NXF1_PONAB
ID NXF1_PONAB Reviewed; 626 AA.
AC Q5R752;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Nuclear RNA export factor 1;
GN Name=NXF1;
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: Involved in the nuclear export of mRNA species bearing
CC retroviral constitutive transport elements (CTE) and in the export of
CC mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-
CC NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction
CC with ALYREF/THOC4 and THOC5 components of the TREX complex.
CC ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1
CC heterodimer for export. Also involved in nuclear export of m6A-
CC containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-
CC containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear
CC export. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SUBUNIT: Heterodimer (via NTF2 domain) with NXT1. The formation of
CC NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA
CC export. Forms a complex with RANBP2/NUP358, NXT1 and RANGAP1.
CC Associates with the exon junction complex (EJC) and with the
CC transcription/export (TREX) complex. Found in a mRNA complex with UPF3A
CC and UPF3B. Found in a post-splicing complex with RBM8A, UPF1, UPF2,
CC UPF3A, UPF3B and RNPS1. Interacts (via N-terminus) with DHX9 (via N-
CC terminus); this interaction is direct and negatively regulates NXF1-
CC mediated nuclear export of constitutive transport element (CTE)-
CC containing cellular mRNAs. Interacts with ALYREF/THOC4. Interacts with
CC FYTTD1/UIF. Interacts with EIF4A3. Interacts with NUPL2. Interacts with
CC THOC5. Interacts with CHTOP. Interacts with FRG1 (via N-terminus).
CC Interacts with LUZP4. Interacts with FMR1; the interaction occurs in a
CC mRNA-dependent and polyribosomes-independent manner in the nucleus.
CC Interacts with CPSF6 (via N-terminus); this interaction is direct.
CC Interacts with RBM15. Interacts with RBM15B. Interacts with MCM3AP;
CC this interaction is not mediated by RNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus {ECO:0000250|UniProtKB:Q9UBU9}.
CC Note=Localized predominantly in the nucleoplasm and at both the
CC nucleoplasmic and cytoplasmic faces of the nuclear pore complex.
CC Shuttles between the nucleus and the cytoplasm. Travels to the
CC cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The
CC association with the TREX complex seems to occur in regions surrounding
CC nuclear speckles known as perispeckles. Nucleus; nuclear rim.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The minimal CTE binding domain consists of an RNP-type RNA
CC binding domain (RBD) and leucine-rich repeats.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The nucleoporin binding domain consists of a NTF2 domain (also
CC called NTF2-like domain) and a TAP-C domain (also called UBA-like
CC domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2
CC and the other in the TAP-C domain) which contribute to nucleoporin
CC association and act synergistically to export cellular mRNAs.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The NTF2 domain is functional only in the presence of NXT1 and
CC is essential for the export of mRNA from the nucleus. It inhibits RNA
CC binding activity through an intramolecular interaction with the N-
CC terminal RNA binding domain (RBD); the inhibition is removed by an
CC association with the TREX complex, specifically involving ALYREF/THOC4
CC and THOC5. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The TAP-C domain mediates direct interactions with nucleoporin-
CC FG-repeats and is necessary and sufficient for localization of NXF1 to
CC the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has
CC a critical role in the interaction with nucleoporins.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The leucine-rich repeats are essential for the export of mRNA
CC from the nucleus. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SIMILARITY: Belongs to the NXF family. {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; CR860266; CAH92408.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q5R752; -.
DR BMRB; Q5R752; -.
DR SMR; Q5R752; -.
DR STRING; 9601.ENSPPYP00000003631; -.
DR eggNOG; KOG3763; Eukaryota.
DR InParanoid; Q5R752; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd14342; UBA_TAP-C; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR005637; TAP_C_dom.
DR InterPro; IPR015245; Tap_RNA-bd.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10662; PTHR10662; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF09162; Tap-RNA_bind; 1.
DR Pfam; PF03943; TAP_C; 1.
DR SMART; SM00804; TAP_C; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Leucine-rich repeat; Methylation; mRNA transport;
KW Nitration; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT CHAIN 2..626
FT /note="Nuclear RNA export factor 1"
FT /id="PRO_0000270917"
FT DOMAIN 119..198
FT /note="RRM"
FT REPEAT 266..291
FT /note="LRR 1"
FT REPEAT 292..315
FT /note="LRR 2"
FT REPEAT 316..350
FT /note="LRR 3"
FT REPEAT 351..378
FT /note="LRR 4"
FT DOMAIN 393..543
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 572..626
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..198
FT /note="Interaction with ALYREF/THOC4 and LUZP4"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT REGION 2..118
FT /note="RNA-binding (RBD)"
FT /evidence="ECO:0000250"
FT REGION 2..60
FT /note="Minor non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 61..118
FT /note="Major non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 61..118
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT MOTIF 67..100
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 83..110
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 42
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 126
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
SQ SEQUENCE 626 AA; 70914 MW; 68B3EEF3DE003492 CRC64;
MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA
MSDAQDGPRV RYNPYTTRPN RRGDAWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF
KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL
DRENRRISII INPSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVS
QNIDVVLNRR SCMAATLRVI EENIPELLSL NLSHNRLYRL DDMSSIVQKV PNLKILNLSG
NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYIRS VVACVSAIRE RFPKLLRLDG
HELPPPIAFD VEAPTTLPPC KGSYFGTENL KSLVLHFLQQ YYAIYDSGDR QGLLDAYHDG
ACCSLSIPFI PQNPARSSLA EYFKDSRNVK KLKDPTLRFR LLKHTRLNVV AFLNELPKTQ
HDVNSFVVDI SAQTSTLPCF SVNGVFKEVD GKSRDSLRAF TRTFIAVPAS NSGLCIVNDE
LFVRNASSEE IQRAFAMPAP TPSSSPVPTL SPEQQEMLQA FSTQSGMNLE WSQKCLQDNN
WDYTRSAQAF THLKAKGEIP EVAFMK
