SFSWA_RAT
ID SFSWA_RAT Reviewed; 945 AA.
AC D3ZTQ1; Q5BJQ4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-945.
RC TISSUE=Brain;
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 [3]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-601 AND SER-903, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role as an alternative splicing regulator. Regulate
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 (By similarity).
CC Represses the splicing of MAPT/Tau exon 10. {ECO:0000250,
CC ECO:0000269|PubMed:15009664}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CH473973; EDM13504.1; -; Genomic_DNA.
DR EMBL; BC091384; AAH91384.1; -; mRNA.
DR RefSeq; XP_006249333.1; XM_006249271.3.
DR AlphaFoldDB; D3ZTQ1; -.
DR SMR; D3ZTQ1; -.
DR STRING; 10116.ENSRNOP00000001235; -.
DR iPTMnet; D3ZTQ1; -.
DR PaxDb; D3ZTQ1; -.
DR PeptideAtlas; D3ZTQ1; -.
DR PRIDE; D3ZTQ1; -.
DR Ensembl; ENSRNOT00000093237; ENSRNOP00000076174; ENSRNOG00000000931.
DR GeneID; 304431; -.
DR CTD; 6433; -.
DR RGD; 1305004; Sfswap.
DR eggNOG; KOG1847; Eukaryota.
DR GeneTree; ENSGT00940000153892; -.
DR InParanoid; D3ZTQ1; -.
DR OrthoDB; 1414730at2759; -.
DR PhylomeDB; D3ZTQ1; -.
DR TreeFam; TF106264; -.
DR PRO; PR:D3ZTQ1; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Genevisible; D3ZTQ1; RN.
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; ISO:RGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISO:RGD.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA: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_0000413024"
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 157..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..298
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..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..566
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 714..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 269..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
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:22673903"
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:22673903"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3USH5"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12872"
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:0000250|UniProtKB:Q3USH5"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 543..570
FT /note="Missing (in Ref. 2; AAH91384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 945 AA; 104147 MW; 798AF7450C11BAB4 CRC64;
MYGAGGGRAK AERKGGVKEE AGPGGTGTGG NRVELLVFGY ACKLFRDDER ALAQEQGQHL
IPWMGDHKIL IDRYDGRGHL HDLSAYDAEY ATWNRDYQLS EEEARVEALC DEERYLALHT
DLLEEEARQE EEYKRLSEAL AEDGNYSAVG FTYGSDYYDP SEPTEEEEPS KQREKSEAEN
LEENEEPFIA PLGLSVPSDV ELPPTAKMHA IIERTANFVC KQGAQFEIML KAKQARNSQF
DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE SKSEEKKKSG PTSDNEEEDD EEDGSYLHPS
LFASKKSSRL EELMKPLKVV DPDHPLAALV RKAQADSSAP APPTADGTPA QPSQVEYTAD
STVAAMYYSY YMLPDGTYCL APPPPGIDVA TYYSTLPAGV TVSSSPGVTT TVPPPPGTTP
PPPPTTAESS SGVTSTTTTT SALAPVAIIP PPPDIQPVID KLAEYVARNG LKFETSVRAK
NDQRFEFLQP WHQYNAYYEF KKQFFLQKEG GGSTQAASTA EEAPTETAVE ESSEAGEDGA
PEGMAETGGR GSGKKEAGSS KSTVDGKLVK ASFAPISFAI KAKENDLLPL EKNRVKLDDD
SEEDEESREC QESTSSVANP SPAAAPPSAV VEEKKPQLTQ EELEAKQAKQ KLEDRLAAAA
REKLAQASKE SKEKQLQAER KRKAALFLQT LKNPLPDAEV GKLEESTFGV EETGVMPCPL
LVGGRTLPML EGKPPERPSS RCRDPPREEE REKKKKKHKK RSRTRSRSPK YHSSSKPRSR
SHSKAKHSLP SAYRTVRRSR SRSRSPRRRA HSPERRREDR SVPTAYRMSG SPGVSRKRTR
SRSPHEKKKK RRSRSRTKAK ARSQSTSPSK QAAQRPSAHS AHSASISPVE SRGSSQERSR
GVSQEKDGQI SSAIVSSVQS KITQDLMAKV RAMLAASKNL QTSAS
