ID   SF01_MOUSE              Reviewed;         653 AA.
AC   Q64213; E9QK02; O08817; P70167; Q61454; Q921Z4;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 6.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Splicing factor 1;
DE   AltName: Full=CW17;
DE   AltName: Full=Mammalian branch point-binding protein;
DE            Short=BBP;
DE            Short=mBBP;
DE   AltName: Full=Transcription factor ZFM1;
DE            Short=mZFM;
DE   AltName: Full=Zinc finger gene in MEN1 locus;
DE   AltName: Full=Zinc finger protein 162;
GN   Name=Sf1; Synonyms=Zfm1, Zfp162;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CW17 AND CW17E).
RC   STRAIN=C57BL/10; TISSUE=Spleen;
RX   PubMed=9212169; DOI=10.1089/dna.1997.16.761;
RA   Wrehlke C., Schmitt-Wrede H.-P., Qiao Z.D., Wunderlich F.;
RT   "Enhanced expression in spleen macrophages of the mouse homolog to the
RT   human putative tumor suppressor gene ZFM1.";
RL   DNA Cell Biol. 16:761-767(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57B1/10;
RX   PubMed=10360842; DOI=10.1089/104454999315303;
RA   Wrehlke C., Wiedemeyer W.-R., Schmitt-Wrede H.-P., Mincheva A., Lichter P.,
RA   Wunderlich F.;
RT   "Genomic organization of mouse gene zfp162 (mzfm).";
RL   DNA Cell Biol. 18:419-428(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CW17E AND 3).
RC   STRAIN=C3H/He; TISSUE=Mammary tumor, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND TYR-87, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND TYR-87, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Necessary for the ATP-dependent first step of spliceosome
CC       assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3'
CC       of the pre-mRNA. May act as transcription repressor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Interacts with RBM17.
CC       Binds EWSR1, FUS and TAF15 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=CW17;
CC         IsoId=Q64213-1; Sequence=Displayed;
CC       Name=CW17E;
CC         IsoId=Q64213-2; Sequence=VSP_050424;
CC       Name=3;
CC         IsoId=Q64213-3; Sequence=VSP_008840;
CC   -!- TISSUE SPECIFICITY: Detected at intermediate levels in spleen. Lower
CC       levels in heart, kidney, brain, liver, testis, bone marrow, adrenal
CC       gland, lymph nodes, pancreas and thymus.
CC   -!- PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and
CC       spliceosome assembly. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}.
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DR   EMBL; X80159; CAA56440.1; -; mRNA.
DR   EMBL; X85802; CAA59797.1; -; mRNA.
DR   EMBL; Y08907; CAA70113.1; -; Genomic_DNA.
DR   EMBL; Y12838; CAA73359.1; -; Genomic_DNA.
DR   EMBL; AC127556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC167245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009091; AAH09091.1; -; mRNA.
DR   EMBL; BC055370; AAH55370.1; -; mRNA.
DR   CCDS; CCDS50368.1; -. [Q64213-3]
DR   CCDS; CCDS50369.1; -. [Q64213-2]
DR   AlphaFoldDB; Q64213; -.
DR   BMRB; Q64213; -.
DR   SMR; Q64213; -.
DR   ComplexPortal; CPX-5861; SF1-U2AF65 splicing factor complex.
DR   DIP; DIP-60453N; -.
DR   ELM; Q64213; -.
DR   IntAct; Q64213; 2.
DR   STRING; 10090.ENSMUSP00000121309; -.
DR   GlyGen; Q64213; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q64213; -.
DR   PhosphoSitePlus; Q64213; -.
DR   SwissPalm; Q64213; -.
DR   EPD; Q64213; -.
DR   jPOST; Q64213; -.
DR   MaxQB; Q64213; -.
DR   PaxDb; 10090-ENSMUSP00000121309; -.
DR   PeptideAtlas; Q64213; -.
DR   ProteomicsDB; 261501; -. [Q64213-1]
DR   ProteomicsDB; 261502; -. [Q64213-2]
DR   ProteomicsDB; 261503; -. [Q64213-3]
DR   Pumba; Q64213; -.
DR   Antibodypedia; 15586; 503 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000131252.8; ENSMUSP00000121309.2; ENSMUSG00000024949.18. [Q64213-3]
DR   AGR; MGI:1095403; -.
DR   MGI; MGI:1095403; Sf1.
DR   VEuPathDB; HostDB:ENSMUSG00000024949; -.
DR   eggNOG; KOG0119; Eukaryota.
DR   GeneTree; ENSGT00940000157258; -.
DR   InParanoid; Q64213; -.
DR   OMA; KPWQQRG; -.
DR   TreeFam; TF319159; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   ChiTaRS; Sf1; mouse.
DR   PRO; PR:Q64213; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q64213; Protein.
DR   Bgee; ENSMUSG00000024949; Expressed in retinal neural layer and 88 other cell types or tissues.
DR   ExpressionAtlas; Q64213; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR   GO; GO:0016604; C:nuclear body; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR   GO; GO:0089701; C:U2AF complex; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0033327; P:Leydig cell differentiation; IGI:MGI.
DR   GO; GO:0030238; P:male sex determination; IGI:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0030575; P:nuclear body organization; IMP:MGI.
DR   GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; IGI:MGI.
DR   CDD; cd22382; KH-I_SF1; 1.
DR   Gene3D; 6.10.140.1790; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR045071; BBP-like.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR032570; SF1-HH.
DR   InterPro; IPR047086; SF1-HH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR   PANTHER; PTHR11208:SF45; SPLICING FACTOR 1; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF16275; SF1-HH; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
DR   Genevisible; Q64213; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   RNA-binding; Spliceosome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15637"
FT   CHAIN           2..653
FT                   /note="Splicing factor 1"
FT                   /id="PRO_0000050130"
FT   DOMAIN          141..222
FT                   /note="KH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   ZN_FING         277..296
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..19
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        346..361
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..518
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..584
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15637"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15637"
FT   MOD_RES         20
FT                   /note="Phosphoserine; by PKG"
FT                   /evidence="ECO:0000250|UniProtKB:Q15637"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         87
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15637"
FT   VAR_SEQ         529..653
FT                   /note="TTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPLPPGVQPPLPPG
FT                   APPPPPCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGRQP
FT                   QQRPWWTGWFGKAA -> SLPAAAMARAMRVRTFRAHW (in isoform CW17E)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9212169"
FT                   /id="VSP_050424"
FT   VAR_SEQ         586..653
FT                   /note="PCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGR
FT                   QPQQRPWWTGWFGKAA -> PPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMP
FT                   PFGMPPAPPPPPPQN (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_008840"
FT   CONFLICT        184
FT                   /note="K -> E (in Ref. 1; CAA59797 and 2; CAA73359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="P -> S (in Ref. 4; AAH55370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        524
FT                   /note="P -> L (in Ref. 4; AAH09091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586
FT                   /note="P -> T (in Ref. 2; CAA73359/CAA70113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   653 AA;  70403 MW;  5C159302822509D1 CRC64;
     MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED
     LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH TLITEMVALN
     PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK
     GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR
     KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP
     QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA SNPPPPSLMS
     TTQSRPPWMN SGPSENRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP
     PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP
     PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS
     IPPWQQQQAA AAASPGTPQM QGNPTMVPLP PGVQPPLPPG APPPPPCSIE CLLCLLSSPN
     SLCLSPNRAA RIPPRGSDGP SHESEDFPRP LVTLPGRQPQ QRPWWTGWFG KAA
//