NTF2_RAT
ID NTF2_RAT Reviewed; 127 AA.
AC P61972; P13662;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Nuclear transport factor 2 {ECO:0000305};
DE Short=NTF-2;
GN Name=Nutf2 {ECO:0000312|RGD:1359213};
GN Synonyms=Ntf2 {ECO:0000303|PubMed:8812990};
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 [GENOMIC DNA], AND CRYSTALLIZATION.
RC TISSUE=Kidney;
RX PubMed=8812990; DOI=10.1006/jsbi.1996.0049;
RA Kent H.M., Clarkson W.D., Bullock T.L., Stewart M.;
RT "Crystallization and preliminary X-ray diffraction analysis of nuclear
RT transport factor 2.";
RL J. Struct. Biol. 116:326-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH NUP54; NUP58 AND NUP62.
RC TISSUE=Macrophage;
RX PubMed=8707840; DOI=10.1083/jcb.134.3.589;
RA Hu T., Guan T., Gerace L.;
RT "Molecular and functional characterization of the p62 complex, an assembly
RT of nuclear pore complex glycoproteins.";
RL J. Cell Biol. 134:589-601(1996).
RN [4]
RP FUNCTION, INTERACTION WITH RAN, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-42.
RX PubMed=9822603; DOI=10.1093/emboj/17.22.6587;
RA Ribbeck K., Lipowsky G., Kent H.M., Stewart M., Goerlich D.;
RT "NTF2 mediates nuclear import of Ran.";
RL EMBO J. 17:6587-6598(1998).
RN [5]
RP MUTAGENESIS OF TYR-19; ASP-23 AND GLU-42.
RX PubMed=11038179; DOI=10.1083/jcb.151.2.321;
RA Lane C.M., Cushman I., Moore M.S.;
RT "Selective disruption of nuclear import by a functional mutant nuclear
RT transport carrier.";
RL J. Cell Biol. 151:321-332(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION, AND INTERACTION
RP WITH RAN.
RX PubMed=8757804; DOI=10.1006/jmbi.1996.0411;
RA Bullock T.L., Clarkson W.D., Kent H.M., Stewart M.;
RT "The 1.6-A resolution crystal structure of nuclear transport factor 2
RT (NTF2).";
RL J. Mol. Biol. 260:422-431(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS LYS-42 AND ALA-66,
RP INTERACTION WITH RAN AND NUCLEOPORINS, AND MUTAGENESIS OF ASP-23; GLU-42;
RP HIS-66; 92-ASP--ASP-94; ASP-117; HIS-124 AND PHE-126.
RX PubMed=9368653; DOI=10.1006/jmbi.1997.1255;
RA Clarkson W.D., Corbett A.H., Paschal B.M., Kent H.M., McCoy A.J.,
RA Gerace L., Silver P.A., Stewart M.;
RT "Nuclear protein import is decreased by engineered mutants of nuclear
RT transport factor 2 (NTF2) that do not bind GDP-Ran.";
RL J. Mol. Biol. 272:716-730(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP-BOUND RAN, AND
RP HOMODIMERIZATION.
RX PubMed=9533885; DOI=10.1006/jmbi.1997.1602;
RA Stewart M., Kent H.M., McCoy A.J.;
RT "Structural basis for molecular recognition between nuclear transport
RT factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran.";
RL J. Mol. Biol. 277:635-646(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-127 OF MUTANT ALA-7, FUNCTION,
RP INTERACTION WITH NUCLEOPORINS AND GDP-BOUND RAN, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TRP-7.
RX PubMed=10543952; DOI=10.1006/jmbi.1999.3166;
RA Bayliss R., Ribbeck K., Akin D., Kent H.M., Feldherr C.M., Gorlich D.,
RA Stewart M.;
RT "Interaction between NTF2 and xFxFG-containing nucleoporins is required to
RT mediate nuclear import of RanGDP.";
RL J. Mol. Biol. 293:579-593(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANTS GLU-84; GLU-102 AND
RP GLU-118, INTERACTION WITH NUCLEOPORINS AND GDP-BOUND RAN, SUBCELLULAR
RP LOCATION, HOMODIMERIZATION, AND MUTAGENESIS OF MET-84; MET-102 AND MET-118.
RX PubMed=11846560; DOI=10.1006/jmbi.2001.5136;
RA Chaillan-Huntington C., Butler P.J., Huntington J.A., Akin D., Feldherr C.,
RA Stewart M.;
RT "NTF2 monomer-dimer equilibrium.";
RL J. Mol. Biol. 314:465-477(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT ALA-23, INTERACTION WITH
RP NUCLEOPORINS AND GDP-BOUND RAN, SUBCELLULAR LOCATION, HOMODIMERIZATION, AND
RP MUTAGENESIS OF ASP-23 AND ILE-64.
