SMU1_CAEEL
ID SMU1_CAEEL Reviewed; 510 AA.
AC G5EEG7;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Smu-1 suppressor of mec-8 and unc-52 protein {ECO:0000305};
DE Short=Smu1 {ECO:0000303|PubMed:27150041};
DE AltName: Full=Suppressor of Mec and Unc defects 1 {ECO:0000305};
GN Name=smu-1 {ECO:0000303|PubMed:11438655, ECO:0000312|WormBase:CC4.3};
GN ORFNames=CC4.3 {ECO:0000312|WormBase:CC4.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAK00353.1};
RN [1] {ECO:0000312|EMBL:AAK00353.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF 255-GLN--ASP-510.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAK00353.1};
RX PubMed=11438655; DOI=10.1128/mcb.21.15.4985-4995.2001;
RA Spike C.A., Shaw J.E., Herman R.K.;
RT "Analysis of smu-1, a gene that regulates the alternative splicing of unc-
RT 52 pre-mRNA in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 21:4985-4995(2001).
RN [2] {ECO:0000312|EMBL:CAB04014.1, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB04014.1,
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMU-2.
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 [4] {ECO:0007744|PDB:5EN6, ECO:0007744|PDB:5EN7, ECO:0007744|PDB:5EN8}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 2-181 IN COMPLEX WITH SMU-2,
RP INTERACTION WITH SMU-2, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ILE-15; PHE-18
RP AND LEU-96.
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: Involved in pre-mRNA splicing as a component of the
CC spliceosome (By similarity). Selectively regulates alternative splicing
CC of unc-52 exon 17 (PubMed:11438655, PubMed:15254247). Thus, smu-1
CC mutants selectively suppress the effects of unc-52 nonsense mutations
CC in exon 17 by promoting the accumulation of unc-52 isoforms that lack
CC exon 17 and enhance the effects of unc-52 mutations that affect the
CC exon 16 splice donor site (PubMed:11438655, PubMed:15254247). In
CC contrast, smu-1 mutants do not suppress unc-52 nonsense mutations in
CC exon 18 (PubMed:11438655). {ECO:0000250|UniProtKB:Q2TAY7,
CC ECO:0000269|PubMed:11438655, ECO:0000269|PubMed:15254247}.
CC -!- SUBUNIT: Component of the spliceosome B complex (By similarity).
CC Homodimer (via LisH domain) (PubMed:27150041). The homodimer interacts
CC (via the N-terminal region including the LisH and CTLH domains) with
CC smu-2, giving rise to a heterotetramer (PubMed:15254247,
CC PubMed:27150041). {ECO:0000250|UniProtKB:Q2TAY7,
CC ECO:0000269|PubMed:15254247, ECO:0000269|PubMed:27150041}.
CC -!- INTERACTION:
CC G5EEG7; G5EEG7: smu-1; NbExp=3; IntAct=EBI-2411547, EBI-2411547;
CC G5EEG7; Q9N4U5: smu-2; NbExp=6; IntAct=EBI-2411547, EBI-2415311;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11438655,
CC ECO:0000269|PubMed:15254247}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in the intestine and germline
CC in adult hermaphrodites. {ECO:0000269|PubMed:11438655}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitous. Detected throughout embryonic and
CC larval development and in adult hermaphrodites.
CC {ECO:0000269|PubMed:11438655}.
CC -!- DOMAIN: The WD repeats assemble into a seven-bladed WD propeller.
CC {ECO:0000269|PubMed:27150041}.
CC -!- SIMILARITY: Belongs to the WD repeat SMU1 family. {ECO:0000305}.
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DR EMBL; AF330595; AAK00353.1; -; mRNA.
DR EMBL; BX284601; CAB04014.1; -; Genomic_DNA.
DR PIR; T20276; T20276.
DR RefSeq; NP_493279.1; NM_060878.5.
DR PDB; 5EN6; X-ray; 3.10 A; A/B=2-181.
