SCAF8_MOUSE
ID SCAF8_MOUSE Reviewed; 1268 AA.
AC Q6DID3; Q3TTX6; Q5U5V8; Q80TJ3; Q8C037;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=SR-related and CTD-associated factor 8 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 16 {ECO:0000305};
GN Name=Scaf8 {ECO:0000312|MGI:MGI:1925212};
GN Synonyms=Kiaa1116 {ECO:0000303|PubMed:12693553},
GN Rbm16 {ECO:0000312|MGI:MGI:1925212};
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 MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-1268.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Skin;
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 [4]
RP INTERACTION WITH POLR2A.
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 [5]
RP INTERACTION WITH POLR2A, AND SUBCELLULAR LOCATION.
RX PubMed=9528809; DOI=10.1128/mcb.18.4.2406;
RA Patturajan M., Wei X., Berezney R., Corden J.L.;
RT "A nuclear matrix protein interacts with the phosphorylated C-terminal
RT domain of RNA polymerase II.";
RL Mol. Cell. Biol. 18:2406-2415(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1071, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Anti-terminator protein required to prevent early mRNA
CC termination during transcription. Together with SCAF4, acts by
CC suppressing the use of early, alternative poly(A) sites, thereby
CC preventing the accumulation of non-functional truncated proteins.
CC Mechanistically, associates with the phosphorylated C-terminal
CC heptapeptide repeat domain (CTD) of the largest RNA polymerase II
CC subunit (POLR2A), and subsequently binds nascent RNA upstream of early
CC polyadenylation sites to prevent premature mRNA transcript cleavage and
CC polyadenylation. Independently of SCAF4, also acts as a positive
CC regulator of transcript elongation. {ECO:0000250|UniProtKB:Q9UPN6}.
CC -!- SUBUNIT: Interacts with POLR2A; via C-terminal heptapeptide repeat
CC domain (CTD) phosphorylated at 'Ser-2' and 'Ser-5' (PubMed:9528809).
CC Identified in a complex with CDC5L and other spliceosomal proteins (By
CC similarity). {ECO:0000250|UniProtKB:Q9UPN6,
CC ECO:0000269|PubMed:9528809}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9528809}. Nucleus
CC matrix {ECO:0000269|PubMed:9528809}. Note=Detected in granular nuclear
CC foci which correspond to sites of active transcription.
CC {ECO:0000250|UniProtKB:Q9UPN6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65733.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK122451; BAC65733.1; ALT_INIT; mRNA.
DR EMBL; BC038363; AAH38363.1; -; mRNA.
DR EMBL; BC075621; AAH75621.1; -; mRNA.
DR EMBL; AK032418; BAC27860.1; -; mRNA.
DR EMBL; AK161113; BAE36197.1; -; mRNA.
DR CCDS; CCDS49927.1; -.
DR RefSeq; NP_598884.2; NM_134123.3.
DR AlphaFoldDB; Q6DID3; -.
DR SMR; Q6DID3; -.
DR BioGRID; 223085; 2.
DR IntAct; Q6DID3; 1.
DR MINT; Q6DID3; -.
DR STRING; 10090.ENSMUSP00000076024; -.
DR iPTMnet; Q6DID3; -.
DR PhosphoSitePlus; Q6DID3; -.
DR EPD; Q6DID3; -.
DR jPOST; Q6DID3; -.
DR MaxQB; Q6DID3; -.
DR PaxDb; Q6DID3; -.
DR PeptideAtlas; Q6DID3; -.
DR PRIDE; Q6DID3; -.
DR ProteomicsDB; 255478; -.
DR Antibodypedia; 33407; 101 antibodies from 22 providers.
DR Ensembl; ENSMUST00000076734; ENSMUSP00000076024; ENSMUSG00000046201.
DR GeneID; 106583; -.
DR KEGG; mmu:106583; -.
DR UCSC; uc008aei.2; mouse.
DR CTD; 22828; -.
DR MGI; MGI:1925212; Scaf8.
DR VEuPathDB; HostDB:ENSMUSG00000046201; -.
DR eggNOG; KOG0132; Eukaryota.
DR GeneTree; ENSGT00530000063946; -.
DR HOGENOM; CLU_005263_1_0_1; -.
