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SMU1_ARATH
ID   SMU1_ARATH              Reviewed;         511 AA.
AC   Q8W117; Q9C9T9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 148.
DE   RecName: Full=Suppressor of mec-8 and unc-52 protein homolog 1;
DE            Short=AtSMU-1;
DE   AltName: Full=RNA splicing protein SMU1;
DE   AltName: Full=WD40 repeat-containing protein SMU1;
GN   Name=SMU1; OrderedLocusNames=At1g73720; ORFNames=F25P22.14;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SMU2, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=19734266; DOI=10.1104/pp.109.141705;
RA   Chung T., Wang D., Kim C.S., Yadegari R., Larkins B.A.;
RT   "Plant SMU-1 and SMU-2 homologues regulate pre-mRNA splicing and multiple
RT   aspects of development.";
RL   Plant Physiol. 151:1498-1512(2009).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Auxiliary spliceosomal protein involved in splicing of
CC       specific pre-mRNAs that affect multiple aspects of development.
CC       Required for proper accumulation of SMU2.
CC       {ECO:0000269|PubMed:19734266}.
CC   -!- SUBUNIT: Component of the spliceosome B complex (By similarity).
CC       Interacts with SMU2 (PubMed:19734266). {ECO:0000250|UniProtKB:Q2TAY7,
CC       ECO:0000269|PubMed:19734266}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19734266}.
CC   -!- TISSUE SPECIFICITY: Expressed in actively dividing cells, such as newly
CC       emerged leaves and root tips. Detected in embryo, female gametophyte
CC       including egg cell, central cell, synergid cells and the antipodal
CC       cells, and mature pollen. {ECO:0000269|PubMed:19734266}.
CC   -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC       {ECO:0000269|PubMed:19734266}.
CC   -!- SIMILARITY: Belongs to the WD repeat SMU1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC012679; AAG52064.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35501.1; -; Genomic_DNA.
DR   EMBL; AF462796; AAL58892.1; -; mRNA.
DR   EMBL; AY102129; AAM26696.1; -; mRNA.
DR   PIR; D96764; D96764.
DR   RefSeq; NP_177513.2; NM_106031.4.
DR   AlphaFoldDB; Q8W117; -.
DR   SMR; Q8W117; -.
DR   BioGRID; 28926; 20.
DR   IntAct; Q8W117; 3.
DR   STRING; 3702.AT1G73720.1; -.
DR   iPTMnet; Q8W117; -.
DR   PaxDb; Q8W117; -.
DR   PRIDE; Q8W117; -.
DR   ProteomicsDB; 228449; -.
DR   EnsemblPlants; AT1G73720.1; AT1G73720.1; AT1G73720.
DR   GeneID; 843707; -.
DR   Gramene; AT1G73720.1; AT1G73720.1; AT1G73720.
DR   KEGG; ath:AT1G73720; -.
DR   Araport; AT1G73720; -.
DR   TAIR; locus:2027749; AT1G73720.
DR   eggNOG; KOG0275; Eukaryota.
DR   HOGENOM; CLU_000288_57_38_1; -.
DR   InParanoid; Q8W117; -.
DR   OMA; FIEVWNY; -.
DR   OrthoDB; 1467963at2759; -.
DR   PhylomeDB; Q8W117; -.
DR   PRO; PR:Q8W117; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8W117; baseline and differential.
DR   Genevisible; Q8W117; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IMP:TAIR.
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; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Repeat; Spliceosome; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..511
FT                   /note="Suppressor of mec-8 and unc-52 protein homolog 1"
FT                   /id="PRO_0000429841"
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          211..252
FT                   /note="WD 1"
FT   REPEAT          261..300
FT                   /note="WD 2"
FT   REPEAT          303..344
FT                   /note="WD 3"
FT   REPEAT          345..384
FT                   /note="WD 4"
FT   REPEAT          393..434
FT                   /note="WD 5"
FT   REPEAT          480..511
FT                   /note="WD 6"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   511 AA;  57724 MW;  042D5AC50ED94F8A CRC64;
     MALEIEARDV IKIMLQFCKE NSLNQTFQTL QSECQVSLNT VDSVETFISD INSGRWDSVL
     PQVSQLKLPR NKLEDLYEQI VLEMIELREL DTARAILRQT QVMGVMKQEQ AERYLRMEHL
     LVRSYFDPHE AYGDSTKERK RAQIAQAVAA EVTVVPPSRL MALIGQALKW QQHQGLLPPG
     TQFDLFRGTA AMKQDVEDTH PNVLTHTIKF GKKSHAECAR FSPDGQFLAS SSVDGFIEVW
     DYISGKLKKD LQYQADESFM MHDDPVLCID FSRDSEMLAS GSQDGKIKIW RIRTGVCIRR
     FDAHSQGVTS LSFSRDGSQL LSTSFDQTAR IHGLKSGKLL KEFRGHTSYV NHAIFTSDGS
     RIITASSDCT VKVWDSKTTD CLQTFKPPPP LRGTDASVNS IHLFPKNTEH IVVCNKTSSI
     YIMTLQGQVV KSFSSGNREG GDFVAACVST KGDWIYCIGE DKKLYCFNYQ SGGLEHFMMV
     HEKDVIGITH HPHRNLLATY SEDCTMKLWK P
 
 
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