SPN1_HUMAN
ID SPN1_HUMAN Reviewed; 360 AA.
AC O95149; A6NE34; A8K0B0; D3DW76;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Snurportin-1;
DE AltName: Full=RNA U transporter 1;
GN Name=SNUPN; Synonyms=RNUT1, SPN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-52; 54-69; 128-144;
RP 211-221 AND 323-327, FUNCTION IN U SNRNP NUCLEAR IMPORT, INTERACTION WITH
RP KPNB1, RNA-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9670026; DOI=10.1093/emboj/17.14.4114;
RA Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M.,
RA Luehrmann R.;
RT "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel
RT domain structure.";
RL EMBO J. 17:4114-4126(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [6]
RP FUNCTION, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, INTERACTION
RP WITH IPO7; KPNB1 AND XPO1, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH
RP XPO1 AND RAN, AND SUBCELLULAR LOCATION.
RX PubMed=10209022; DOI=10.1083/jcb.145.2.255;
RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
RA Hartmann E., Luehrmann R., Goerlich D.;
RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
RL J. Cell Biol. 145:255-264(1999).
RN [7]
RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX, INTERACTION WITH DDX20; SMN1 AND
RP SNRPB, AND SUBCELLULAR LOCATION.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex
RT with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [8]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-27; TRP-107; 203-PHE--TRP-207 AND
RP TRP-276, AND RNA-BINDING.
RX PubMed=16030253; DOI=10.1091/mbc.e05-04-0316;
RA Ospina J.K., Gonsalvez G.B., Bednenko J., Darzynkiewicz E., Gerace L.,
RA Matera A.G.;
RT "Cross-talk between snurportin1 subdomains.";
RL Mol. Biol. Cell 16:4660-4671(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 97-300 IN COMPLEX WITH M3G-CAP,
RP MUTAGENESIS OF TRP-107 AND TRP-276, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15920472; DOI=10.1038/sj.emboj.7600701;
RA Strasser A., Dickmanns A., Luehrmann R., Ficner R.;
RT "Structural basis for m3G-cap-mediated nuclear import of spliceosomal
RT UsnRNPs by snurportin1.";
RL EMBO J. 24:2235-2243(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-64 IN COMPLEX WITH KPNB1, AND
RP INTERACTION WITH KPNB1.
RX PubMed=18187419; DOI=10.1074/jbc.m709093200;
RA Mitrousis G., Olia A.S., Walker-Kopp N., Cingolani G.;
RT "Molecular basis for the recognition of snurportin 1 by importin beta.";
RL J. Biol. Chem. 283:7877-7884(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 25-64 IN COMPLEX WITH KPNB1, AND
RP INTERACTION WITH KPNB1.
RX PubMed=20476751; DOI=10.1021/bi100292y;
RA Bhardwaj A., Cingolani G.;
RT "Conformational selection in the recognition of the snurportin importin
RT beta binding domain by importin beta.";
RL Biochemistry 49:5042-5047(2010).
CC -!- FUNCTION: Functions as an U snRNP-specific nuclear import adapter.
CC Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import
CC of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs.
CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472,
CC ECO:0000269|PubMed:16030253, ECO:0000269|PubMed:9670026}.
CC -!- SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN,
CC SMN1 and ZNF259. Component of a nuclear export receptor complex
CC composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export
CC complex with SNUPN, Ran and XPO1. Interacts (via IBB domain) with
CC KPNB1; the interaction is direct. Interacts with DDX20, IPO7, SMN1,
CC SNRPB and XPO1. Interacts directly with XPO1. Its interaction with XPO1
CC and binding to m3G-cap U snRNPs appears to be mutually exclusive.
CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:12095920,
CC ECO:0000269|PubMed:15920472, ECO:0000269|PubMed:16030253,
CC ECO:0000269|PubMed:18187419, ECO:0000269|PubMed:20476751,
CC ECO:0000269|PubMed:9670026}.
CC -!- INTERACTION:
CC O95149; O14980: XPO1; NbExp=8; IntAct=EBI-714033, EBI-355867;
CC O95149; Q6P5F9: Xpo1; Xeno; NbExp=2; IntAct=EBI-714033, EBI-2550236;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10209022,
CC ECO:0000269|PubMed:15920472}. Cytoplasm {ECO:0000269|PubMed:12095920,
CC ECO:0000269|PubMed:9670026, ECO:0000305|PubMed:10209022}.
