SPN1_BOVIN
ID SPN1_BOVIN Reviewed; 362 AA.
AC Q2TBK8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Snurportin-1;
DE AltName: Full=RNA U transporter 1;
GN Name=SNUPN; Synonyms=RNUT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; BC109999; AAI10000.1; -; mRNA.
DR RefSeq; NP_001033635.1; NM_001038546.2.
DR RefSeq; XP_005222006.1; XM_005221949.3.
DR RefSeq; XP_010815368.1; XM_010817066.2.
DR RefSeq; XP_010815369.1; XM_010817067.2.
DR AlphaFoldDB; Q2TBK8; -.
DR SMR; Q2TBK8; -.
DR STRING; 9913.ENSBTAP00000028371; -.
DR PaxDb; Q2TBK8; -.
DR PRIDE; Q2TBK8; -.
DR Ensembl; ENSBTAT00000028371; ENSBTAP00000028371; ENSBTAG00000021293.
DR Ensembl; ENSBTAT00000076267; ENSBTAP00000067932; ENSBTAG00000021293.
DR GeneID; 515588; -.
DR KEGG; bta:515588; -.
DR CTD; 10073; -.
DR VEuPathDB; HostDB:ENSBTAG00000021293; -.
DR VGNC; VGNC:35088; SNUPN.
DR eggNOG; KOG3132; Eukaryota.
DR GeneTree; ENSGT00510000047494; -.
DR HOGENOM; CLU_056809_0_0_1; -.
DR InParanoid; Q2TBK8; -.
DR OMA; KRSQEGM; -.
DR OrthoDB; 1342398at2759; -.
DR TreeFam; TF313108; -.
DR Reactome; R-BTA-191859; snRNP Assembly.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000021293; Expressed in spermatid and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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..362
FT /note="Snurportin-1"
FT /id="PRO_0000247291"
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..40
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..330
FT /note="Necessary for binding to the m3G-cap structure"
FT /evidence="ECO:0000250|UniProtKB:O95149"
FT REGION 319..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="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"
SQ SEQUENCE 362 AA; 41492 MW; 7797B2E57CFF8164 CRC64;
MEELSQALAG SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRQLLEL QKLKRLDYVN
HARRLAEDDW TGMESEEEEE KKDDEEMDVD TGKELPKRYA NQLMLSEWLI DVPSDLGQEW
IVVVCPVGKR SLIVASQGLT SAYTKSGYCV NTFPSLLPGG NRRNSTTEKD YTILDCIYSE
VNQTYYVLDV MCWRGHPFYD CQTDFRFYWL HSKLPEEEGL GEKTKRNPFK FVGLKNFPCT
PESLCKVLSM DFPFEVDGLL FYHKQTHYSP GSTPLVGWLR PYMVSDVLGV AVPACPLTTK
PEYAGYQLQQ IIEHKKSKKE GIMGKLTPRA SENGHYELEH LSTPKLKSPP QRPNHPESLM
EN
