RTF1_PONAB
ID RTF1_PONAB Reviewed; 665 AA.
AC Q5RAD5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=RNA polymerase-associated protein RTF1 homolog;
DE Flags: Fragment;
GN Name=RTF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. Binds single-stranded DNA. Required for
CC maximal induction of heat-shock genes. Required for the trimethylation
CC of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell
CC pluripotency; this function is synergistic with CXXC1 indicative for an
CC involvement of a SET1 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (By similarity). The PAF1 complex interacts
CC with PHF5A (By similarity). {ECO:0000250|UniProtKB:A2AQ19,
CC ECO:0000250|UniProtKB:Q92541}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- DOMAIN: The Plus3 domain mediates single-stranded DNA-binding.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91275.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR859083; CAH91275.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q5RAD5; -.
DR BMRB; Q5RAD5; -.
DR SMR; Q5RAD5; -.
DR STRING; 9601.ENSPPYP00000007219; -.
DR eggNOG; KOG2402; Eukaryota.
DR InParanoid; Q5RAD5; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.200; -; 1.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR Pfam; PF03126; Plus-3; 1.
DR SMART; SM00719; Plus3; 1.
DR SUPFAM; SSF159042; SSF159042; 1.
DR PROSITE; PS51360; PLUS3; 1.
PE 2: Evidence at transcript level;
KW Activator; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT CHAIN <1..>665
FT /note="RNA polymerase-associated protein RTF1 homolog"
FT /id="PRO_0000255937"
FT DOMAIN 348..479
FT /note="Plus3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00693"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..555
FT /evidence="ECO:0000255"
FT COMPBIAS 62..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92541"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92541"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92541"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92541"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92541"
FT NON_TER 1
FT NON_TER 665
SQ SEQUENCE 665 AA; 75334 MW; 91373B4734450F6D CRC64;
GVGRAAAAAA AVAVPLAGGQ EGSPGGGRRG SRGTTMVKKR KGRVVIDSDT EDSGSDENLD
QELPSLAKRK RSDSEEKEPP VSQPAASSDS ETSDSDDEWT FGSNKNKKKG KARKIEKKGT
MKKQANKTAS SGSSDKDSSA ESSAPEEGEV SDSDSNSSSS SSDSDSSSED EEFHDGYGED
LMGDEEDRAR LEQMTEKERE QELFNRIEKR EVLKRRFEIK KKLKTAKKKE KKEKKKKQEE
EQEKKKLTQI QESQVTSHNK ERRSKRDEKL DKKSQAMEEL KAEREKRKNR TVELLAKKQP
LKTSEVYSDD EEEEEDDKSS EKSDRSSRTS SSDEEEEKEE IPPKSQPVSL PEELNRVRLS
RHKLERWCHM PFFAKTVTGC FVRIGIGNHN SKPVYRVAEI TGVVETAKVY QLGGTRTNKG
LQLRHGNDQR VFRLEFVSNQ EFTESEFMKW KEAMFSAGMQ LPTLDEINKK ELSIKEALNY
KFNDQDIEEI VKEKERFRKA PPNYAMKKTQ LLKEKAMAED LGDQDKAKQI QDQLNELEER
AEALDRQRTK NISAISYINQ RNREWNIVES EKALVAESHN MKNQQMDPFT RRQCKPTIVS
NSRDPAVQAA ILAQLNAKYG SGVLPDAPKE MSKGQGKDKD LNSKSASDLS EDLFKVHDFD
VKIDL
