SA114_SCHPO
ID SA114_SCHPO Reviewed; 481 AA.
AC O13900;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Pre-mRNA-splicing factor sap114;
DE AltName: Full=Spliceosome-associated protein 145;
GN Name=sap114; ORFNames=SPAC22A12.09c;
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 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).
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}.
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DR EMBL; CU329670; CAB16579.1; -; Genomic_DNA.
DR PIR; T38149; T38149.
DR RefSeq; NP_593239.1; NM_001018636.2.
DR AlphaFoldDB; O13900; -.
DR SMR; O13900; -.
DR BioGRID; 277942; 204.
DR IntAct; O13900; 4.
DR STRING; 4896.SPAC22A12.09c.1; -.
DR iPTMnet; O13900; -.
DR MaxQB; O13900; -.
DR PaxDb; O13900; -.
DR PRIDE; O13900; -.
DR EnsemblFungi; SPAC22A12.09c.1; SPAC22A12.09c.1:pep; SPAC22A12.09c.
DR GeneID; 2541437; -.
DR KEGG; spo:SPAC22A12.09c; -.
DR PomBase; SPAC22A12.09c; sap114.
DR VEuPathDB; FungiDB:SPAC22A12.09c; -.
DR eggNOG; KOG0007; Eukaryota.
DR HOGENOM; CLU_013259_3_1_1; -.
DR InParanoid; O13900; -.
DR OMA; HFSARMP; -.
DR PhylomeDB; O13900; -.
DR PRO; PR:O13900; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005686; C:U2 snRNP; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; ISS:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR045146; SF3A1.
DR InterPro; IPR022030; SF3A1_dom.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR15316; PTHR15316; 1.
DR Pfam; PF12230; PRP21_like_P; 1.
DR Pfam; PF01805; Surp; 2.
DR SMART; SM00648; SWAP; 2.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50128; SURP; 2.
PE 1: Evidence at protein level;
KW Chaperone; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome.
FT CHAIN 1..481
FT /note="Pre-mRNA-splicing factor sap114"
FT /id="PRO_0000290652"
FT REPEAT 44..86
FT /note="SURP motif 1"
FT REPEAT 147..189
FT /note="SURP motif 2"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 54409 MW; 2304459FC2735878 CRC64;
MSSLMEFQDR NTTNNETEHQ KSITDQSSSV PAGVILPPPA IREIIDKSAS YVARNGPAFE
EKIRQNEQAN TKFAFLHAND PYHPYYQHKL TEAREGKLKS HATGLSTQKT STLARPIQKP
IEATIPAPSP YLFSEPLPSI SSLDLDVLRL TARYAAVRGS SFLVSLSQKE WNNTQFDFLK
PNNALYPYFM RIVQQYTSLI REPISSPEQE LRENVRDPYS LLSKIQPRVR WQSHMESQKK
KQKEEAEKEK LEYAQIDWND FVVVEVIQFT KSDEHAKLAK PTNLADLQTA TLEQKSAMFT
MPDQNYTIEE APPTAEPWEP ISAPKKQEFG VSLPPSLASP EKGGISSTTS VSPAAQASPV
LSTTTQPKVQ KPVPKAFQPK VPMEISPFSG ELVPATELEE HMRLKLLDPR WQEQRKVEES
RKSTLNLENV NVAANMKRLV SQRTDLFDVQ NGVEISQEEI ERRKRAATQS AWGATPTNKR
R
