M., Clatterbuck S., Goodman R.,
Gall J.G.;
"The Drosophila melanogaster Cajal body.";
J. Cell Biol. 172:875-884(2006).
[9] {ECO:0000305}
FUNCTION, SUBUNIT, INTERACTION WITH ACTN, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=17353360; DOI=10.1083/jcb.200610053;
Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K.,
Matera A.G.;
"A Drosophila melanogaster model of spinal muscular atrophy reveals a
function for SMN in striated muscle.";
J. Cell Biol. 176:831-841(2007).
[10] {ECO:0000305}
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17595295; DOI=10.1073/pnas.0704977104;
Liu J.L., Gall J.G.;
"U bodies are cytoplasmic structures that contain uridine-rich small
nuclear ribonucleoproteins and associate with P bodies.";
Proc. Natl. Acad. Sci. U.S.A. 104:11655-11659(2007).
[11] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=18791638; DOI=10.1371/journal.pone.0003209;
Chang H.C., Dimlich D.N., Yokokura T., Mukherjee A., Kankel M.W.,
Sen A., Sridhar V., Fulga T.A., Hart A.C., Van Vactor D.,
Artavanis-Tsakonas S.;
"Modeling spinal muscular atrophy in Drosophila.";
PLoS ONE 3:E3209-E3209(2008).
[12] {ECO:0000305}
FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH THE
SPLICEOSOME USNRNP PROTEINS SNRNP-U1-70K, U2A, SNF/U1A AND U5-116KD,
INTERACTION WITH THE SNRNP SM PROTEINS, AND INTERACTION WITH GEM3.
PubMed=18621711; DOI=10.1073/pnas.0802287105;
Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.;
"Evolution of an RNP assembly system: a minimal SMN complex
facilitates formation of UsnRNPs in Drosophila melanogaster.";
Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2008).
[13] {ECO:0000305}
INTERACTION WITH SMD1.
PubMed=18369183; DOI=10.1261/rna.940708;
Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.;
"Sm protein methylation is dispensable for snRNP assembly in
Drosophila melanogaster.";
RNA 14:878-887(2008).
[14] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=19464282; DOI=10.1016/j.ydbio.2009.05.553;
Lee L., Davies S.E., Liu J.L.;
"The spinal muscular atrophy protein SMN affects Drosophila germline
nuclear organization through the U body-P body pathway.";
Dev. Biol. 332:142-155(2009).
[15] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=20452345; DOI=10.1016/j.yexcr.2010.05.001;
Cauchi R.J., Sanchez-Pulido L., Liu J.L.;
"Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are
components of U bodies.";
Exp. Cell Res. 316:2354-2364(2010).
[16] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=21490958; DOI=10.1371/journal.pgen.1002030;
Grice S.J., Liu J.L.;
"Survival motor neuron protein regulates stem cell division,
proliferation, and differentiation in Drosophila.";
PLoS Genet. 7:E1002030-E1002030(2011).
[17] {ECO:0000305}
FUNCTION.
PubMed=23103409; DOI=10.1016/j.brainres.2012.10.035;
Timmerman C., Sanyal S.;
"Behavioral and electrophysiological outcomes of tissue-specific Smn
knockdown in Drosophila melanogaster.";
Brain Res. 1489:66-80(2012).
[18] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23063130; DOI=10.1016/j.cell.2012.09.011;
Imlach W.L., Beck E.S., Choi B.J., Lotti F., Pellizzoni L.,
McCabe B.D.;
"SMN is required for sensory-motor circuit function in Drosophila.";
Cell 151:427-439(2012).
[19] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23063131; DOI=10.1016/j.cell.2012.09.012;
Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K.,
Jiao W., Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.;
"An SMN-dependent U12 splicing event essential for motor circuit
function.";
Cell 151:440-454(2012).
[20] {ECO:0000305}
FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-20;
PHE-70; TYR-203; THR-205 AND GLY-206.
PubMed=22813737; DOI=10.1016/j.celrep.2012.05.014;
Praveen K., Wen Y., Matera A.G.;
"A Drosophila model of spinal muscular atrophy uncouples snRNP
biogenesis functions of survival motor neuron from locomotion and
viability defects.";
Cell Rep. 1:624-631(2012).
[21] {ECO:0000305}
FUNCTION.