RX PubMed=15522285; DOI=10.1016/j.jmb.2004.09.043;
RA Cushman I., Bowman B.R., Sowa M.E., Lichtarge O., Quiocho F.A., Moore M.S.;
RT "Computational and biochemical identification of a nuclear pore complex
RT binding site on the nuclear transport carrier NTF2.";
RL J. Mol. Biol. 344:303-310(2004).
CC -!- FUNCTION: Mediates the import of GDP-bound RAN from the cytoplasm into
CC the nucleus which is essential for the function of RAN in cargo
CC receptor-mediated nucleocytoplasmic transport. Thereby, plays
CC indirectly a more general role in cargo receptor-mediated
CC nucleocytoplasmic transport. Interacts with GDP-bound RAN in the
CC cytosol, recruits it to the nuclear pore complex via its interaction
CC with nucleoporins and promotes its nuclear import.
CC {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:9822603}.
CC -!- SUBUNIT: Homodimer (PubMed:8757804, PubMed:9533885, PubMed:11846560,
CC PubMed:15522285). Interacts with RAN (GDP-bound form); the interaction
CC is direct and regulates RAN nuclear import (PubMed:9822603,
CC PubMed:8757804, PubMed:9368653, PubMed:9533885, PubMed:11846560,
CC PubMed:15522285). Interacts with the nucleoporins NUP54, NUP58 and
CC NUP62 (via FG repeats); recruits NUTF2 to the nuclear pore complex a
CC step required for NUTF2-mediated GDP-bound RAN nuclear import
CC (PubMed:8707840, PubMed:9368653, PubMed:10543952, PubMed:11846560,
CC PubMed:15522285). Interacts with CAPG; mediates its nuclear import (By
CC similarity). {ECO:0000250|UniProtKB:P61970,
CC ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560,
CC ECO:0000269|PubMed:15522285, ECO:0000269|PubMed:8707840,
CC ECO:0000269|PubMed:8757804, ECO:0000269|PubMed:9368653,
CC ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9822603}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9822603}.
CC Nucleus outer membrane {ECO:0000269|PubMed:10543952,
CC ECO:0000269|PubMed:11846560, ECO:0000269|PubMed:15522285,
CC ECO:0000269|PubMed:9822603}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560,
CC ECO:0000269|PubMed:15522285}. Nucleus inner membrane
CC {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is
CC essentially nucleoplasmic, enriched in nucleoplasmic foci.
CC {ECO:0000250|UniProtKB:P61970}.
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DR EMBL; X91651; CAA62839.1; -; Genomic_DNA.
DR EMBL; BC061569; AAH61569.1; -; mRNA.
DR RefSeq; NP_001007630.1; NM_001007629.1.
DR RefSeq; XP_006255542.1; XM_006255480.3.
DR PDB; 1A2K; X-ray; 2.50 A; A/B=1-127.
DR PDB; 1AR0; X-ray; 2.30 A; A/B=1-127.
DR PDB; 1ASK; X-ray; 2.30 A; A/B=1-127.
DR PDB; 1GY6; X-ray; 1.60 A; A/B=1-127.
DR PDB; 1JB2; X-ray; 2.00 A; A/B=1-127.
DR PDB; 1JB4; X-ray; 2.23 A; A/B=1-127.
DR PDB; 1JB5; X-ray; 2.30 A; A/B=1-127.
DR PDB; 1OUN; X-ray; 2.30 A; A/B=1-127.
DR PDB; 1QMA; X-ray; 2.50 A; A/B/C/D=2-127.
DR PDB; 1U5O; X-ray; 2.50 A; A/B=1-127.
DR PDB; 5BXQ; X-ray; 2.50 A; A/B=1-127.
DR PDBsum; 1A2K; -.
DR PDBsum; 1AR0; -.
DR PDBsum; 1ASK; -.
DR PDBsum; 1GY6; -.
DR PDBsum; 1JB2; -.
DR PDBsum; 1JB4; -.
DR PDBsum; 1JB5; -.
DR PDBsum; 1OUN; -.
DR PDBsum; 1QMA; -.
DR PDBsum; 1U5O; -.
DR PDBsum; 5BXQ; -.
DR AlphaFoldDB; P61972; -.
DR BMRB; P61972; -.
DR SMR; P61972; -.
DR BioGRID; 253720; 5.
DR IntAct; P61972; 1.
DR STRING; 10116.ENSRNOP00000025608; -.
DR iPTMnet; P61972; -.
DR PhosphoSitePlus; P61972; -.
DR SwissPalm; P61972; -.
DR jPOST; P61972; -.
DR PaxDb; P61972; -.
DR PRIDE; P61972; -.
DR Ensembl; ENSRNOT00000101055; ENSRNOP00000080316; ENSRNOG00000018945.
DR GeneID; 291981; -.
DR KEGG; rno:291981; -.
DR UCSC; RGD:1359213; rat.
DR CTD; 10204; -.
DR RGD; 1359213; Nutf2.
DR eggNOG; KOG2104; Eukaryota.
