SMN_SCHPO
ID SMN_SCHPO Reviewed; 152 AA.
AC Q09808;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=SMN complex subunit smn1 {ECO:0000312|PomBase:SPAC2G11.08c};
DE AltName: Full=Gemin-1 {ECO:0000305};
DE AltName: Full=Survival motor neuron protein {ECO:0000305};
GN Name=smn1 {ECO:0000303|PubMed:10749974};
GN Synonyms=yab8 {ECO:0000303|PubMed:10749974};
GN ORFNames=SPAC2G11.08c {ECO:0000312|PomBase:SPAC2G11.08c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION, FUNCTION, INTERACTION WITH YIP1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TYR-136 AND GLY-143.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10749974; DOI=10.1093/hmg/9.5.675;
RA Owen N., Doe C.L., Mellor J., Davies K.E.;
RT "Characterization of the Schizosaccharomyces pombe orthologue of the human
RT survival motor neuron (SMN) protein.";
RL Hum. Mol. Genet. 9:675-684(2000).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10816558; DOI=10.1074/jbc.m001441200;
RA Paushkin S., Charroux B., Abel L., Perkinson R.A., Pellizzoni L.,
RA Dreyfuss G.;
RT "The survival motor neuron protein of Schizosaccharomyces pombe.
RT Conservation of survival motor neuron interaction domains in divergent
RT organisms.";
RL J. Biol. Chem. 275:23841-23846(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20400941; DOI=10.1038/emboj.2010.70;
RA Campion Y., Neel H., Gostan T., Soret J., Bordonne R.;
RT "Specific splicing defects in S. pombe carrying a degron allele of the
RT Survival of Motor Neuron gene.";
RL EMBO J. 29:1817-1829(2010).
RN [5] {ECO:0007744|PDB:4RG5}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 119-150, SUBUNIT, AND INTERACTION
RP WITH YIP11.
RX PubMed=26092730; DOI=10.1074/jbc.m115.667279;
RA Gupta K., Martin R., Sharp R., Sarachan K.L., Ninan N.S., Van Duyne G.D.;
RT "Oligomeric Properties of Survival Motor Neuron.Gemin2 Complexes.";
RL J. Biol. Chem. 290:20185-20199(2015).
RN [6] {ECO:0007744|PDB:7BB3}
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 10-35 AND 120-147, FUNCTION,
RP SUBUNIT, IDENTIFICATION IN THE CORE SMN COMPLEX, INTERACTION WITH YIP11 AND
RP GEM8, AND MUTAGENESIS OF SER-130 AND ALA-134.
RX PubMed=33754639; DOI=10.1093/nar/gkab158;
RA Veepaschit J., Viswanathan A., Bordonne R., Grimm C., Fischer U.;
RT "Identification and structural analysis of the Schizosaccharomyces pombe
RT SMN complex.";
RL Nucleic Acids Res. 49:gkab158-gkab158(2021).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (PubMed:20400941, PubMed:33754639, PubMed:10749974). Most
CC spliceosomal snRNPs contain a common set of Sm proteins smb1, smd1,
CC smd2, smd3, sme1, smf1 and smg1 that assemble in a heptameric protein
CC ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm
CC core) (By similarity). In the cytosol, the Sm proteins smd1, smd2,
CC sme1, smf1 and smg1 (5Sm) are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone saf5 that controls the assembly of the core
CC snRNP (By similarity). To assemble core snRNPs, the SMN complex accepts
CC the trapped 5Sm proteins from saf5 forming an intermediate (By
CC similarity). Binding of snRNA inside 5Sm triggers eviction of the SMN
CC complex, thereby allowing binding of smd3 and smb1 to complete assembly
CC of the core snRNP (By similarity). Within the SMN complex, smn1 acts as
CC a structural backbone and together with yip11/gem2 it gathers the Sm
CC complex subunits (PubMed:33754639). {ECO:0000250|UniProtKB:Q16637,
CC ECO:0000269|PubMed:10749974, ECO:0000269|PubMed:20400941,
CC ECO:0000269|PubMed:33754639}.
CC -!- SUBUNIT: Homooligomer; may form homodimers and homotetramers
CC (PubMed:26092730, PubMed:33754639). Part of the core SMN complex at
CC least composed of smn1, yip11/gem2, gem6, gem7 and gem8
CC (PubMed:33754639). Part of the SMN-Sm complex (PubMed:10816558).