PubMed=23029159; DOI=10.1371/journal.pone.0045649;
Ruiz O.E., Nikolova L.S., Metzstein M.M.;
"Drosophila Zpr1 (Zinc finger protein 1) is required downstream of
both EGFR and FGFR signaling in tracheal subcellular lumen
formation.";
PLoS ONE 7:E45649-E45649(2012).
[22] {ECO:0000305}
INTERACTION WITH MSK AND SNUP.
PubMed=23885126; DOI=10.1091/mbc.E13-03-0118;
Natalizio A.H., Matera A.G.;
"Identification and characterization of Drosophila Snurportin reveals
a role for the import receptor Moleskin/Importin7 in snRNP
biogenesis.";
Mol. Biol. Cell 24:2932-2942(2013).
[23] {ECO:0000312|PDB:4V98}
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-122, FUNCTION, AND
SUBUNIT.
PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
Stark H., Schindelin H., Fischer U.;
"Structural basis of assembly chaperone-mediated snRNP formation.";
Mol. Cell 49:692-703(2013).
-!- FUNCTION: The SMN complex plays an essential role in spliceosomal
snRNP assembly in the cytoplasm, is required for pre-mRNA splicing
in the nucleus and acts as a chaperone that discriminates target
and non-target RNAs of Sm proteins. Required for normal expression
of spliceosomal snRNAs and for U12 intron splicing. Required in
cholinergic neurons, but not in motor neurons, to ensure correct
splicing and proper levels of stas mRNA and normal
neurotransmitter release by motor neurons (PubMed:23063130 and
PubMed:23063131). However, Smn is required in motor neurons, but
not in cholinergic neurons, for normal motor behavior but plays no
role in synaptic transmission according to PubMed:23103409. In
both muscle and neurons, required for the formation of a normal
neuromuscular junction (NMJ) structure. Plays a neuron-specific
role in long-term homeostatic compensation at the larval NMJ. In
the thorax of adult flies, required for Act88F, an indirect flight
muscle (IFM)-specific actin, expression and for proper IFM
myofibril formation. In nurse cells, oocytes and follicle cells,
required to maintain normal organization of nuclear compartments
including chromosomes, nucleoli, Cajal bodies, histone locus
bodies and heterochromatin. Required for the functional integrity
of the cytoplasmic U snRNP body (U body) and P body. Required in
dividing postembryonic neuroblasts (pNBs) for the correct basal
localization of mira. The tight regulation of its expression is
critical for stem cell division, proliferation and differentiation
in male germline and developing central nervous system (CNS).
Required for tracheal terminal cell lumen formation.
{ECO:0000269|PubMed:12783845, ECO:0000269|PubMed:17353360,
ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:18791638,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:21490958,
ECO:0000269|PubMed:22813737, ECO:0000269|PubMed:23029159,
ECO:0000269|PubMed:23063130, ECO:0000269|PubMed:23063131,
ECO:0000269|PubMed:23103409, ECO:0000269|PubMed:23333303}.
-!- SUBUNIT: Homodimer (via C-terminal region) (PubMed:11113446,
PubMed:12783845, PubMed:22813737). Part of the core SMN complex,
which seems to be composed of Smn and Gem2 only (PubMed:18621711,
PubMed:23333303). The SMN complex associates with the entire set
of spliceosomal snRNP Sm proteins, SmB, SmD1, SmD2, SmD3, SmE, SmF
and SmG, and with the snRNP-specific proteins snRNP-U1-70K, U2A,
snf/U1A and U5-116KD (PubMed:18621711, PubMed:23333303).
Associates weakly with Gem3 (PubMed:18621711). Interacts with SmB
and SmD1; the interaction is favored by methylation of the Sm
proteins (PubMed:16753561, PubMed:18369183). Interacts with Actn;
the interaction occurs in thoracic tissues and in adult flies
(PubMed:17353360). Interacts with Rpp20 (PubMed:14715275).
Interacts with msk and Snup; these interactions are RNA-dependent
(PubMed:23885126). {ECO:0000269|PubMed:11113446,
ECO:0000269|PubMed:12783845, ECO:0000269|PubMed:14715275,
ECO:0000269|PubMed:16753561, ECO:0000269|PubMed:17353360,
ECO:0000269|PubMed:18369183, ECO:0000269|PubMed:18621711,
ECO:0000269|PubMed:22813737, ECO:0000269|PubMed:23333303,
ECO:0000269|PubMed:23885126}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-185315, EBI-185315;
Q9VVX0:Gem2; NbExp=5; IntAct=EBI-185315, EBI-108834;
Q2MGL3:Rpp20; NbExp=3; IntAct=EBI-185315, EBI-1151669;
Q16637:SMN2 (xeno); NbExp=2; IntAct=EBI-185315, EBI-395421;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16533947,
ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:17595295,
ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
ECO:0000269|PubMed:20452345, ECO:0000269|PubMed:21490958}.
