SFR19_RAT
ID SFR19_RAT Reviewed; 1258 AA.
AC Q63624;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Splicing factor, arginine/serine-rich 19;
DE AltName: Full=CTD-binding SR-like protein rA1;
DE AltName: Full=SR-related and CTD-associated factor 1;
GN Name=Scaf1; Synonyms=Sfrs19;
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;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-1258, FUNCTION, AND INTERACTION WITH
RP POLR2A.
RC TISSUE=Hippocampus;
RX PubMed=8692929; DOI=10.1073/pnas.93.14.6975;
RA Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M.,
RA Corden J.L.;
RT "The C-terminal domain of the largest subunit of RNA polymerase II
RT interacts with a novel set of serine/arginine-rich proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-512; SER-520;
RP SER-678; SER-684; SER-693; SER-697; SER-914 AND THR-950, AND IDENTIFICATION
RP 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: May function in pre-mRNA splicing.
CC {ECO:0000269|PubMed:8692929}.
CC -!- SUBUNIT: Interacts with POLR2A. {ECO:0000269|PubMed:8692929}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AABR03002356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U49056; AAC52657.1; ALT_INIT; mRNA.
DR PIR; T31421; T31421.
DR RefSeq; NP_062257.1; NM_019384.1.
DR RefSeq; XP_008757631.2; XM_008759409.2.
DR RefSeq; XP_008757632.1; XM_008759410.2.
DR RefSeq; XP_017445105.1; XM_017589616.1.
DR AlphaFoldDB; Q63624; -.
DR SMR; Q63624; -.
DR STRING; 10116.ENSRNOP00000027801; -.
DR iPTMnet; Q63624; -.
DR PhosphoSitePlus; Q63624; -.
DR PaxDb; Q63624; -.
DR PRIDE; Q63624; -.
DR Ensembl; ENSRNOT00000081430; ENSRNOP00000072566; ENSRNOG00000056946.
DR GeneID; 56081; -.
DR KEGG; rno:56081; -.
DR CTD; 58506; -.
DR RGD; 708405; Scaf1.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR HOGENOM; CLU_006936_0_0_1; -.
DR InParanoid; Q63624; -.
DR OMA; PDERAPT; -.
DR OrthoDB; 332377at2759; -.
DR PhylomeDB; Q63624; -.
DR TreeFam; TF332183; -.
DR PRO; PR:Q63624; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000056946; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q63624; RN.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IMP:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR InterPro; IPR042841; SCAF1.
DR PANTHER; PTHR47013; PTHR47013; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..1258
FT /note="Splicing factor, arginine/serine-rich 19"
FT /id="PRO_0000299408"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1258
FT /note="Necessary for interaction with the CTD domain of
FT POLR2A"
FT /evidence="ECO:0000250"
FT REGION 1223..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..875
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..987
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 691
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C3"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 938
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C3"
FT MOD_RES 950
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 814
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT CONFLICT 101
FT /note="L -> V (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> G (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="P -> A (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> G (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="S -> R (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="R -> G (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 746..748
FT /note="TRP -> PRT (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="S -> R (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="A -> S (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="E -> D (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="P -> A (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="A -> D (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="S -> R (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1101
FT /note="L -> F (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="G -> A (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="A -> S (in Ref. 2; AAC52657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1258 AA; 133856 MW; BBEC7D4027E2F179 CRC64;
MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD LPNDKDGSRC
CGLQWRRCCR SPRSEPRSQE SGGADMATVL DTAADSFLVE LVSILDPPDT WVPSHLDLQP
GESEDVLELV AEVRIGDRDP MPLPVPSLLP RLRAWRTGKT VSPQSHASRP ACSRHLLTLG
TGDGGPAPPP APSSASSSPS PSPSSSSPSP PPPPPPPPPP ALPAPRFDIY DPFHPTDEAY
SPPPAPEQKY DPFEPTGSNP SSSAGTPSPE EEEEEEEEEE EEGLSQSISR ISETLAGIYD
DNSLSQDFPG DDSPHREPPP PQTLGAPGTP PQADSTRAEG APRRRVFVVG PEAEACLEGK
VSVEVVTTAG GPALPLPPLP PTDPEIEEGE IVQPEEEPRV AVSLFRAARP RQPPASVATL
ASVAAPAAPP ASAPRAPEGD DFLSLHADSD GEGALQVDLG EPPAPPAADA RWGGLDLRRK
ILTQRRERYR QRSASPGPPP ARKKARRERQ RSGDPAPPDS PTWEAKKHRS RERKLGSHST
ARRRSRSRSR RRSRSRSADR RRGSHRSRSR EKRRRRRRSA SPPPAASSSS SSRRERHRGK
RREGGKKKKK RSRSRAEKRS GDLEKLPAPV PPSGSDRDSR RRGAVPPSIQ DLTDHDLFAI
KRTITVGRPD KTEPRAPSPA PAVSPKREVL YDSEGLSADE RGAKGDKDRR RSGAASSSSS
SREKASRRKA LDGDRGRDRD RSSKKTRPPK DSAPGSGALP KAPPSSGSSS SSSSCSSRKV
KLQSKVAVLI REGVSSTTPA KDSSSSGLGS IGVKFSRDRE SRSPFLKPDE RAPAEGVKVA
PGSTKPKKTK AKAKAGAKKA KGTKGKTKPS KTRKKVRSGG SSTASGGPGS LKKSKADSCS
QAASAKGTEE TSWSGEERTT KAPSTPPPKV APPPPALTPD SQTVDSSCKT PEVSFLPEEA
SEDTGVRVGA EEEEEEEEEE EEEEEQQPAT TTATSTAAAA PSTAPSAGST AGDSGAEDGP
AARASQLPTL PPPMPWNLPA GVDCTTSGVL ALTALLFKME EANLASRAKA QELIQATNQI
LSHRKPPSTL GVTPAPVPTS LGLPPGPSSY LLPGSLPIGG CGSTPPTPTG LVPASDKREG
SSSSEGRGDT DKYLKKLHTQ ERAVEEVKLA IKPYYQKKDI TKEEYKDILR KAVHKICHSK
SGEINPVKVS NLVRAYVQRY RYFRKHGRKP GDPPGPPRPP KEPGPPDKGG PGLPLPPL
