SAP61_SCHPO
ID SAP61_SCHPO Reviewed; 492 AA.
AC O59706;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Pre-mRNA-splicing factor sap61;
DE AltName: Full=Spliceosome-associated protein 61;
GN Name=sap61; ORFNames=SPBC36.09;
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-360, 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 mRNA splicing where it associates with cdc5 and
CC the other cwf proteins as part of the spliceosome.
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:0000305|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19057.1; -; Genomic_DNA.
DR PIR; T40304; T40304.
DR RefSeq; NP_595337.1; NM_001021245.2.
DR AlphaFoldDB; O59706; -.
DR SMR; O59706; -.
DR BioGRID; 277448; 17.
DR IntAct; O59706; 6.
DR STRING; 4896.SPBC36.09.1; -.
DR iPTMnet; O59706; -.
DR MaxQB; O59706; -.
DR PaxDb; O59706; -.
DR PRIDE; O59706; -.
DR EnsemblFungi; SPBC36.09.1; SPBC36.09.1:pep; SPBC36.09.
DR GeneID; 2540932; -.
DR KEGG; spo:SPBC36.09; -.
DR PomBase; SPBC36.09; sap61.
DR VEuPathDB; FungiDB:SPBC36.09; -.
DR eggNOG; KOG2636; Eukaryota.
DR HOGENOM; CLU_027160_1_0_1; -.
DR InParanoid; O59706; -.
DR OMA; KDAHRRN; -.
DR PhylomeDB; O59706; -.
DR PRO; PR:O59706; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; 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:0003723; F:RNA binding; ISS:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR031776; SF3A3.
DR InterPro; IPR031774; SF3A3_dom.
DR InterPro; IPR024598; SF3a60/Prp9_C.
DR InterPro; IPR021966; SF3a60_bindingd.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12786:SF2; PTHR12786:SF2; 1.
DR Pfam; PF16837; SF3A3; 1.
DR Pfam; PF12108; SF3a60_bindingd; 1.
DR Pfam; PF11931; SF3a60_Prp9_C; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..492
FT /note="Pre-mRNA-splicing factor sap61"
FT /id="PRO_0000352806"
FT ZN_FING 243..267
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..428
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 268..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 492 AA; 57255 MW; 5208F677B10E9B95 CRC64;
MSESVLETER YAHEELERLQ QAIVDRQVAN PKAPRERLRL EHQSAQFLNQ FRETSKKLLV
SHESSDRLKD QEVARINADD DLTEFYKSLG EIQEFHKKYP DHKVEDLSQL YSIKPSQPGI
DEIDTLFRGE EMYGRFMDLN ECYEEYINLS NVQHISYLEY LKNLEDFDQI PKPEKNQTYI
NYITHLYEYL VSFYRRTHPL SNLDKIIAVF DTEFDAAWEA GLPGWYSHNA EAEKDGKDST
EAFYCEVCQK FFGKITVFEA HKKSKAHNKA VKRMQSSSPS TTSNTNEKQK GPKAIARIEF
LIKKLTSLLD DVRKDTRENV VRRQTLTAAE RLAEVEAAER EAFEQSTPSV SVEGNQDEES
DQDDEEKIYN PLKLPLGWDG KPIPFWLWKL HGLGKEFPCE ICGNYVYMGR KAFDKHFTEQ
RHIYGLKCLG ISPSPLFNQI TSIDEALQLW QKYKVDSKKR ETTMASLNEM EDDEGNVMSE
KVYNDLKAQG LL