Nucleus, gem {ECO:0000269|PubMed:16533947,
ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:17595295,
ECO:0000269|PubMed:18791638, ECO:0000269|PubMed:19464282,
ECO:0000269|PubMed:20452345, ECO:0000269|PubMed:21490958}.
Cytoplasm, myofibril, sarcomere, I band
{ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
ECO:0000269|PubMed:21490958}. Cytoplasm, myofibril, sarcomere, Z
line {ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
ECO:0000269|PubMed:21490958}. Note=Component of U bodies. High
expression detected in the cytoplasm of female germline stem cells
and cystoblast which persists up to stage 10 egg chambers.
Accumulates in the cytoplasm of dividing pNBs. Colocalizes with
Actn at the Z-line of IFMs. Expression concentrates at the post-
synaptic region of NMJs in larval brain.
{ECO:0000269|PubMed:16533947, ECO:0000269|PubMed:17353360,
ECO:0000269|PubMed:17595295, ECO:0000269|PubMed:18791638,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:20452345,
ECO:0000269|PubMed:21490958}.
-!- TISSUE SPECIFICITY: In late first instar larvae, expressed in
pNBs. Expression increases as the pNBs enlarge, with the highest
accumulation observed in dividing pNBs of second and third instar
larvae. Enriched in type ID (thoracic and brain lobe), type IA and
all the mira-expressing NBs of the brain lobes. In larvae, also
expressed in muscle fibers. In larval and adult testis, expressed
in germline stem cells and gonialblast, expression decreases as
cells differentiate into cysts and spermatocytes. In adult fly
thorax, expressed in the IFMs. In adult ovary, expressed in
germline stem cells, cystoblasts, follicle cells, nurse cells and
oocyte (at protein level). Also expressed in larval salivary
glands. {ECO:0000269|PubMed:12783845, ECO:0000269|PubMed:16533947,
ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:17595295,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:21490958}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed ubiquitously throughout development. Expression is high
during embryogenesis but decreases 30-fold in adult flies (at
protein level). {ECO:0000269|PubMed:11113446,
ECO:0000269|PubMed:12783845, ECO:0000269|PubMed:16533947,
ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:18791638}.
-!- DISRUPTION PHENOTYPE: Embryos lacking maternal and zygotic Smn die
between 0 and 4 hours after egg laying. Zygotic mutants never
initiate pupation but instead persist as third instar larvae,
often surviving at this stage for several days. Mutant larvae
exhibit reduced CNS, testes and muscle size, decreased locomotion
and altered rhythmic motor activity. At the NMJ, mutant larvae
show an overall decrease in the number of synaptic boutons, but an
increase in enlarged ones, loss of large glutamate receptor
clusters and an aberrant increase in evoked excitatory
postsynaptic potential (eEPSP) amplitude and in miniature EPSP
frequency. Mutant larvae also show defective mira subcellular
localization in pNBs. Mutant larvae show a decrease of
spliceosomal snRNA levels and splicing defects in U12 intron-
containing genes (PubMed:23063131). But appreciable splicing
defects in U12 intron-containing genes are not observed in mutant
larvae, although a decrease in spliceosomal snRNA levels is
detected, in PubMed:22813737. {ECO:0000269|PubMed:12783845,
ECO:0000269|PubMed:17353360, ECO:0000269|PubMed:18791638,
ECO:0000269|PubMed:19464282, ECO:0000269|PubMed:21490958,
ECO:0000269|PubMed:22813737, ECO:0000269|PubMed:23063130,
ECO:0000269|PubMed:23063131}.
-!- SIMILARITY: Belongs to the SMN family. {ECO:0000255}.
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EMBL; AF296281; AAG17893.1; -; mRNA.
EMBL; AE014296; AAF49446.1; -; Genomic_DNA.
EMBL; AE014296; AGB94647.1; -; Genomic_DNA.
EMBL; AY058529; AAL13758.1; -; mRNA.
RefSeq; NP_001261954.1; NM_001275025.1.
RefSeq; NP_524112.1; NM_079388.4.
UniGene; Dm.2679; -.
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.