CC Note=Nucleoplasmic shuttling protein. Its nuclear import involves the
CC nucleocytoplasmic transport receptor importin beta (PubMed:10209022,
CC PubMed:12095920). It is re-exported to the cytoplasm by the XPO1-
CC dependent nuclear export receptor pathway (PubMed:10209022).
CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:12095920}.
CC -!- SIMILARITY: Belongs to the snurportin family. {ECO:0000305}.
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DR EMBL; AF039029; AAC70906.1; -; mRNA.
DR EMBL; CR456811; CAG33092.1; -; mRNA.
DR EMBL; AK289475; BAF82164.1; -; mRNA.
DR EMBL; CH471136; EAW99245.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99246.1; -; Genomic_DNA.
DR EMBL; BC004203; AAH04203.1; -; mRNA.
DR CCDS; CCDS10281.1; -.
DR RefSeq; NP_001036046.1; NM_001042581.1.
DR RefSeq; NP_001036053.1; NM_001042588.1.
DR RefSeq; NP_005692.1; NM_005701.3.
DR PDB; 1XK5; X-ray; 2.40 A; A=97-300.
DR PDB; 2P8Q; X-ray; 2.35 A; B=25-64.
DR PDB; 2Q5D; X-ray; 3.20 A; C/D=25-64.
DR PDB; 2QNA; X-ray; 2.84 A; B=1-66.
DR PDB; 3GB8; X-ray; 2.90 A; B=1-328.
DR PDB; 3GJX; X-ray; 2.50 A; B/E=1-360.
DR PDB; 3LWW; X-ray; 3.15 A; B/D=25-64.
DR PDB; 3NBY; X-ray; 3.42 A; B/E=15-360.
DR PDB; 3NBZ; X-ray; 2.80 A; B/E=15-360.
DR PDB; 3NC0; X-ray; 2.90 A; B/E=15-360.
DR PDB; 5DIS; X-ray; 2.85 A; C=1-287.
DR PDBsum; 1XK5; -.
DR PDBsum; 2P8Q; -.
DR PDBsum; 2Q5D; -.
DR PDBsum; 2QNA; -.
DR PDBsum; 3GB8; -.
DR PDBsum; 3GJX; -.
DR PDBsum; 3LWW; -.
DR PDBsum; 3NBY; -.
DR PDBsum; 3NBZ; -.
DR PDBsum; 3NC0; -.
DR PDBsum; 5DIS; -.
DR AlphaFoldDB; O95149; -.
DR SASBDB; O95149; -.
DR SMR; O95149; -.
DR BioGRID; 115384; 39.
DR ComplexPortal; CPX-1032; Importin complex, Snurportin variant.
DR CORUM; O95149; -.
DR DIP; DIP-48513N; -.
DR ELM; O95149; -.
DR IntAct; O95149; 26.
DR MINT; O95149; -.
DR STRING; 9606.ENSP00000454852; -.
DR ChEMBL; CHEMBL3885569; -.
DR GlyGen; O95149; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95149; -.
DR PhosphoSitePlus; O95149; -.
DR BioMuta; SNUPN; -.
DR EPD; O95149; -.
DR jPOST; O95149; -.
DR MassIVE; O95149; -.
DR MaxQB; O95149; -.
DR PaxDb; O95149; -.
DR PeptideAtlas; O95149; -.
DR PRIDE; O95149; -.
DR ProteomicsDB; 50662; -.
DR Antibodypedia; 27339; 195 antibodies from 25 providers.
DR DNASU; 10073; -.
DR Ensembl; ENST00000308588.10; ENSP00000309831.5; ENSG00000169371.14.
DR Ensembl; ENST00000564644.5; ENSP00000454852.1; ENSG00000169371.14.
DR Ensembl; ENST00000564675.5; ENSP00000458053.1; ENSG00000169371.14.
DR Ensembl; ENST00000567134.5; ENSP00000456224.1; ENSG00000169371.14.
DR GeneID; 10073; -.
DR KEGG; hsa:10073; -.
DR MANE-Select; ENST00000308588.10; ENSP00000309831.5; NM_005701.4; NP_005692.1.
DR UCSC; uc002ban.4; human.
