SMU2_CAEEL
ID SMU2_CAEEL Reviewed; 547 AA.
AC Q9N4U5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Smu-2 suppressor of mec-8 and unc-52 protein {ECO:0000305};
DE AltName: Full=RED homolog {ECO:0000303|PubMed:27150041};
DE AltName: Full=Suppressor of Mec and Unc defects 2 {ECO:0000305};
GN Name=smu-2 {ECO:0000312|WormBase:Y49F6B.4};
GN ORFNames=Y49F6B.4 {ECO:0000312|WormBase:Y49F6B.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CCD64715.1, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD64715.1,
RC ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMU-1, DISRUPTION
RP PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15254247; DOI=10.1128/mcb.24.15.6811-6823.2004;
RA Spartz A.K., Herman R.K., Shaw J.E.;
RT "SMU-2 and SMU-1, Caenorhabditis elegans homologs of mammalian spliceosome-
RT associated proteins RED and fSAP57, work together to affect splice site
RT choice.";
RL Mol. Cell. Biol. 24:6811-6823(2004).
RN [3] {ECO:0007744|PDB:5EN6, ECO:0007744|PDB:5EN7}
RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 163-223 IN COMPLEX WITH SMU-1,
RP INTERACTION WITH SMU-1, DOMAIN, AND MUTAGENESIS OF VAL-212 AND PHE-220.
RX PubMed=27150041; DOI=10.1016/j.str.2016.03.016;
RA Ulrich A.K., Schulz J.F., Kamprad A., Schuetze T., Wahl M.C.;
RT "Structural Basis for the Functional Coupling of the Alternative Splicing
RT Factors Smu1 and RED.";
RL Structure 24:762-773(2016).
CC -!- FUNCTION: Auxiliary spliceosomal protein that regulates selection of
CC alternative splice sites in a small set of target pre-mRNA species
CC (Probable). Selectively regulates alternative splicing of unc-52 exon
CC 17. Thus, smu-2 mutants selectively suppress the effects of unc-52
CC nonsense mutations in exon 17 by promoting the accumulation of unc-52
CC isoforms that lack exon 17. In contrast, smu-2 mutants do not suppress
CC the effects of an unc-52 mutation that affects the 5' splice site of
CC exon 16. Required for normal accumulation of smu-1 (PubMed:15254247).
CC {ECO:0000269|PubMed:15254247, ECO:0000305}.
CC -!- SUBUNIT: Probable component of the spliceosome (By similarity).
CC Heterotetramer with smu-1 (PubMed:27150041). The smu-1 homodimer
CC interacts (via the N-terminal region including the LisH and CTLH
CC domains) with smu-2, giving rise to a heterotetramer (PubMed:15254247,
CC PubMed:27150041). {ECO:0000250|UniProtKB:Q13123,
CC ECO:0000269|PubMed:15254247, ECO:0000269|PubMed:27150041}.
CC -!- INTERACTION:
CC Q9N4U5; G5EEG7: smu-1; NbExp=6; IntAct=EBI-2415311, EBI-2411547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15254247}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15254247}.
CC -!- DEVELOPMENTAL STAGE: Detected at all stages of development, during
CC early embryogenesis and in oocytes, in larvae and adults.
CC {ECO:0000269|PubMed:15254247}.
CC -!- DOMAIN: Intrinsically disordered protein (Probable).
CC {ECO:0000305|PubMed:27150041}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown gives rise to no visible
CC phenotype in wild-type, but suppresses the effects of unc-52 mutations.
CC {ECO:0000269|PubMed:15254247}.
CC -!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
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DR EMBL; BX284602; CCD64715.1; -; Genomic_DNA.
DR RefSeq; NP_494559.1; NM_062158.4.
DR PDB; 5EN6; X-ray; 3.10 A; C/D=163-223.
DR PDB; 5EN7; X-ray; 2.94 A; B/D/F/H=163-223.
DR PDBsum; 5EN6; -.
DR PDBsum; 5EN7; -.
DR AlphaFoldDB; Q9N4U5; -.
DR SMR; Q9N4U5; -.
DR DIP; DIP-55152N; -.
DR IntAct; Q9N4U5; 3.
DR STRING; 6239.Y49F6B.4; -.
DR EPD; Q9N4U5; -.
DR PaxDb; Q9N4U5; -.
DR PeptideAtlas; Q9N4U5; -.
DR EnsemblMetazoa; Y49F6B.4.1; Y49F6B.4.1; WBGene00004896.
DR GeneID; 173693; -.
DR KEGG; cel:CELE_Y49F6B.4; -.
DR UCSC; Y49F6B.4; c. elegans.
DR CTD; 173693; -.
DR WormBase; Y49F6B.4; CE25338; WBGene00004896; smu-2.
DR eggNOG; KOG2498; Eukaryota.
DR GeneTree; ENSGT00940000165879; -.
DR HOGENOM; CLU_026814_2_0_1; -.
DR InParanoid; Q9N4U5; -.
DR OMA; EPEYKSA; -.
DR OrthoDB; 500537at2759; -.
DR PhylomeDB; Q9N4U5; -.
DR PRO; PR:Q9N4U5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004896; Expressed in embryo and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0040011; P:locomotion; IGI:WormBase.
DR GO; GO:0007638; P:mechanosensory behavior; IGI:WormBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048644; P:muscle organ morphogenesis; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0048666; P:neuron development; IGI:WormBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:WormBase.
DR DisProt; DP01313; -.
DR InterPro; IPR039896; Red-like.
DR InterPro; IPR012492; RED_C.
DR InterPro; IPR012916; RED_N.
DR PANTHER; PTHR12765; PTHR12765; 1.
DR Pfam; PF07807; RED_C; 1.
DR Pfam; PF07808; RED_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..547
FT /note="Smu-2 suppressor of mec-8 and unc-52 protein"
FT /id="PRO_0000441749"
FT REPEAT 336..337
FT /note="1"
FT REPEAT 339..340
FT /note="2"
FT REPEAT 348..349
FT /note="3"
FT REPEAT 350..351
FT /note="4"
FT REPEAT 352..353
FT /note="5"
FT REPEAT 354..355
FT /note="6"
FT REPEAT 356..357
FT /note="7"
FT REPEAT 358..359
FT /note="8"
FT REPEAT 360..361
FT /note="9"
FT REPEAT 362..363
FT /note="10"
FT REPEAT 364..365
FT /note="11"
FT REPEAT 367..368
FT /note="12"
FT REGION 18..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..223
FT /note="Required and sufficient for interaction with smu-1"
FT /evidence="ECO:0000269|PubMed:27150041"
FT REGION 164..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..368
FT /note="12 X 2 AA repeats of R-[DS]"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..94
FT /evidence="ECO:0000255"
FT COILED 371..427
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 212
FT /note="V->R: Disrupts interaction with smu-1."
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 220
FT /note="F->R: Disrupts interaction with smu-1."
FT /evidence="ECO:0000269|PubMed:27150041"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:5EN7"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:5EN7"
SQ 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
