GEMI8_SCHPO
ID GEMI8_SCHPO Reviewed; 166 AA.
AC Q9USY8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Uncharacterized protein C16H5.15;
GN Name=gem8 {ECO:0000303|PubMed:33754639};
GN ORFNames=SPBC16H5.15 {ECO:0000312|PomBase:SPBC16H5.15};
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE CORE SMN COMPLEX, INTERACTION WITH SMN1 AND
RP GEM7, AND DISRUPTION PHENOTYPE.
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 (Probable). Most spliceosomal snRNPs contain a common set of Sm
CC proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP (Sm core) (By similarity). In the
CC cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are
CC trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
CC controls the assembly of the core snRNP (By similarity). To assemble
CC core snRNPs, the SMN complex accepts the trapped 5Sm proteins from
CC CLNS1A forming an intermediate (By similarity). Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP (By
CC similarity). {ECO:0000250|UniProtKB:Q9NWZ8,
CC ECO:0000305|PubMed:33754639}.
CC -!- SUBUNIT: Part of the core SMN complex at least composed of smn1,
CC yip11/gem2, gem6, gem7 and gem8 (PubMed:33754639). Interacts with smn1;
CC the interaction is direct (PubMed:33754639). Interacts with gem7; the
CC interaction is direct (PubMed:33754639). {ECO:0000269|PubMed:33754639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Inviable cell population (PubMed:33754639).
CC Degron-mediated knockdown leads to decreased cellular levels of Sm-
CC class snRNPs and defects in spliceosome activity (PubMed:33754639).
CC {ECO:0000269|PubMed:33754639}.
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DR EMBL; CU329671; CAB60139.1; -; Genomic_DNA.
DR PIR; T39620; T39620.
DR RefSeq; NP_595942.1; NM_001021850.2.
DR AlphaFoldDB; Q9USY8; -.
DR SASBDB; Q9USY8; -.
DR SMR; Q9USY8; -.
DR BioGRID; 276431; 2.
DR MaxQB; Q9USY8; -.
DR PaxDb; Q9USY8; -.
DR EnsemblFungi; SPBC16H5.15.1; SPBC16H5.15.1:pep; SPBC16H5.15.
DR GeneID; 2539885; -.
DR KEGG; spo:SPBC16H5.15; -.
DR PomBase; SPBC16H5.15; -.
DR VEuPathDB; FungiDB:SPBC16H5.15; -.
DR eggNOG; ENOG502SGGI; Eukaryota.
DR HOGENOM; CLU_1603692_0_0_1; -.
DR InParanoid; Q9USY8; -.
DR OMA; KFHDEHF; -.
DR PRO; PR:Q9USY8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032797; C:SMN complex; IDA:PomBase.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IMP:PomBase.
DR InterPro; IPR024526; DUF3807.
DR PANTHER; PTHR40642; PTHR40642; 1.
DR Pfam; PF12720; DUF3807; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..166
FT /note="Uncharacterized protein C16H5.15"
FT /id="PRO_0000353136"
FT REGION 1..58
FT /note="May interact with smn1"
FT /evidence="ECO:0000269|PubMed:33754639"
SQ SEQUENCE 166 AA; 19685 MW; D8984D1D20EAB8CE CRC64;
MSSEITEGDL QKFHDEHFNA KAVNLWNVAF AQNDRGGNSE SANVEYTQSV ERYPDGTIRT
LTDEQILWFR ESEKRELMWK KEKEQLLKEK ELRQKALDKE RMVSSKPETN PKTPISLKEL
KDIEIYQNQF HYSAYEILEE EKILDNIFRK FTALPIKYWP ATPIRG
