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Smu-2 suppressor of mec-8 and unc-52 protein (RED homolog) (Suppressor of Mec and Unc defects 2)

 SMU2_CAEEL              Reviewed;         547 AA.
Q9N4U5;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 100.
RecName: Full=Smu-2 suppressor of mec-8 and unc-52 protein {ECO:0000305};
AltName: Full=RED homolog {ECO:0000303|PubMed:27150041};
AltName: Full=Suppressor of Mec and Unc defects 2 {ECO:0000305};
Name=smu-2 {ECO:0000312|WormBase:Y49F6B.4};
ORFNames=Y49F6B.4 {ECO:0000312|WormBase:Y49F6B.4};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:CCD64715.1, ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD64715.1,
ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMU-1, DISRUPTION
PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=15254247; DOI=10.1128/MCB.24.15.6811-6823.2004;
Spartz A.K., Herman R.K., Shaw J.E.;
"SMU-2 and SMU-1, Caenorhabditis elegans homologs of mammalian
spliceosome-associated proteins RED and fSAP57, work together to
affect splice site choice.";
Mol. Cell. Biol. 24:6811-6823(2004).
[3] {ECO:0000244|PDB:5EN6, ECO:0000244|PDB:5EN7}
X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 163-223 IN COMPLEX WITH
SMU-1, INTERACTION WITH SMU-1, DOMAIN, AND MUTAGENESIS OF VAL-212 AND
PHE-220.
PubMed=27150041; DOI=10.1016/j.str.2016.03.016;
Ulrich A.K., Schulz J.F., Kamprad A., Schuetze T., Wahl M.C.;
"Structural Basis for the Functional Coupling of the Alternative
Splicing Factors Smu1 and RED.";
Structure 24:762-773(2016).
-!- FUNCTION: Auxiliary spliceosomal protein that regulates selection
of alternative splice sites in a small set of target pre-mRNA
species (Probable). Selectively regulates alternative splicing of
unc-52 exon 17. Thus, smu-2 mutants selectively suppress the
effects of unc-52 nonsense mutations in exon 17 by promoting the
accumulation of unc-52 isoforms that lack exon 17. In contrast,
smu-2 mutants do not suppress the effects of an unc-52 mutation
that affects the 5' splice site of exon 16. Required for normal
accumulation of smu-1 (PubMed:15254247).
{ECO:0000269|PubMed:15254247, ECO:0000305}.
-!- SUBUNIT: Probable component of the spliceosome (By similarity).
Heterotetramer with smu-1 (PubMed:27150041). The smu-1 homodimer
interacts (via the N-terminal region including the LisH and CTLH
domains) with smu-2, giving rise to a heterotetramer
(PubMed:15254247, PubMed:27150041). {ECO:0000250|UniProtKB:Q13123,
ECO:0000269|PubMed:15254247, ECO:0000269|PubMed:27150041}.
-!- INTERACTION:
G5EEG7:smu-1; NbExp=6; IntAct=EBI-2415311, EBI-2411547;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15254247}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15254247}.
-!- DEVELOPMENTAL STAGE: Detected at all stages of development, during
early embryogenesis and in oocytes, in larvae and adults.
{ECO:0000269|PubMed:15254247}.
-!- DOMAIN: Intrinsically disordered protein (Probable).
{ECO:0000305|PubMed:27150041}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown gives rise to no
visible phenotype in wild-type, but suppresses the effects of unc-
52 mutations. {ECO:0000269|PubMed:15254247}.
-!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
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EMBL; BX284602; CCD64715.1; -; Genomic_DNA.
RefSeq; NP_494559.1; NM_062158.4.
UniGene; Cel.22720; -.
PDB; 5EN6; X-ray; 3.10 A; C/D=163-223.
PDB; 5EN7; X-ray; 2.94 A; B/D/F/H=163-223.
PDBsum; 5EN6; -.
PDBsum; 5EN7; -.
ProteinModelPortal; Q9N4U5; -.
SMR; Q9N4U5; -.
DIP; DIP-55152N; -.
IntAct; Q9N4U5; 3.
STRING; 6239.Y49F6B.4; -.
EPD; Q9N4U5; -.
PaxDb; Q9N4U5; -.
PeptideAtlas; Q9N4U5; -.
EnsemblMetazoa; Y49F6B.4; Y49F6B.4; WBGene00004896.
GeneID; 173693; -.
KEGG; cel:CELE_Y49F6B.4; -.
UCSC; Y49F6B.4; c. elegans.
CTD; 173693; -.
