ID A0A2Y9R1Y1_TRIMA Unreviewed; 361 AA.
AC A0A2Y9R1Y1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Snurportin-1 {ECO:0000256|ARBA:ARBA00016034, ECO:0000256|PIRNR:PIRNR037955};
DE AltName: Full=RNA U transporter 1 {ECO:0000256|ARBA:ARBA00031454, ECO:0000256|PIRNR:PIRNR037955};
GN Name=LOC101340442 {ECO:0000313|RefSeq:XP_023585608.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023585608.1};
RN [1] {ECO:0000313|RefSeq:XP_023585608.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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DR RefSeq; XP_004374817.1; XM_004374760.1.
DR RefSeq; XP_023585608.1; XM_023729840.1.
DR AlphaFoldDB; A0A2Y9R1Y1; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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; IPR002652; Importin-a_IBB.
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.
DR PROSITE; PS51214; IBB; 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:UP000248480};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR037955};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037955}.
FT DOMAIN 11..73
FT /note="IBB"
FT /evidence="ECO:0000259|PROSITE:PS51214"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..361
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 COMPBIAS 316..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:0000256|PIRSR:PIRSR037955-1"
FT SITE 145
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000256|PIRSR:PIRSR037955-1"
FT SITE 278
FT /note="Interaction with m3G-cap structure"
FT /evidence="ECO:0000256|PIRSR:PIRSR037955-1"
SQ SEQUENCE 361 AA; 41226 MW; CFFC97F7E1B54E5A CRC64;
MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKTKRLDYVN
HARRLAEDDW TGMESDEDED KKDDEEMDID IGKKLPKRYA NQLMLSEWLI DVPSDLGQEW
IVVVCPVGKR ALIVASRGST SAYTKSGYCV NRFSSLLPGG NRRNSTTAKD YTILDCIYSE
VNQTYYVLDV MCWRGHPFYD CQTDFRFYWM HSKLPEEEGL GEKTKLNPFK FVGLKNFPCT
PESLCKVLSM DFPFEVDGLL FYHKQTHYSP GSTPLVGWLR PYMVSDVLGV AVPAGPLTTK
PEYAGHQLQQ IVAHKRSQRE GTKEITHKAS ENGHYELEHL STPKLKSPPR CPDHPGSLME
N
//
