SFSWA_MOUSE
ID SFSWA_MOUSE Reviewed; 945 AA.
AC Q3USH5; Q8CCZ1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Splicing factor, suppressor of white-apricot homolog;
DE AltName: Full=Splicing factor, arginine/serine-rich 8;
DE AltName: Full=Suppressor of white apricot protein homolog;
GN Name=Sfswap; Synonyms=Sfrs8, Srsf8, Swap;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845.
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-601; SER-621;
RP SER-899 AND SER-903, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: Plays a role as an alternative splicing regulator. Regulates
CC its own expression at the level of RNA processing. Also regulates the
CC splicing of fibronectin and CD45 genes. May act, at least in part, by
CC interaction with other R/S-containing splicing factors. Represses the
CC splicing of MAPT/Tau exon 10 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q3USH5; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-8387273, EBI-744603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AC114614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031872; BAC27586.1; -; mRNA.
DR EMBL; AK140369; BAE24357.1; -; mRNA.
DR CCDS; CCDS19694.1; -.
DR RefSeq; NP_758480.2; NM_172276.3.
DR AlphaFoldDB; Q3USH5; -.
DR SMR; Q3USH5; -.
DR BioGRID; 231165; 2.
DR IntAct; Q3USH5; 3.
DR MINT; Q3USH5; -.
DR STRING; 10090.ENSMUSP00000062413; -.
DR iPTMnet; Q3USH5; -.
DR PhosphoSitePlus; Q3USH5; -.
DR EPD; Q3USH5; -.
DR jPOST; Q3USH5; -.
DR MaxQB; Q3USH5; -.
DR PaxDb; Q3USH5; -.
DR PeptideAtlas; Q3USH5; -.
DR PRIDE; Q3USH5; -.
DR ProteomicsDB; 256631; -.
DR Antibodypedia; 19429; 188 antibodies from 27 providers.
DR DNASU; 231769; -.
DR Ensembl; ENSMUST00000053737; ENSMUSP00000062413; ENSMUSG00000029439.
DR GeneID; 231769; -.
DR KEGG; mmu:231769; -.
DR UCSC; uc008zsu.1; mouse.
DR CTD; 6433; -.
DR MGI; MGI:101760; Sfswap.
DR VEuPathDB; HostDB:ENSMUSG00000029439; -.
DR eggNOG; KOG1847; Eukaryota.
DR GeneTree; ENSGT00940000153892; -.
DR HOGENOM; CLU_015459_0_0_1; -.
DR InParanoid; Q3USH5; -.
DR OMA; IAFNYDE; -.
DR OrthoDB; 1414730at2759; -.
DR TreeFam; TF106264; -.
DR BioGRID-ORCS; 231769; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Sfswap; mouse.
DR PRO; PR:Q3USH5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3USH5; protein.
DR Bgee; ENSMUSG00000029439; Expressed in embryonic post-anal tail and 246 other tissues.
DR ExpressionAtlas; Q3USH5; baseline and differential.
DR Genevisible; Q3USH5; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IDA:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR040397; SWAP.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR InterPro; IPR019147; SWAP_N_domain.
DR PANTHER; PTHR13161; PTHR13161; 1.
DR Pfam; PF09750; DRY_EERY; 1.
DR Pfam; PF01805; Surp; 2.
DR SMART; SM01141; DRY_EERY; 1.
DR SMART; SM00648; SWAP; 2.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50128; SURP; 2.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..945
FT /note="Splicing factor, suppressor of white-apricot
FT homolog"
FT /id="PRO_0000413023"
FT REPEAT 211..253
FT /note="SURP motif 1"
FT REPEAT 458..498
FT /note="SURP motif 2"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 632..686
FT /evidence="ECO:0000255"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..811
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..859
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12872"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12872"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12872"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 945 AA; 104190 MW; 7B2CBDCB63A89AA2 CRC64;
MYGAGGGRAK PERKGGVKEE AGPGGTGTGG NRVELLVFGY ACKLFRDDER ALAQEQGQHL
IPWMGDPKIL IDRYDGRGHL HDLSAYDAEY ATWNRDYQLS EEEARVEALC DEERYLALHT
DLLEEEARQE EEYKRLSEAL AEDGNYSAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN
LEENEEPFIA PLGLSVPSDV ELPPTAKMHA IIERTANFVC KQGAQFEIML KAKQARNSQF
DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE SKNEEKKKSG PTSDNEEEDD EEDGSYLHPS
LFASKKSSRL EELMKPLKVV DPDHPLAALV RKAQADSSAP APPTADGTPA QPSQVEYTAD
STVAAMYYSY YMLPDGTYCL APPPPGIDVA TYYSTLPAGV TVSSSPGVTT TVPPPPGTTP
PPPPTTAEPS SGVTSTTTTT SALAPVAIIP PPPDIQPVID KLAEYVARNG LKFETSVRAK
NDQRFEFLQP WHQYNAYYEF KKQFFLQKEG GGSTQAASTA EEAPTETAVE ESGEAGEDGA
PEGMAETGGR GSGKKEAGSS KSTVDGKLVK ASFAPISFAI KAKENDLLPL EKNRVKLDDD
SEEDEESREC QESTSSVANP SPAAAPPSVA VEEKKPQLTQ EELEAKQAKQ KLEDRLAAAA
REKLAQASKE SKEKQLQAER KRKAALFLQT LKNPLPEAEV GKLEESTFGV EDTGVMPCPL
LVGGRTLPIL EGKPPERPSN RCRDPPREEE REKKKKKHKK RSRTRSRSPK YHSSSKPRSR
SHSKAKHSLP SAYRTVRRSR SRSRSPRRRA HSPERRREER SVPTAYRMSG SPGVSRKRTR
SRSPHEKKKK RRSRSRTKAK ARSQSTSPSK QAAQRPSAHS AHSASISPVE SRGSSQERSR
GVSQEKDGQI SSAIVSSVQS KITQDLMAKV RAMLAASKNL QTSAS
