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SMU1_CRIGR
ID   SMU1_CRIGR              Reviewed;         513 AA.
AC   Q76B40;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=WD40 repeat-containing protein SMU1;
DE   AltName: Full=Smu-1 suppressor of mec-8 and unc-52 protein homolog;
DE   Contains:
DE     RecName: Full=WD40 repeat-containing protein SMU1, N-terminally processed;
GN   Name=SMU1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-489.
RX   PubMed=15878348; DOI=10.1016/j.yexcr.2005.02.017;
RA   Sugaya K., Hongo E., Tsuji H.;
RT   "A temperature-sensitive mutation in the WD repeat-containing protein Smu1
RT   is related to maintenance of chromosome integrity.";
RL   Exp. Cell Res. 306:242-251(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=17105761; DOI=10.1242/jcs.03288;
RA   Sugaya K., Hongo E., Ishihara Y., Tsuji H.;
RT   "The conserved role of Smu1 in splicing is characterized in its mammalian
RT   temperature-sensitive mutant.";
RL   J. Cell Sci. 119:4944-4951(2006).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21519198; DOI=10.4161/rna.8.3.14656;
RA   Sugaya K., Ishihara Y., Sugaya K.;
RT   "Enlargement of speckles of SF2/ASF due to loss of function of Smu1 is
RT   characterized in the mammalian temperature-sensitive mutant.";
RL   RNA Biol. 8:488-495(2011).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC       spliceosome (Probable). Regulates alternative splicing of the HSPG2
CC       pre-mRNA (PubMed:17105761). Required for normal accumulation of IK (By
CC       similarity). Required for normal mitotic spindle assembly and normal
CC       progress through mitosis (PubMed:15878348).
CC       {ECO:0000250|UniProtKB:Q2TAY7, ECO:0000269|PubMed:15878348,
CC       ECO:0000269|PubMed:17105761, ECO:0000305|PubMed:21519198}.
CC   -!- SUBUNIT: Component of the spliceosome B complex. Interacts with IK.
CC       {ECO:0000250|UniProtKB:Q2TAY7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99M63}. Nucleus
CC       {ECO:0000269|PubMed:21519198}. Nucleus speckle
CC       {ECO:0000269|PubMed:21519198}. Note=Colocalizes with SRSF1 in nuclear
CC       speckles. {ECO:0000269|PubMed:21519198}.
CC   -!- DOMAIN: The WD repeats assemble into a seven-bladed WD propeller.
CC       {ECO:0000250|UniProtKB:G5EEG7}.
CC   -!- SIMILARITY: Belongs to the WD repeat SMU1 family. {ECO:0000305}.
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DR   EMBL; AB111945; BAD04854.1; -; mRNA.
DR   RefSeq; NP_001231781.1; NM_001244852.1.
DR   AlphaFoldDB; Q76B40; -.
DR   SMR; Q76B40; -.
DR   STRING; 10029.NP_001231781.1; -.
DR   GeneID; 100736555; -.
DR   KEGG; cge:100736555; -.
DR   CTD; 55234; -.
DR   eggNOG; KOG0275; Eukaryota.
DR   OrthoDB; 1467963at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 3.
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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR22848; PTHR22848; 1.
DR   Pfam; PF00400; WD40; 5.
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; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW   Nucleus; Repeat; Spliceosome; Ubl conjugation; WD repeat.
FT   CHAIN           1..513
FT                   /note="WD40 repeat-containing protein SMU1"
FT                   /id="PRO_0000424519"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TAY7"
FT   CHAIN           2..513
FT                   /note="WD40 repeat-containing protein SMU1, N-terminally
FT                   processed"
FT                   /id="PRO_0000237589"
FT   DOMAIN          6..38
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          40..92
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REPEAT          212..253
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          262..303
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          305..346
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          347..386
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          395..436
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          440..479
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          482..513
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   REGION          2..315
FT                   /note="Required for interaction with IK"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TAY7"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TAY7"
FT   MOD_RES         2
FT                   /note="N-acetylserine; in WD40 repeat-containing protein
FT                   SMU1, N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TAY7"
FT   CROSSLNK        379
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TAY7"
FT   MUTAGEN         489
FT                   /note="G->R: Temperature-sensitive mutation in tsTM18 cell
FT                   line with chromosomal instability and cell cycle arrest at
FT                   S and G2 phases with decreased DNA synthesis at the
FT                   nonpermissive temperature of 39 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:15878348"
SQ   SEQUENCE   513 AA;  57544 MW;  CB201E939DCCA188 CRC64;
     MSIEIESSDV IRLIMQYLKE NSLHRALATL QEETTVSLNT VDSIESFVAD INSGHWDTVL
     QAIQSLKLPD KTLIDLYEQV VLELIELREL GAARSLLRQT DPMIMLKQTQ PERYIHLENL
     LARSYFDPRE AYPDGSSKEK RRAAIAQALA GEVSVVPPSR LMALLGQALK WQQHQGLLPP
     GMTIDLFRGK AAVKDVEEEK FPTQLSRHIK FGQKSHVECA RFSPDGQYLV TGSVDGFIEV
     WNFTTGKIRK DLKYQAQDNF MMMDDAVLCM CFSRDTEMLA TGAQDGKIKV WKIQSGQCLR
     RFERAHSKGV TCLSFSKDSS QILSASFDQT IRIHGLKSGK TLKEFRGHSS FVNEATFTQD
     GHYIISASSD GTVKIWNMKT TECSNTFKSL GSTAGTDITV NSVILLPKNP EHFVVCNRSN
     TVVIMNMQGQ IVRSFSSGKR EGGDFVCCAL SPRGEWIYCV GEDFVLYCFS TVTGKLERTL
     TVHEKDVIGI AHHPHQNLIA TYSEDGLLKL WKP
 
 
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