SF3B1_SCHPO
ID SF3B1_SCHPO Reviewed; 1205 AA.
AC Q10178; Q9USE7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=U2 snRNP component prp10;
GN Name=prp10; Synonyms=sap155; ORFNames=SPAC27F1.09c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 78-253, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=9837997; DOI=10.1093/nar/26.24.5662;
RA Habara Y., Urushiyama S., Tani T., Ohshima Y.;
RT "The fission yeast prp10(+) gene involved in pre-mRNA splicing encodes a
RT homologue of highly conserved splicing factor, SAP155.";
RL Nucleic Acids Res. 26:5662-5669(1998).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Contacts pre-mRNA on both sides of the branch site early in
CC spliceosome assembly. {ECO:0000250, ECO:0000269|PubMed:9837997}.
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:10759889,
CC ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9837997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q10178-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q10178-2; Sequence=VSP_042618;
CC Name=E;
CC IsoId=Q10178-3; Sequence=VSP_042618, VSP_042619;
CC -!- SIMILARITY: Belongs to the SF3B1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93298.3; -; Genomic_DNA.
DR EMBL; AB027815; BAA87119.1; -; Genomic_DNA.
DR PIR; T38467; T38467.
DR RefSeq; NP_594538.2; NM_001019967.2.
DR AlphaFoldDB; Q10178; -.
DR SMR; Q10178; -.
DR BioGRID; 278116; 31.
DR IntAct; Q10178; 4.
DR STRING; 4896.SPAC27F1.09c.1; -.
DR iPTMnet; Q10178; -.
DR MaxQB; Q10178; -.
DR PaxDb; Q10178; -.
DR PRIDE; Q10178; -.
DR EnsemblFungi; SPAC27F1.09c.1; SPAC27F1.09c.1:pep; SPAC27F1.09c. [Q10178-3]
DR GeneID; 2541619; -.
DR KEGG; spo:SPAC27F1.09c; -.
DR PomBase; SPAC27F1.09c; prp10.
DR eggNOG; KOG0213; Eukaryota.
DR HOGENOM; CLU_002242_0_1_1; -.
DR InParanoid; Q10178; -.
DR OMA; LWHPARK; -.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:Q10178; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005686; C:U2 snRNP; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISO:PomBase.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015016; SF3b_su1.
DR InterPro; IPR038737; SF3b_su1-like.
DR PANTHER; PTHR12097; PTHR12097; 1.
DR Pfam; PF08920; SF3b1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..1205
FT /note="U2 snRNP component prp10"
FT /id="PRO_0000174326"
FT REPEAT 393..429
FT /note="HEAT 1"
FT REPEAT 431..473
FT /note="HEAT 2"
FT REPEAT 475..505
FT /note="HEAT 3"
FT REPEAT 506..540
FT /note="HEAT 4"
FT REPEAT 541..578
FT /note="HEAT 5"
FT REPEAT 582..619
FT /note="HEAT 6"
FT REPEAT 665..702
FT /note="HEAT 7"
FT REPEAT 745..782
FT /note="HEAT 8"
FT REPEAT 828..865
FT /note="HEAT 9"
FT REPEAT 912..949
FT /note="HEAT 10"
FT REPEAT 954..991
FT /note="HEAT 11"
FT REPEAT 993..1024
FT /note="HEAT 12"
FT REPEAT 1025..1061
FT /note="HEAT 13"
FT REPEAT 1065..1102
FT /note="HEAT 14"
FT REPEAT 1107..1142
FT /note="HEAT 15"
FT REPEAT 1143..1179
FT /note="HEAT 16"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 4..20
FT /note="Missing (in isoform B and isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_042618"
FT VAR_SEQ 55..76
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_042619"
SQ SEQUENCE 1205 AA; 137183 MW; BE72C08FEACC8ADF CRC64;
MSTGTYPYKM FKMDVTNLNK VEDVEIERLR AERELLRRQK EAAKNSSTNG SVNIEGTQDS
NDLQYNAHLF KSSNPKEEYD SAIDVRNDIS QDEDDYKRTN DVNDSYRLVR QYEAPKELLN
EYADESYDPM QERQSKKQIQ DRESDYQKQR YDRQLTPTRV DAFQPDGTQS NGRSYAEVMR
QVELEKEERR VHMELNQRRR EGTLKEVEEE ESISDKKREL ELNNTEISQK PKRSRWDQAP
PSVTQVSTTK RRSRWDKAPE NFTISEHVIE NGISEDLINK EVNVVEEKLR PPVRLLTEEE
LNELLPSEGY AILEPPPGYL ESIHPELLQK GTTLDTYHVP QEQELPLEKE LPAALPTEIP
GVGDLAFFKQ EDVKYFGKLL KVEDEAKLTI AELRERKILR LLLKVKNGTP PMRKSALRQL
TDQARDFGAA ALFNQILPLL MERTLEDQER HLLVKVIDRI LYKLDDLVRP FTHKILVVIE
PLLIDEDYYA RAEGREIISN LAKASGLAHM IATMRPDIDH VDEYVRNTTA RAFSVVASAL
GVPALLPFLK AVCRSKKSWQ ARHTGVRIIQ QIALLLGCSI LPHLKNLVDC IGHGLEDEQQ
KVRIMTALSL SALAEAATPY GIEAFDSVLK PLWSGVQRHR GKSLAAFLKA TGFIIPLMEP
EYASHFTRRI MKILLREFNS PDEEMKKIVL KVVSQCASTD GVTPEYLRTD VLPEFFHCFW
SRRMASDRRS YKQVVETTVV LAQQVGSRQI VERVVNNFKD ESEPYRKMTA ETVDKVIGSL
GVSEIDERLE ELLLDGVLFA FQEQSVEEKV ILTCFSTVVN ALGTRCKPYL PQIVSTILYR
LNNKSANVRE QAADLVSSIT IVLKACGEEA LMRKLGVVLY EYLGEEYPEV LGSILGAIKA
IVSVVGMSSM QPPIRDLLPR LTPILRNRHE KVQENTIDLV GKIADRGSEY VSAREWMRIC
FELIDMLKAH KKSIRRAAVN TFGYISKAIG PQDVLATLLN NLKVQERQNR VCTTVAIAIV
AETCMPFTVV PALMADYRTP EMNVQNGVLK SLAFMFEYIG EQARDYVYAI TPLLADALMD
RDAVHRQTAA SVIKHLSLGC VGLGVEDAMI HLLNILWPNI LEESPHVINA VREGIDGIRN
CIGVGPIMAY LVQGLFHPSR KVRNTYWTSY NSAYVQSADA MVPYYPHVDD DQFNNYDMKT
LHICI
