ID G1Q2I2_MYOLU Unreviewed; 350 AA.
AC G1Q2I2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Snurportin-1 {ECO:0000256|ARBA:ARBA00016034, ECO:0000256|PIRNR:PIRNR037955};
DE AltName: Full=RNA U transporter 1 {ECO:0000256|PIRNR:PIRNR037955};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017915.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017915.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000017915.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003975, ECO:0000256|PIRNR:PIRNR037955}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037955}.
CC -!- SIMILARITY: Belongs to the snurportin family.
CC {ECO:0000256|ARBA:ARBA00007540, ECO:0000256|PIRNR:PIRNR037955}.
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; AAPE02039582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1Q2I2; -.
DR STRING; 59463.ENSMLUP00000017915; -.
DR Ensembl; ENSMLUT00000026795.1; ENSMLUP00000017915.1; ENSMLUG00000027485.1.
DR eggNOG; KOG3132; Eukaryota.
DR GeneTree; ENSGT00510000047494; -.
DR HOGENOM; CLU_056809_0_0_1; -.
DR InParanoid; G1Q2I2; -.
DR OMA; NIEHRHT; -.
DR TreeFam; TF313108; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0061015; P:snRNA import into nucleus; IEA:UniProtKB-UniRule.
DR CDD; cd09232; Snurportin-1_C; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR InterPro; IPR017336; Snurportin-1.
DR InterPro; IPR024721; Snurportin-1_N.
DR InterPro; IPR047857; Snurportin1_C.
DR PANTHER; PTHR13403:SF6; SNURPORTIN-1; 1.
DR PANTHER; PTHR13403; SNURPORTIN1 RNUT1 PROTEIN RNA, U TRANSPORTER 1; 1.
DR Pfam; PF11538; Snurportin1; 1.
DR PIRSF; PIRSF037955; Snurportin-1; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037955};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR037955};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037955}.
FT DOMAIN 29..52
FT /note="Snurportin-1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11538"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 93
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000256|PIRSR:PIRSR037955-1"
FT SITE 132
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000256|PIRSR:PIRSR037955-1"
FT SITE 265
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000256|PIRSR:PIRSR037955-1"
SQ SEQUENCE 350 AA; 39917 MW; D5EE308CCF0AFC99 CRC64;
MEELSQALAS SFSVSQDLNS TAAPHPRLSE RRQQLLEWQK FKRLDYVNHA RRLAEDDWTG
MESEEEDKKY DEEMGIDTGK KLPKLYANQL MLSEWLIEVP SDLGQEWIVV VCPVGKRALI
VASRGSTSAY TKSGYCVNKF SSLLPGGNKR NSTTAKDSTI LDCIYSEAKQ TYYILDVMCW
RGHPFYDCQT DFRFYWMHSK LSEEEGLGEN TKLNPFKFVG LKNFPCTPES LGKVLSMDFP
FEVDGLLFYH KQTHYSPGST PLVGWLRPYM VSDILGVAMP AGGPLTTKPE YAGHQLQQII
EHKRSQKEGM KEKPTHKAFD NGHYELEHLS TPELKSDPHN LDQLGSRMEN
//
