SCAF8_RAT
ID SCAF8_RAT Reviewed; 1268 AA.
AC Q63623;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=SR-related and CTD-associated factor 8 {ECO:0000303|PubMed:9528809};
DE AltName: Full=RNA-binding motif protein 16 {ECO:0000305};
GN Name=Scaf8 {ECO:0000303|PubMed:9528809, ECO:0000312|RGD:708362};
GN Synonyms=Rbm16 {ECO:0000312|RGD:708362};
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 [MRNA], AND INTERACTION WITH 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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP 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: 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:8692929,
CC PubMed:9528809). Identified in a complex with CDC5L and other
CC spliceosomal proteins (By similarity). {ECO:0000250|UniProtKB:Q9UPN6,
CC ECO:0000269|PubMed:8692929, 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 ---------------------------------------------------------------------------
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; U49055; AAC52656.1; -; mRNA.
DR PIR; T31420; T31420.
DR RefSeq; NP_620794.1; NM_139094.1.
DR AlphaFoldDB; Q63623; -.
DR SMR; Q63623; -.
DR STRING; 10116.ENSRNOP00000062541; -.
DR iPTMnet; Q63623; -.
DR PhosphoSitePlus; Q63623; -.
DR jPOST; Q63623; -.
DR PaxDb; Q63623; -.
DR PRIDE; Q63623; -.
DR GeneID; 245926; -.
DR KEGG; rno:245926; -.
DR UCSC; RGD:708362; rat.
DR CTD; 22828; -.
DR RGD; 708362; Scaf8.
DR eggNOG; KOG0132; Eukaryota.
DR InParanoid; Q63623; -.
DR OrthoDB; 821342at2759; -.
DR PhylomeDB; Q63623; -.
DR PRO; PR:Q63623; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; ISO:RGD.
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; IMP:RGD.
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; IMP:RGD.
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_0000394195"
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 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 753..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1063
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 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 947..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1063
FT /note="Basic and acidic 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 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:Q6DID3"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN6"
SQ SEQUENCE 1268 AA; 139504 MW; 516022F8E284126E CRC64;
MEAVKTFNSE LYSLNDYKPP ISKAKMTQIT KAAIKAIKFY KHVVQSVEKF IQKCKPEYKV
PGLYVIDSIV RQSRHQVGQE KDVCAPRFSN NIISTFQNLY RCPGDDKSKI VRVLNLWQKN
NVFKSEIIQP LLDMAAGIPP PVVTPVLAST TVAMSNTPGT PVTPVTPANV VQGLPDPWVS
QITNTDTLAA VAQILQSPQG QQLQQLIQTL QIQQQKPQPS ILQALDAGLV VQLQALTAQL
TAAAAAANTL TPLDQGVSFN KKLMDRFDFG EDSEHSEESK KEIPTPQLSH VSESVNNSIF
HQIAEQLQQQ NLEQLRQQLL EQQQPQKVTP QDSQEGAFGS EHSASPSQGS SQQHFLEPEA
NLDDSIDIQQ QDMDIDEGQD VVEEEIFEPE AKKVAVRSRS RTHSRSRSRS PRKRRSRSRS
GSRKRKHRKR SRSRSRERKR KSSRSYSSER RAREREKERQ KKGLPPVRSK TLSVCSTTLW
VGQVDKKATQ QDLTNLFEEF GQIESINMIP PRGCAYVCMV HRQDSFRALQ KLSSGSYKIG
SKVIKIAWAL NKGVKTEYKQ FWDVDLGVTY IPWEKVKVDD LDGFAEGGMI DQETVNAEWE
TVKTSEPVKE TVQTTQSPAA VEKETVVTTQ SEVFPPPVTM LQIPVAPTVP AVSLVPPAFP
VSMPVPPPGF SPIPPPPFLR ASFNPSQPPP GFMPPPVPPP VVPPPAIPPV VPTSLVQPPL
SMTPETVKDV GFGSLVLPGG SVAGNLAPST LPAGNVFNPP SKAEPEEKVP HLTEHQIPSG
ENTRPVIPSD IPSSAPMLAQ PPGASNTSGI LCVQRPNVSS NSEILGVRPA NVSNSAAIMG
AQPPNMLNNS GILGIQPPNV SSGSGLLGVL PPNLPNNSGL VGLQPPNVTN PAGLLGTQPP
IGPQNLPPLT IPAQRMPALP MLDIRPGLIA QAPGPRFPLL QPGIPPQRGI PPPSVLDAAL
HPPPRGPFPP GDLFSQPERP FLAPGRPNID SVPNPDKRIP LGNDNIQQEG DRDYRFPPIE
TREGINRPPP VDVRDVVGRP IDPREGPGRP PLDGRDHFGR PPVDMRETLV RPGLDHLGRR
DHFGFPPEKP WGPRDFDERE HRVLPVFGGP KGLHEERGRF RAGNYRFDPR SGPWNRGFGQ
EVHRDFDDRR RPWERQRDRD DRDFDFCREI NGNRLGRDRI QNTWVPPPHA RVFDYFEGAT
SQRKGENVPQ VNGGNTERHA PPPPLPVQKD PELYEKLASS GDADKEESGT AAGVESEAVV
ESTETEGT
