ID   NXF1_COTJA              Reviewed;         616 AA.
AC   P58797;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
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;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLN-246.
RX   PubMed=11358864; DOI=10.1101/gad.888201;
RA   Coburn G.A., Wiegand H.L., Kang Y., Ho D.N., Georgiadis M.M., Cullen B.R.;
RT   "Using viral species specificity to define a critical protein/RNA
RT   interaction surface.";
RL   Genes Dev. 15:1194-1205(2001).
CC   -!- FUNCTION: Involved in the nuclear export of mRNA from the nucleus to
CC       the cytoplasm.
CC   -!- SUBUNIT: Heterodimer with NXT1. The formation of NXF1/NXT1 heterodimers
CC       is required for the NXF1-mediated nuclear mRNA export. Part of the exon
CC       junction complex (By similarity). {ECO:0000250}.
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   -!- DOMAIN: The leucine-rich repeats and the NTF2-domain are essential for
CC       the export of mRNA from the nucleus. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Changing a single residue, Gln-246 to Arg, the residue
CC       found in human NXF1, fully rescues both constitutive transport element
CC       (CTE) function and CTE binding.
CC   -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
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DR   EMBL; AF343749; AAK58910.1; -; mRNA.
DR   AlphaFoldDB; P58797; -.
DR   SMR; P58797; -.
DR   PRIDE; P58797; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
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   1: Evidence at protein level;
KW   Cytoplasm; Leucine-rich repeat; mRNA transport; Nucleus;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..616
FT                   /note="Nuclear RNA export factor 1"
FT                   /id="PRO_0000220532"
FT   DOMAIN          116..195
FT                   /note="RRM"
FT   REPEAT          263..288
FT                   /note="LRR 1"
FT   REPEAT          289..312
FT                   /note="LRR 2"
FT   REPEAT          313..340
FT                   /note="LRR 3"
FT   REPEAT          341..368
FT                   /note="LRR 4"
FT   DOMAIN          383..533
FT                   /note="NTF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT   DOMAIN          562..616
FT                   /note="TAP-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         246
FT                   /note="Q->R: Rescues CTE function and binding."
FT                   /evidence="ECO:0000269|PubMed:11358864"
SQ   SEQUENCE   616 AA;  69330 MW;  D14903DDCF1BF1BD CRC64;
     MAEEGKGGYS EHDDRVVGRG FSGRRKKGRG PFRGKMYSEM NRNSRNRGGT GPSSSRQRQD
     EDDGDVAMSD AHDAPRGRYL PYGPRPSRAP HLTVRRDLPP PDRSGGGSRD GGRRNWFKIT
     IPYGKKYDKT WLLSSIQNLC SVPFTPVEFH YDHNRAQFYV EDATTASALK QVSRKITDRD
     NYKVVIIINS SAPPPSLQNE LKPEEIEQLK VCMSKRYDGA QRALDLKGLR VDPDLVSQSI
     DVVLNQRSCM MVVLRIIEEN IPELQSLNLS SNKLYRLDDL AELAIKAAGL KVLDLSRNEL
     KSERELDKVK GLKLEELWLD GNPLCDGFRD QSSYISSVRE RFPKLLRLDG HELPPPIAFD
     VEAPVTLPPC KGSYFGSDDL KVLVLRFLQQ YYSIYDSSDR QGLLDAYHDG ACCSLSIPFG
     PQNPPRNTLN EYFKDSRNVK KLKDPTMRFK LLKHTRLNVV AFLNELPRTQ HDVSSFVVDV
     CAQTNTLLCF AVHGIFKEVD GKSRDSVRAF TRMFIAVPAG NTGLCIVNDK LFVRNATADE
     LRKAFVMPAP TPSSSPVPSL AAEQQEMLAA FAMQSGMNLE WSQKCLQDND WDYGRAGQVF
     TQLKLEGKIP EVAFLK