SMU1_MOUSE
ID SMU1_MOUSE Reviewed; 513 AA.
AC Q3UKJ7; Q6PFR6; Q8BMY4; Q9D1I8; Q9JJ70;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR;
RA Minami N., Miyamoto M., Aizawa A., Imai H.;
RT "cDNA from mouse 2-cell embryo.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=15031102; DOI=10.1016/j.ydbio.2003.11.024;
RA Powles N., Babbs C., Ficker M., Schimmang T., Maconochie M.;
RT "Identification and analysis of genes from the mouse otic vesicle and their
RT association with developmental subprocesses through in situ
RT hybridization.";
RL Dev. Biol. 268:24-38(2004).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome (By similarity). Regulates alternative splicing of the
CC HSPG2 pre-mRNA (By similarity). Required for normal accumulation of IK
CC (By similarity). Required for normal mitotic spindle assembly and
CC normal progress through mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q2TAY7, ECO:0000250|UniProtKB:Q76B40}.
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:0000250|UniProtKB:Q76B40}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q76B40}. Note=Colocalizes with SRSF1 in nuclear
CC speckles. {ECO:0000250|UniProtKB:Q76B40}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UKJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UKJ7-2; Sequence=VSP_018593;
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc expressed in otic vesicle.
CC {ECO:0000269|PubMed:15031102}.
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}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=BAC25322.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB044414; BAA96656.1; -; mRNA.
DR EMBL; AK003493; BAB22820.1; -; mRNA.
DR EMBL; AK011140; BAC25322.1; ALT_FRAME; mRNA.
DR EMBL; AK145982; BAE26804.1; -; mRNA.
DR EMBL; AK159635; BAE35249.1; -; mRNA.
DR EMBL; AK168813; BAE40640.1; -; mRNA.
DR EMBL; BC057446; AAH57446.1; -; mRNA.
DR CCDS; CCDS18050.1; -. [Q3UKJ7-1]
DR RefSeq; NP_067510.3; NM_021535.4. [Q3UKJ7-1]
DR AlphaFoldDB; Q3UKJ7; -.
DR SMR; Q3UKJ7; -.
DR BioGRID; 216611; 31.
DR IntAct; Q3UKJ7; 4.
DR MINT; Q3UKJ7; -.
DR STRING; 10090.ENSMUSP00000030117; -.
DR iPTMnet; Q3UKJ7; -.
DR PhosphoSitePlus; Q3UKJ7; -.
DR EPD; Q3UKJ7; -.
DR MaxQB; Q3UKJ7; -.
DR PaxDb; Q3UKJ7; -.
DR PeptideAtlas; Q3UKJ7; -.
DR PRIDE; Q3UKJ7; -.
DR ProteomicsDB; 261584; -. [Q3UKJ7-1]
DR ProteomicsDB; 261585; -. [Q3UKJ7-2]
DR Antibodypedia; 10816; 110 antibodies from 24 providers.
DR DNASU; 74255; -.
DR Ensembl; ENSMUST00000030117; ENSMUSP00000030117; ENSMUSG00000028409. [Q3UKJ7-1]
DR GeneID; 74255; -.
DR KEGG; mmu:74255; -.
DR UCSC; uc008shu.2; mouse. [Q3UKJ7-1]
DR CTD; 55234; -.
DR MGI; MGI:1915546; Smu1.
DR VEuPathDB; HostDB:ENSMUSG00000028409; -.
DR eggNOG; KOG0275; Eukaryota.
DR GeneTree; ENSGT00940000155007; -.
DR HOGENOM; CLU_000288_57_38_1; -.
DR InParanoid; Q3UKJ7; -.
DR OMA; FIEVWNY; -.
DR OrthoDB; 1467963at2759; -.
DR PhylomeDB; Q3UKJ7; -.
DR TreeFam; TF313969; -.
DR BioGRID-ORCS; 74255; 21 hits in 62 CRISPR screens.
DR ChiTaRS; Smu1; mouse.
DR PRO; PR:Q3UKJ7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3UKJ7; protein.
DR Bgee; ENSMUSG00000028409; Expressed in spermatocyte and 267 other tissues.
DR Genevisible; Q3UKJ7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Spliceosome; Ubl conjugation; WD repeat.
FT CHAIN 1..513
FT /note="WD40 repeat-containing protein SMU1"
FT /id="PRO_0000424521"
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_0000237591"
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 VAR_SEQ 333..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018593"
FT CONFLICT 49
FT /note="A -> V (in Ref. 2; BAE26804)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="R -> L (in Ref. 2; BAB22820)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="P -> L (in Ref. 1; BAA96656)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="L -> F (in Ref. 1; BAA96656)"
FT /evidence="ECO:0000305"
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