PDBsum; 4V98; -.
ProteinModelPortal; Q9VV74; -.
SMR; Q9VV74; -.
BioGrid; 65147; 46.
DIP; DIP-18223N; -.
IntAct; Q9VV74; 11.
STRING; 7227.FBpp0302954; -.
PaxDb; Q9VV74; -.
PRIDE; Q9VV74; -.
EnsemblMetazoa; FBtr0075395; FBpp0075153; FBgn0036641.
EnsemblMetazoa; FBtr0329921; FBpp0302954; FBgn0036641.
GeneID; 39844; -.
KEGG; dme:Dmel_CG16725; -.
UCSC; CG16725-RA; d. melanogaster.
CTD; 39844; -.
FlyBase; FBgn0036641; Smn.
eggNOG; KOG4327; Eukaryota.
eggNOG; ENOG4111ME8; LUCA.
InParanoid; Q9VV74; -.
KO; K13129; -.
OMA; AAPWNSF; -.
OrthoDB; EOG091G0F71; -.
PhylomeDB; Q9VV74; -.
GenomeRNAi; 39844; -.
PRO; PR:Q9VV74; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0036641; -.
Genevisible; Q9VV74; DM.
GO; GO:0015030; C:Cajal body; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0071254; C:cytoplasmic U snRNP body; IDA:UniProtKB.
GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
GO; GO:0031674; C:I band; IDA:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IEA:GOC.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0034730; C:SmD-containing SMN-Sm protein complex; IDA:UniProtKB.
GO; GO:0032797; C:SMN complex; IGI:FlyBase.
GO; GO:0034718; C:SMN-Gemin2 complex; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0030018; C:Z disc; IDA:FlyBase.
GO; GO:0051393; F:alpha-actinin binding; IPI:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:UniProtKB.
GO; GO:0045175; P:basal protein localization; IMP:UniProtKB.
GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IMP:UniProtKB.
GO; GO:1990194; P:cytoplasmic U snRNP body assembly; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:UniProtKB.
GO; GO:0002164; P:larval development; IMP:UniProtKB.
GO; GO:0008345; P:larval locomotory behavior; IMP:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
GO; GO:0048601; P:oocyte morphogenesis; IMP:UniProtKB.
GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:UniProtKB.
GO; GO:0022618; P:ribonucleoprotein complex assembly; IMP:FlyBase.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0017145; P:stem cell division; IMP:UniProtKB.
GO; GO:0072089; P:stem cell proliferation; IMP:UniProtKB.
GO; GO:0072553; P:terminal button organization; IMP:UniProtKB.
GO; GO:0035154; P:terminal cell fate specification, open tracheal system; IMP:FlyBase.
InterPro; IPR010304; Survival_motor_neuron.
InterPro; IPR002999; Tudor.
Pfam; PF06003; SMN; 2.
SMART; SM00333; TUDOR; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
mRNA processing; mRNA splicing; Nucleus; Reference proteome;
Spliceosome.
CHAIN 1 226 Survival motor neuron protein.
/FTId=PRO_0000424374.
DOMAIN 69 128 Tudor. {ECO:0000255}.
REGION 159 226 Required for homodimerization.
{ECO:0000269|PubMed:11113446}.
MUTAGEN 20 20 D->V: Does not affect homodimer
formation. {ECO:0000269|PubMed:22813737}.
MUTAGEN 70 70 F->S: Does not affect homodimer
formation. {ECO:0000269|PubMed:22813737}.
MUTAGEN 201 201 S->F: In allele Smn-B; homozygous lethal
at late larval stages and abolishes
homodimerization.
{ECO:0000269|PubMed:12783845}.
MUTAGEN 202 202 G->S: In allele Smn-73Ao; homozygous
lethal at late larval stages and
abolishes homodimerization.
{ECO:0000269|PubMed:12783845}.
MUTAGEN 203 203 Y->C: Weakly inhibits homodimer
formation. {ECO:0000269|PubMed:22813737}.
MUTAGEN 205 205 T->I: Rescues larval viability and
locomotion defects and only partially
restores U5 and U12 snRNA levels in the
null mutant. Weakly inhibits homodimer
formation. Does not affect protein
stability. {ECO:0000269|PubMed:22813737}.
MUTAGEN 206 206 G->S: Inhibits homodimer formation.
{ECO:0000269|PubMed:22813737}.
HELIX 15 23 {ECO:0000244|PDB:4V98}.
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


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