SA145_SCHPO
ID SA145_SCHPO Reviewed; 601 AA.
AC Q9UUI3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Pre-mRNA-splicing factor sap145;
DE AltName: Full=Spliceosome-associated protein 145;
GN Name=sap145; ORFNames=SPAC22F8.10c;
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 IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in pre-mRNA splicing. May be involved in endoplasmic
CC reticulum-associated protein degradation (ERAD) and required for growth
CC at low and high temperatures (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB52720.1; -; Genomic_DNA.
DR PIR; T38200; T38200.
DR RefSeq; NP_594733.1; NM_001020161.2.
DR AlphaFoldDB; Q9UUI3; -.
DR SMR; Q9UUI3; -.
DR BioGRID; 278106; 33.
DR IntAct; Q9UUI3; 2.
DR STRING; 4896.SPAC22F8.10c.1; -.
DR iPTMnet; Q9UUI3; -.
DR MaxQB; Q9UUI3; -.
DR PaxDb; Q9UUI3; -.
DR PRIDE; Q9UUI3; -.
DR EnsemblFungi; SPAC22F8.10c.1; SPAC22F8.10c.1:pep; SPAC22F8.10c.
DR GeneID; 2541609; -.
DR KEGG; spo:SPAC22F8.10c; -.
DR PomBase; SPAC22F8.10c; sap145.
DR VEuPathDB; FungiDB:SPAC22F8.10c; -.
DR eggNOG; KOG2330; Eukaryota.
DR HOGENOM; CLU_014435_1_1_1; -.
DR InParanoid; Q9UUI3; -.
DR OMA; RYWGEIG; -.
DR PhylomeDB; Q9UUI3; -.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:Q9UUI3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:PomBase.
DR InterPro; IPR007180; DUF382.
DR InterPro; IPR006568; PSP_pro-rich.
DR Pfam; PF04037; DUF382; 1.
DR Pfam; PF04046; PSP; 1.
DR SMART; SM00581; PSP; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..601
FT /note="Pre-mRNA-splicing factor sap145"
FT /id="PRO_0000343537"
FT REGION 35..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..90
FT /evidence="ECO:0000255"
FT COMPBIAS 52..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..454
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 601 AA; 69185 MW; 3A0B235301B594A4 CRC64;
MYLLTRPKHC CLDFLLMAEI QTAQNPLKEL EKILERNNKQ KNKKSRNQVR REKKKLLREK
TNSGAKLAEK NSDDKDQLTE NNDNLYNDKK SNGNFYDTNK TDSVDGMVYT TIVDSVELDP
NDPLIEQFKD VFNRFKADGQ EKDFEDTDKG QIMYSDDEIL SEGEEDALQK QQEEKLSKKK
LRKLKRMTVA QLKMLSEKAD VVEWWDVSSL DPLFLTHLKA YPNTVPVPRH WNQKRDYLSG
QRGIERQLFE LPSYIRATGI VQMRNAVHEN EADMPLRQKM RERVQPKMGK LDIDYQKLHD
AFFRYQTKPV LTGFGECYFE GKELEADVKE KRPGDISEEL REALGIAPGA PPPWLFAMQR
YGPPPSYPDL KIPGVNCPIP TGAQWGFHPG GWGKPPVDQF NRPLYGDVFG NVKPRIHAGT
GSPVSTQHWG ELEEFEEEES SEEEESEDVE YPTEEITERE TIEEYQSASE PRSQREDLHA
EPLTYFNQSN VEVDNVELRK NTQPSSDAAN RDLYQVLPEK STNISGFMGP QHQYDIPTAE
DTLPQKRNAH SMLSSTNKGD VALNQSSNWQ DELSELVSEQ AMKVGAAKRQ KTQSKRDKFR
L