DR PDB; 5EN7; X-ray; 2.94 A; A/C/E/G=2-181.
DR PDB; 5EN8; X-ray; 2.23 A; A/B=2-181.
DR PDBsum; 5EN6; -.
DR PDBsum; 5EN7; -.
DR PDBsum; 5EN8; -.
DR AlphaFoldDB; G5EEG7; -.
DR SMR; G5EEG7; -.
DR DIP; DIP-61923N; -.
DR IntAct; G5EEG7; 2.
DR STRING; 6239.CC4.3.1; -.
DR EPD; G5EEG7; -.
DR PaxDb; G5EEG7; -.
DR PeptideAtlas; G5EEG7; -.
DR EnsemblMetazoa; CC4.3.1; CC4.3.1; WBGene00004895.
DR EnsemblMetazoa; CC4.3.2; CC4.3.2; WBGene00004895.
DR GeneID; 173175; -.
DR KEGG; cel:CELE_CC4.3; -.
DR CTD; 173175; -.
DR WormBase; CC4.3; CE15742; WBGene00004895; smu-1.
DR eggNOG; KOG0275; Eukaryota.
DR GeneTree; ENSGT00940000155007; -.
DR HOGENOM; CLU_000288_57_38_1; -.
DR InParanoid; G5EEG7; -.
DR OMA; FIEVWNY; -.
DR OrthoDB; 1467963at2759; -.
DR PhylomeDB; G5EEG7; -.
DR PRO; PR:G5EEG7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004895; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
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; ISS:UniProtKB.
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 GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR045184; SMU1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22848; PTHR22848; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome; WD repeat.
FT CHAIN 1..510
FT /note="Smu-1 suppressor of mec-8 and unc-52 protein"
FT /id="PRO_0000441748"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 41..93
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 212..251
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 260..301
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 303..344
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 345..379
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 380..423
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 425..467
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 470..509
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..181
FT /note="Required and sufficient for interaction with smu-2"
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 15
FT /note="I->A: Mildly reduces homodimerization."
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 15
FT /note="I->R: Disrupts homodimerization."
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 18
FT /note="F->S,R: Disrupts homodimerization."
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 96
FT /note="L->R: Disrupts interaction with smu-2."
FT /evidence="ECO:0000269|PubMed:27150041"
FT MUTAGEN 255..510
FT /note="Missing: In mn415; enhances accumulation of an
FT alternatively spliced isoform of unc-52 that skips exon 17.
FT Selective suppressor of unc-52 missense mutations in exon
FT 17."
FT /evidence="ECO:0000269|PubMed:11438655"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:5EN8"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:5EN8"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:5EN8"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:5EN8"
SQ SEQUENCE 510 AA; 57251 MW; 8D8CBAEF0FE9E2B6 CRC64;
MSSIEIESSD VIRLIEQFLK ESNLHRTLAI LQEETNVSLN TVDSIDGFCN EITSGNWDNV
LKTVQSLKLP AKKLIDLYEH VIIELVELRE LATARLVARQ TDPMILLKQI DPDRFARLES
LINRPYFDGQ EVYGDVSKEK RRSVIAQTLS SEVHVVAPSR LLSLLGQSLK WQLHQGLLPP
GTAIDLFRGK AAQKEQIEER YPTMMARSIK FSTKSYPESA VFSPDANYLV SGSKDGFIEV
WNYMNGKLRK DLKYQAQDNL MMMDAAVRCI SFSRDSEMLA TGSIDGKIKV WKVETGDCLR
RFDRAHTKGV CAVRFSKDNS HILSGGNDHV VRVHGMKSGK CLKEMRGHSS YITDVRYSDE
GNHIISCSTD GSIRVWHGKS GECLSTFRVG SEDYPILNVI PIPKSDPPQM IVCNRSNTLY
VVNISGQVVR TMTSGKREKG DFINCILSPK GEWAYAIAED GVMYCFMVLS GTLETTLPVT
ERLPIGLAHH PHQNLIASYA EDGLLKLWTD
