ICLN_SCHPO
ID ICLN_SCHPO Reviewed; 217 AA.
AC O13777; Q9P6N0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Splicing factor saf5;
GN Name=saf5 {ECO:0000312|PomBase:SPAC1610.01};
GN Synonyms=icln {ECO:0000303|PubMed:24298023},
GN lot5 {ECO:0000312|PomBase:SPAC1610.01};
GN ORFNames=SPAC1610.01 {ECO:0000312|PomBase:SPAC1610.01},
GN SPAC17A5.17 {ECO:0000312|PomBase:SPAC1610.01};
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 FUNCTION, INTERACTION WITH SMD1 AND SMD3, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24298023; DOI=10.1128/mcb.01407-13;
RA Barbarossa A., Antoine E., Neel H., Gostan T., Soret J., Bordonne R.;
RT "Characterization and in vivo functional analysis of the
RT Schizosaccharomyces pombe ICLN gene.";
RL Mol. Cell. Biol. 34:595-605(2014).
CC -!- FUNCTION: Chaperone that regulates the assembly of spliceosomal U1, U2,
CC U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building
CC blocks of the spliceosome, and thereby plays an important role in the
CC splicing of cellular pre-mRNAs (PubMed:24298023). Most spliceosomal
CC snRNPs contain a common set of Sm proteins smb1, smd1, smd2, smd3,
CC sme1, smf1 and smg1 that assemble in a heptameric protein ring on the
CC Sm site of the small nuclear RNA to form the core snRNP (By
CC similarity). In the cytosol, the Sm proteins smd1, smd2, sme1, smf1 and
CC smg1 are trapped in an inactive 6S pICln-Sm complex by the chaperone
CC saf5 that controls the assembly of the core snRNP (By similarity).
CC Dissociation by the SMN complex of saf5 from the trapped Sm proteins
CC and their transfer to an SMN-Sm complex triggers the assembly of core
CC snRNPs and their transport to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:P54105, ECO:0000269|PubMed:24298023}.
CC -!- SUBUNIT: Interacts with smd1; the interaction is direct
CC (PubMed:24298023). Interacts with smd3; the interaction is direct
CC (PubMed:24298023). {ECO:0000269|PubMed:24298023}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24298023}. Cytoplasm
CC {ECO:0000269|PubMed:24298023}. Note=Localizes to the nucleus
CC predominantly. {ECO:0000269|PubMed:24298023}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular levels of Sm-class snRNPs and
CC leads to abnormal splicing of a subset of introns (PubMed:24298023).
CC Decreases vegetative cell population growth and leads to heat
CC sensitivity (PubMed:24298023). {ECO:0000269|PubMed:24298023}.
CC -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11517.1; -; Genomic_DNA.
DR PIR; T37832; T37832.
DR RefSeq; NP_593485.1; NM_001018918.2.
DR AlphaFoldDB; O13777; -.
DR SMR; O13777; -.
DR BioGRID; 279254; 78.
DR STRING; 4896.SPAC1610.01.1; -.
DR TCDB; 1.A.47.2.1; the nucleotide-sensitive anion-selective channel, icln (icln) family.
DR iPTMnet; O13777; -.
DR MaxQB; O13777; -.
DR PaxDb; O13777; -.
DR EnsemblFungi; SPAC1610.01.1; SPAC1610.01.1:pep; SPAC1610.01.
DR GeneID; 2542806; -.
DR KEGG; spo:SPAC1610.01; -.
DR PomBase; SPAC1610.01; -.
DR VEuPathDB; FungiDB:SPAC1610.01; -.
DR eggNOG; ENOG502S43V; Eukaryota.
DR HOGENOM; CLU_1272916_0_0_1; -.
DR InParanoid; O13777; -.
DR OMA; NHQWITA; -.
DR PRO; PR:O13777; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IPI:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039924; ICln/Lot5/Saf5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR21399; PTHR21399; 1.
DR Pfam; PF03517; Voldacs; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..217
FT /note="Splicing factor saf5"
FT /id="PRO_0000116797"
SQ SEQUENCE 217 AA; 24947 MW; 3B461CC18FE26CFB CRC64;
MITKIDSLPK DLIRKVENGE KLLPNQEIVY FEEKTVPYKI RSDEESFPLG KLITLLVTSQ
SFILFDEEQN SGWKIPYETI TLHAKQSKDK PYVYVQLEGE AIRPLLDHIL KFERSSGTLH
EAPSTEDENE FTDDFLELTL YVTDVDSCYQ ALCTCQSLHP DTFSSDNDVE NASMGNPMSL
FFDPNHQWVT AENVDTSACD NRFDSPESPV LKWHRTE
