SPN1_MOUSE
ID SPN1_MOUSE Reviewed; 358 AA.
AC Q80W37;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Snurportin-1;
DE AltName: Full=RNA U transporter 1;
GN Name=Snupn; Synonyms=Rnut1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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).
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:0000250|UniProtKB:O95149}.
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:0000250|UniProtKB:O95149}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95149}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95149}. Note=Nucleoplasmic shuttling protein.
CC Its nuclear import involves the nucleocytoplasmic transport receptor
CC importin beta. It is re-exported to the cytoplasm by the XPO1-dependent
CC nuclear export receptor pathway. {ECO:0000250|UniProtKB:O95149}.
CC -!- SIMILARITY: Belongs to the snurportin family. {ECO:0000305}.
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DR EMBL; AK155315; BAE33185.1; -; mRNA.
DR EMBL; BC049638; AAH49638.1; -; mRNA.
DR EMBL; BC061258; AAH61258.1; -; mRNA.
DR CCDS; CCDS23214.1; -.
DR RefSeq; NP_848461.1; NM_178374.3.
DR RefSeq; XP_011241086.1; XM_011242784.2.
DR AlphaFoldDB; Q80W37; -.
DR SMR; Q80W37; -.
DR BioGRID; 211191; 3.
DR ComplexPortal; CPX-1111; Importin complex, Snurportin variant.
DR STRING; 10090.ENSMUSP00000067200; -.
DR iPTMnet; Q80W37; -.
DR PhosphoSitePlus; Q80W37; -.
DR EPD; Q80W37; -.
DR MaxQB; Q80W37; -.
DR PaxDb; Q80W37; -.
DR PeptideAtlas; Q80W37; -.
DR PRIDE; Q80W37; -.
DR ProteomicsDB; 258726; -.
DR Antibodypedia; 27339; 195 antibodies from 25 providers.
DR DNASU; 66069; -.
DR Ensembl; ENSMUST00000068856; ENSMUSP00000067200; ENSMUSG00000055334.
DR GeneID; 66069; -.
DR KEGG; mmu:66069; -.
DR UCSC; uc009ptr.1; mouse.
DR CTD; 10073; -.
DR MGI; MGI:1913319; Snupn.
DR VEuPathDB; HostDB:ENSMUSG00000055334; -.
DR eggNOG; KOG3132; Eukaryota.
DR GeneTree; ENSGT00510000047494; -.
DR HOGENOM; CLU_056809_0_0_1; -.
DR InParanoid; Q80W37; -.
DR OMA; KRSQEGM; -.
DR OrthoDB; 1342398at2759; -.
DR PhylomeDB; Q80W37; -.
DR TreeFam; TF313108; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 66069; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Snupn; mouse.
DR PRO; PR:Q80W37; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80W37; protein.
DR Bgee; ENSMUSG00000055334; Expressed in cleaving embryo and 226 other tissues.
DR Genevisible; Q80W37; MM.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR GO; GO:0006404; P:RNA import into nucleus; ISO:MGI.
DR GO; GO:0061015; P:snRNA import into nucleus; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport.
FT CHAIN 1..358
FT /note="Snurportin-1"
FT /id="PRO_0000191072"
FT DOMAIN 11..73
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REGION 1..160
FT /note="Necessary for interaction with XPO1"
FT /evidence="ECO:0000250|UniProtKB:O95149"
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:0000250|UniProtKB:O95149"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..130
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT REGION 210..329
FT /note="Necessary for binding to the m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT REGION 315..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 106
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT SITE 145
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT SITE 278
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95149"
SQ SEQUENCE 358 AA; 41032 MW; 6750602E83C69155 CRC64;
MEELSQALAS SFSVSQELNS TAAPHPRLCQ YKSKYSSLEQ SERRRQLLEL QKSKRLDYVN
HARRLAEDDW TGMESGEEEN KKDEEEMDID PSKKLPKRYA NQLMLSEWLI DVPSDLGQEW
IVVVCPVGKR ALIVASRGST SAYTKSGYCV NRFSSLLPGG NRRNSTTAKD YTILDCIYSE
VNQTYYVLDV MCWRGHPFYD CQTDFRFYWM HSKLPEEEGL GEKTKINPFK FVGLKNFPCT
PESLCEVLSM DFPFEVDGLL FYHKQTHYSP GSTPLVGWLR PYMVSDILGV AVPAGPLTTK
PEYAGHQLQQ IIEHKRSQED TKEKLTHKAS ENGHYELEHL STPKLRNPPH SSESLMDN