DR InParanoid; Q6DID3; -.
DR OMA; QRKADNM; -.
DR OrthoDB; 821342at2759; -.
DR PhylomeDB; Q6DID3; -.
DR TreeFam; TF324527; -.
DR BioGRID-ORCS; 106583; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Scaf8; mouse.
DR PRO; PR:Q6DID3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6DID3; protein.
DR Bgee; ENSMUSG00000046201; Expressed in dorsal pancreas and 249 other tissues.
DR ExpressionAtlas; Q6DID3; baseline and differential.
DR Genevisible; Q6DID3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; ISO:MGI.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; ISS:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd12462; RRM_SCAF8; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034370; SCAF8_RRM.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1268
FT /note="SR-related and CTD-associated factor 8"
FT /id="PRO_0000394194"
FT DOMAIN 1..139
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 477..551
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 270..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..441
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 925
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 936
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 1071
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT CONFLICT 938
FT /note="P -> T (in Ref. 3; BAC27860)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="N -> I (in Ref. 2; AAH38363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1268 AA; 139572 MW; 8FDFB70FCB2791FC CRC64;
MEAVKTFNSE LYSLNDYKPP ISKAKMTQIT KAAIKAIKFY KHVVQSVEKF IQKCKPEYKV
PGLYVIDSIV RQSRHQFGQE KDVFAPRFSN NIISTFQNLY RCPGDDKSKI VRVLNLWQKN
NVFKSEIIQP LLDMAAGIPP PVVTPVLAST TAAMSNTPGT PVTPVTPANV VQGLPDPWVS
QIANTDTLAA VAQILQSPQG QQLQQLIQTL QIQQQKPQPS ILQALDAGLV VQLQALTAQL
TAAAAAANTL TPLDQGVSFN KKLMDRFDFG EDSEHSEESK KEMPTPQLSH VSESVNNSIF
HQIAEQLQQQ NLEQLRQQLL EQQQPQKVTP QDSQEGTFGS EHSASPSQGS SQQHFLEPEA
NLDDSIDIQQ QDMDIDEGQD VVEEEIFEPE AKKVAVRSRS RTHSRSRSRS PRKRRSRSRS
GSRKRKHRKR SRSHSREKKR KASRSYSSER RAREREKERQ KKGLPPVRSK TLSVCSTTLW
VGQVDKKATQ QDLTNLFEEF GQIESINMIP PRGCAYVCMV HRQDSFRALQ KLSSGSYKIG
SKVIKIAWAL NKGVKTEYKQ FWDVDLGVTY IPWEKVKVDD LDGFAEGGMI DQETVNAEWE
TVKASEPVKE PVQTAQSPAP VEKESVVTTQ AEVFPPPVAM LQIPVAPAVP AVSLVPPAFP
VSMPVPPPGF NPIPPPPFLR ASFNPSQPPP GFMPPPVPPP VVPPPAIPPV VPTSLVQPPL
SMTPEAVKDV GFGSLVLPSG SVAGSLAPST LPAGNVFNPP SKAEPEEKVP HLIEHQIPSG
ENTRPVIPSD IPSSAAMLAQ PPGASSTSGI LCVQRPNVSS NSEILGVRPA NVSNSAAIMG
AQPPNILNNS GILAIQPPNV SSGSGLLGVL PPNLPNNSGL VGLQPPNVTS PAGLLGTQPP
IGPQNLPPLA IPAQRMPALP MLDIRPGLIA QAPGPRFPLL QPGIPPQRGI PPPSVLDAAL
HPPPRGPFPP GDLFSQPERP FLAPGRPSID NVPNPDKRIP LGNDNIQQEG DRDYRFPPIE
TREGITRPPQ VDVRDVVGRR LDPREGPGRP PLDARDHFGR PPVDMRENLV RPSLDHLGRR
DHFGFPPEKP WGPRDFDERE HRVLPVFGGP KGLHEERGRF RAGNYRFDPR SGPWNRGFGQ
EVHRDFDDRR RPWERQRDRD DRDFDFCREI NGNRLGRDRI QNTWVPPPHA RVFDYFEGAT
SQRKGDNVPQ VNGENTERHA QPPPLPVQKD PELYEKLASS GDVDKEESGT VAGVESEAVV
ESTETEGT