WormBase; Y49F6B.4; CE25338; WBGene00004896; smu-2.
eggNOG; KOG2498; Eukaryota.
eggNOG; ENOG410YR3Z; LUCA.
GeneTree; ENSGT00630000089902; -.
HOGENOM; HOG000007717; -.
InParanoid; Q9N4U5; -.
KO; K13109; -.
OMA; LEEMNDA; -.
OrthoDB; EOG091G0BYA; -.
PhylomeDB; Q9N4U5; -.
PRO; PR:Q9N4U5; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00004896; Expressed in 5 organ(s), highest expression level in material anatomical entity.
GO; GO:0005730; C:nucleolus; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0040011; P:locomotion; IGI:WormBase.
GO; GO:0007638; P:mechanosensory behavior; IGI:WormBase.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0048644; P:muscle organ morphogenesis; IGI:WormBase.
GO; GO:0002119; P:nematode larval development; IGI:WormBase.
GO; GO:0048666; P:neuron development; IGI:WormBase.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:WormBase.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
InterPro; IPR012492; RED_C.
InterPro; IPR012916; RED_N.
Pfam; PF07807; RED_C; 1.
Pfam; PF07808; RED_N; 1.
ProDom; PD311621; RED_C; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; mRNA processing;
mRNA splicing; Nucleus; Reference proteome; Repeat; Spliceosome.
CHAIN 1 547 Smu-2 suppressor of mec-8 and unc-52
protein.
/FTId=PRO_0000441749.
REPEAT 336 337 1.
REPEAT 339 340 2.
REPEAT 348 349 3.
REPEAT 350 351 4.
REPEAT 352 353 5.
REPEAT 354 355 6.
REPEAT 356 357 7.
REPEAT 358 359 8.
REPEAT 360 361 9.
REPEAT 362 363 10.
REPEAT 364 365 11.
REPEAT 367 368 12.
REGION 163 223 Required and sufficient for interaction
with smu-1.
{ECO:0000269|PubMed:27150041}.
REGION 336 368 12 X 2 AA repeats of R-[DS].
COILED 66 94 {ECO:0000255}.
COILED 371 427 {ECO:0000255}.
COMPBIAS 168 176 Poly-Asp. {ECO:0000255}.
COMPBIAS 185 190 Poly-Ser. {ECO:0000255}.
COMPBIAS 291 295 Poly-Lys. {ECO:0000255}.
COMPBIAS 320 368 Asp-rich. {ECO:0000255|PROSITE-
ProRule:PRU00004}.
COMPBIAS 333 407 Arg-rich. {ECO:0000255|PROSITE-
ProRule:PRU00002}.
COMPBIAS 380 424 Glu-rich. {ECO:0000255|PROSITE-
ProRule:PRU00007}.
MUTAGEN 212 212 V->R: Disrupts interaction with smu-1.
{ECO:0000269|PubMed:27150041}.
MUTAGEN 220 220 F->R: Disrupts interaction with smu-1.
{ECO:0000269|PubMed:27150041}.
HELIX 195 203 {ECO:0000244|PDB:5EN7}.
HELIX 210 220 {ECO:0000244|PDB:5EN7}.
SEQUENCE 547 AA; 62197 MW; DEE969CCA07EDBDA CRC64;
MADNPTNLRN ADFRKLLTSA RSDRPAVSAF AKPADPKTGD DKPASFKHKH LKPAKFKKPQ
AAAHGKAKKE KTEADEDEAA LKNILKNYRD RAAERRKQGD EKEDPSKLTA AYRAVPGDAR
SAQDQADLRK QAILESKYLG GDLEHTHLVK GLDYSLLNKV RSEIDKSDDD DDDDIDTAFD
EKVTSSSSSS KPSEASLLAQ ELAQSHSENR MVRSLHRVLF KNEVPLHNQL FAKGRMAYVV
ELEDEETDIP TTLLRSLHDL PRAESAQSIQ ANNLIILKLS HVLSHLRAEP KKKKKEEFRV
QLGSRDAPGA AAAAPGAKGD SIYDDLDDYV PSRKSRDSRD AGRRGSRRDR SRDRSRDRDR
DRDRDNRDRY FEKSANSRRE EEQNRREQQR ERERAEQERR REREKEREQE KAKEREKKRK
ELEESSGYDE CYPGGLVEMG GAWDSDEEAD YSKMDAGPKK NQAVNRWDFD TEEEYASYME
GREALPKAAY QYGVKNGEGG RKNKKQSAVS DAKRLDRELN EINKIMDKRK AGGDGAGGGG
DYKKPKY


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