NXF1_RAT
ID NXF1_RAT Reviewed; 618 AA.
AC O88984;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Nuclear RNA export factor 1;
DE AltName: Full=Tip-associated protein;
DE AltName: Full=Tip-associating protein;
DE AltName: Full=mRNA export factor TAP;
GN Name=Nxf1; Synonyms=Tap;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Heart ventricle;
RA Tannoch V.J., Cormier-Regard S., Claycomb W.C.;
RL Submitted (SEP-1998) 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). Associates 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 FYTTD1/UIF. Interacts with
CC EIF4A3. Interacts with NUP42. Interacts with ALYREF/THOC4. Interacts
CC with CHTOP. Interacts with FRG1 (via N-terminus). Interacts with LUZP4.
CC Interacts with FMR1; the interaction occurs in a mRNA-dependent and
CC polyribosomes-independent manner in the nucleus. Interacts with CPSF6
CC (via N-terminus); this interaction is direct. Interacts with RBM15.
CC Interacts with RBM15B. Interacts with MCM3AP; this interaction is not
CC mediated by RNA (By similarity). Interacts with DDX3X (via C-terminus);
CC this interaction may be partly involved in DDX3X nuclear export and in
CC NXF1 localization to stress granules. Interacts with PABPC1/PABP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q99JX7,
CC ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the
CC nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the
CC nuclear pore complex. Shuttles between the nucleus and the cytoplasm.
CC Travels to the cytoplasm as part of the exon junction complex (EJC)
CC bound to mRNA. The association with the TREX complex seems to occur in
CC regions surrounding nuclear speckles known as perispeckles. Nucleus;
CC nuclear rim. {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}.
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DR EMBL; AF093139; AAC63367.1; -; mRNA.
DR RefSeq; NP_067590.1; NM_021579.1.
DR AlphaFoldDB; O88984; -.
DR BMRB; O88984; -.
DR SMR; O88984; -.
DR BioGRID; 248722; 1.
DR STRING; 10116.ENSRNOP00000026033; -.
DR iPTMnet; O88984; -.
DR PhosphoSitePlus; O88984; -.
DR jPOST; O88984; -.
DR PaxDb; O88984; -.
DR PRIDE; O88984; -.
DR GeneID; 59087; -.
DR KEGG; rno:59087; -.
DR UCSC; RGD:62014; rat.
DR CTD; 10482; -.
DR RGD; 62014; Nxf1.
DR eggNOG; KOG3763; Eukaryota.
DR InParanoid; O88984; -.
DR OrthoDB; 1051093at2759; -.
DR PhylomeDB; O88984; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR PRO; PR:O88984; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0042405; C:nuclear inclusion body; ISO:RGD.
DR GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR GO; GO:0042272; C:nuclear RNA export factor complex; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006405; P:RNA export from nucleus; ISO:RGD.
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; 2.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Leucine-rich repeat; Methylation; mRNA transport;
KW Nitration; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; RNA-binding; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT CHAIN 2..618
FT /note="Nuclear RNA export factor 1"
FT /id="PRO_0000220531"
FT DOMAIN 118..197
FT /note="RRM"
FT REPEAT 265..290
FT /note="LRR 1"
FT REPEAT 291..314
FT /note="LRR 2"
FT REPEAT 315..342
FT /note="LRR 3"
FT REPEAT 343..370
FT /note="LRR 4"
FT DOMAIN 385..535
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 564..618
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..197
FT /note="Interaction with ALYREF/THOC4 and LUZP4"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT REGION 2..117
FT /note="RNA-binding (RBD)"
FT /evidence="ECO:0000250"
FT REGION 2..59
FT /note="Minor non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 60..117
FT /note="Major non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 60..117
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT MOTIF 66..99
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 82..109
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
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 41
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 41
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 125
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
SQ SEQUENCE 618 AA; 70362 MW; B1F1F9D92212820D CRC64;
MADEGKSYNE HDDRVSFPQR RKKGRGPFRW KCGVGNRRSG RGGSGIRSSR FEEDDGDVAM
NDPQDGPRVR FNPYTTRPNR RRDTWHDRDR IHVTVRRDRA PQERGGAGTS QDGTTKNWFK
ITIPYGKKYD KMWLLSMIQS KCSVPFNPIE FHYENTRAHF FVENATTASA LKAVNYKIQD
RENGRISIII NSSAPPYIVQ NELKPEQVEQ LKLIMSKRYD GSQQALDLKG LRSDPDLVAQ
NIDVVLNRRG CMAAALRIIE ENIPELLSLN LSNNRLYKLD DMSSIVQKAP NLKILNLSGN
ELKSEWELDK IKGLKLEELW LDRNPMCDTF LDQSTYISTI RERFPKLLRL DGHELPPPIA
FDVEAPTMLP PCKGSYFGTE NLKSLVLHFL QQYYAIYDSG DRQGLLDAYH DGACCSLSTP
SNPQNPVRHN LAKYFNDSRN VKKIKDTTTR FRLLKHTRLN VVAFLNELPK THHDVNSFVV
DISAQTSTLL CFSVNGVFKE VDGKSRDSLR AFTRTFIAVP ASNSGLCIVN DELFVRNASP
EEIQRAFAMP APTPSSSPVP TLSQEQQDML QAFSTQSGMN LEWSQKCLQD NNWDYTRSAQ
AFTHLKAKGE IPEVAFMK