DR CTD; 10073; -.
DR DisGeNET; 10073; -.
DR GeneCards; SNUPN; -.
DR HGNC; HGNC:14245; SNUPN.
DR HPA; ENSG00000169371; Low tissue specificity.
DR MIM; 607902; gene.
DR neXtProt; NX_O95149; -.
DR OpenTargets; ENSG00000169371; -.
DR PharmGKB; PA34611; -.
DR VEuPathDB; HostDB:ENSG00000169371; -.
DR eggNOG; KOG3132; Eukaryota.
DR GeneTree; ENSGT00510000047494; -.
DR HOGENOM; CLU_056809_0_0_1; -.
DR InParanoid; O95149; -.
DR OMA; KRSQEGM; -.
DR OrthoDB; 1342398at2759; -.
DR PhylomeDB; O95149; -.
DR TreeFam; TF313108; -.
DR PathwayCommons; O95149; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR SignaLink; O95149; -.
DR BioGRID-ORCS; 10073; 683 hits in 1091 CRISPR screens.
DR ChiTaRS; SNUPN; human.
DR EvolutionaryTrace; O95149; -.
DR GeneWiki; SNUPN; -.
DR GenomeRNAi; 10073; -.
DR Pharos; O95149; Tbio.
DR PRO; PR:O95149; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O95149; protein.
DR Bgee; ENSG00000169371; Expressed in left testis and 106 other tissues.
DR ExpressionAtlas; O95149; baseline and differential.
DR Genevisible; O95149; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:ComplexPortal.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro.
DR GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR GO; GO:0006404; P:RNA import into nucleus; IDA:ComplexPortal.
DR GO; GO:0061015; P:snRNA import into nucleus; IEA:InterPro.
DR DisProt; DP01874; -.
DR IDEAL; IID00115; -.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR017336; Snurportin-1.
DR InterPro; IPR024721; Snurportin-1_N.
DR PANTHER; PTHR13403; PTHR13403; 1.
DR Pfam; PF11538; Snurportin1; 1.
DR PIRSF; PIRSF037955; Snurportin-1; 1.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..360
FT /note="Snurportin-1"
FT /id="PRO_0000191071"
FT DOMAIN 11..73
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REGION 1..159
FT /note="Necessary for interaction with XPO1"
FT /evidence="ECO:0000269|PubMed:10209022"
FT REGION 1..65
FT /note="Necessary for interaction with KPNB1 and m3G-cap U1
FT and U5 snRNP import receptor activity"
FT /evidence="ECO:0000269|PubMed:18187419,
FT ECO:0000269|PubMed:9670026"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..129
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0007744|PDB:1XK5"
FT REGION 208..328
FT /note="Necessary for binding to the m3G-cap structure"
FT /evidence="ECO:0000269|PubMed:9670026"
FT REGION 339..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 105
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0007744|PDB:1XK5"
FT SITE 144
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0007744|PDB:1XK5"
FT SITE 276
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0007744|PDB:1XK5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 27
FT /note="R->A: Abolishes interaction with KPNB1 and m3G-cap
FT U1 snRNP import receptor activity."
FT /evidence="ECO:0000269|PubMed:16030253"
FT MUTAGEN 107
FT /note="W->A: Reduces binding to m3G-cap structure,
FT interaction with XPO1 and snRNP import receptor activity."
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0000269|PubMed:16030253"
FT MUTAGEN 203..207
FT /note="FRFYW->A: Reduces binding to m3G-cap structure."
FT /evidence="ECO:0000269|PubMed:16030253"
FT MUTAGEN 276
FT /note="W->A: Reduces binding to m3G-cap structure,
FT interaction with XPO1 and snRNP import receptor activity."
FT /evidence="ECO:0000269|PubMed:15920472,
FT ECO:0000269|PubMed:16030253"
FT HELIX 1..10
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3NBY"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:2P8Q"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2P8Q"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1XK5"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 119..135
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3NBY"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3NBZ"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1XK5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5DIS"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1XK5"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1XK5"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1XK5"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:1XK5"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1XK5"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:1XK5"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3NBZ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1XK5"
SQ SEQUENCE 360 AA; 41143 MW; 50B456D1C23B4BA1 CRC64;
MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN
HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI
VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN
QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE
SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD
YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS PDHPGCLMEN