CC Interacts with yip11/gem2; the interaction is direct (PubMed:26092730,
CC PubMed:10749974, PubMed:33754639). Interacts with gem8; the interaction
CC is direct (PubMed:33754639). Interacts with proteins of the Sm complex,
CC including smn1, smb1, smd1, smd2 and smd3 (PubMed:10816558).
CC {ECO:0000269|PubMed:10749974, ECO:0000269|PubMed:10816558,
CC ECO:0000269|PubMed:26092730, ECO:0000269|PubMed:33754639}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749974,
CC ECO:0000269|PubMed:10816558}.
CC -!- DISRUPTION PHENOTYPE: Degron-mediated knockdown leads to decreased
CC cellular levels of Sm-class snRNPs, abnormal splicing of a subset of
CC introns, and cell population growth defects.
CC {ECO:0000269|PubMed:20400941}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91173.1; -; Genomic_DNA.
DR PIR; T38574; S62463.
DR RefSeq; NP_593088.1; NM_001018486.2.
DR PDB; 4RG5; X-ray; 1.70 A; A/B=119-150.
DR PDB; 7BB3; X-ray; 2.16 A; A/B=2-152.
DR PDBsum; 4RG5; -.
DR PDBsum; 7BB3; -.
DR AlphaFoldDB; Q09808; -.
DR SASBDB; Q09808; -.
DR SMR; Q09808; -.
DR BioGRID; 278486; 5.
DR STRING; 4896.SPAC2G11.08c.1; -.
DR iPTMnet; Q09808; -.
DR MaxQB; Q09808; -.
DR PaxDb; Q09808; -.
DR PRIDE; Q09808; -.
DR EnsemblFungi; SPAC2G11.08c.1; SPAC2G11.08c.1:pep; SPAC2G11.08c.
DR GeneID; 2542002; -.
DR KEGG; spo:SPAC2G11.08c; -.
DR PomBase; SPAC2G11.08c; smn1.
DR VEuPathDB; FungiDB:SPAC2G11.08c; -.
DR eggNOG; KOG4327; Eukaryota.
DR HOGENOM; CLU_093937_1_0_1; -.
DR InParanoid; Q09808; -.
DR OMA; KNIMMSW; -.
DR PhylomeDB; Q09808; -.
DR PRO; PR:Q09808; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0032797; C:SMN complex; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISO:PomBase.
DR InterPro; IPR040424; Smn1.
DR PANTHER; PTHR39267; PTHR39267; 2.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..152
FT /note="SMN complex subunit smn1"
FT /id="PRO_0000218907"
FT REGION 26..51
FT /note="Interacts with yip11/gem2"
FT /evidence="ECO:0000305|PubMed:26092730"
FT REGION 88..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..152
FT /note="May interact with gem8"
FT /evidence="ECO:0000269|PubMed:33754639"
FT COMPBIAS 89..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 130
FT /note="S->D: Abolishes homooligomerization beyond homodimer
FT formation and results in abnormal SMN complex formation.
FT Decreases vegetative cell population growth."
FT /evidence="ECO:0000269|PubMed:33754639"
FT MUTAGEN 134
FT /note="A->E: Abolishes homooligomerization beyond homodimer
FT formation and results in abnormal SMN complex formation.
FT Decreases vegetative cell population growth."
FT /evidence="ECO:0000269|PubMed:33754639"
FT MUTAGEN 136
FT /note="Y->C: Localizes in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:10749974"
FT MUTAGEN 143
FT /note="G->V: Localizes in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:10749974"
FT HELIX 11..35
FT /evidence="ECO:0007829|PDB:7BB3"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4RG5"
FT HELIX 125..149
FT /evidence="ECO:0007829|PDB:4RG5"
SQ SEQUENCE 152 AA; 17385 MW; CC64455AFC2CFEE6 CRC64;
MDQSQKEVWD DSELRNAFET ALHEFKKYHS IEAKGGVSDP DSRLDGEKLI SAARTEESIS
KLEEGEQMIN QQTETTLEGD THIQQFADNK GLSDEKPETR AAETHQEFME VPPPIRGLTY
DETYKKLIMS WYYAGYYTGL AEGLAKSEQR KD