DR GeneTree; ENSGT00510000047030; -.
DR HOGENOM; CLU_131642_1_1_1; -.
DR InParanoid; P61972; -.
DR OMA; FTEFYYN; -.
DR OrthoDB; 1437819at2759; -.
DR PhylomeDB; P61972; -.
DR TreeFam; TF314422; -.
DR EvolutionaryTrace; P61972; -.
DR PRO; PR:P61972; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000018945; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; P61972; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904046; P:negative regulation of vascular endothelial growth factor production; IMP:RGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0006611; P:protein export from nucleus; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0090204; P:protein localization to nuclear pore; IMP:UniProtKB.
DR CDD; cd00780; NTF2; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR045875; NTF2/Mtr2.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR PANTHER; PTHR12612; PTHR12612; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..127
FT /note="Nuclear transport factor 2"
FT /id="PRO_0000194777"
FT DOMAIN 10..121
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61970"
FT MUTAGEN 7
FT /note="W->A: No effect on interaction with GDP-bound RAN.
FT Decreased interaction with nucleoporins. Decreased
FT localization to the nuclear pore complex. Decreased GDP-
FT bound RAN and other proteins nuclear import."
FT /evidence="ECO:0000269|PubMed:10543952"
FT MUTAGEN 19
FT /note="Y->A: Loss of interaction with GDP-bound RAN. Loss
FT of GDP-bound RAN nuclear import."
FT /evidence="ECO:0000269|PubMed:11038179"
FT MUTAGEN 23
FT /note="D->A,N: No effect on interaction with GDP-bound RAN.
FT Increases GDP-bound RAN nuclear import. Increased
FT interaction with nucleoporins and localization to the
FT nuclear pore complex. Inhibits the nuclear import of
FT nuclear localization signal-containing proteins."
FT /evidence="ECO:0000269|PubMed:11038179,
FT ECO:0000269|PubMed:15522285"
FT MUTAGEN 23
FT /note="D->N: No effect on interaction with GDP-bound RAN.
FT No effect on interaction with nucleoporins. No effect on
FT proteins nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT MUTAGEN 42
FT /note="E->D: Loss of interaction with GDP-bound RAN. Loss
FT of GDP-bound RAN nuclear import."
FT /evidence="ECO:0000269|PubMed:11038179"
FT MUTAGEN 42
FT /note="E->K: Loss of interaction with GDP-bound RAN. No
FT effect on interaction with nucleoporins. Loss of GDP-bound
FT RAN and other proteins nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653,
FT ECO:0000269|PubMed:9822603"
FT MUTAGEN 64
FT /note="I->A: No effect on homodimerization. Decreased
FT interaction with GDP-bound RAN. Loss of interaction with
FT nucleoporins and localization to the nuclear pore complex."
FT /evidence="ECO:0000269|PubMed:15522285"
FT MUTAGEN 64
FT /note="I->Q: No effect on homodimerization. Loss of
FT interaction with GDP-bound RAN. Decreased interaction with
FT nucleoporins and localization to the nuclear pore complex."
FT /evidence="ECO:0000269|PubMed:15522285"
FT MUTAGEN 66
FT /note="H->A: Loss of interaction with GDP-bound RAN. No
FT effect on interaction with nucleoporins. Decreased proteins
FT nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT MUTAGEN 84
FT /note="M->E: Decreased homodimerization."
FT /evidence="ECO:0000269|PubMed:11846560"
FT MUTAGEN 92..94
FT /note="DED->NEN: Loss of interaction with GDP-bound RAN. No
FT effect on interaction with nucleoporins. Loss of proteins
FT nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT MUTAGEN 102
FT /note="M->E: Decreased homodimerization."
FT /evidence="ECO:0000269|PubMed:11846560"
FT MUTAGEN 117
FT /note="D->N: Decreased interaction with GDP-bound RAN. No
FT effect on interaction with nucleoporins. No effect on
FT proteins nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT MUTAGEN 118
FT /note="M->E: Loss of homodimerization. Decreased
FT interaction with GDP-bound RAN. Decreased interaction with
FT nucleoporins. Decreased localization to the nuclear pore
FT complex."
FT /evidence="ECO:0000269|PubMed:11846560"
FT MUTAGEN 124
FT /note="Missing: Loss of interaction with GDP-bound RAN. No
FT effect on interaction with nucleoporins. Decreased proteins
FT nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT MUTAGEN 126
FT /note="Missing: Decreased interaction with GDP-bound RAN.
FT No effect on interaction with nucleoporins. No effect on
FT proteins nuclear import."
FT /evidence="ECO:0000269|PubMed:9368653"
FT HELIX 6..25
FT /evidence="ECO:0007829|PDB:1GY6"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1GY6"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 64..75
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:1GY6"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:1GY6"
SQ SEQUENCE 127 AA; 14478 MW; 817752F20E262FD3 CRC64;
MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP
FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR
LALHNFG
