TNPO3_MOUSE
ID TNPO3_MOUSE Reviewed; 923 AA.
AC Q6P2B1; Q7TSL6; Q8BKX4; Q8BP42;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Transportin-3 {ECO:0000305};
GN Name=Tnpo3 {ECO:0000312|MGI:MGI:1196412};
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] (ISOFORM 1).
RC TISSUE=Embryo, and Olfactory epithelium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 684-923 (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Importin, which transports target proteins into the nucleus.
CC Specifically mediates the nuclear import of splicing factor
CC serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by
CC recognizing phosphorylated SR domains. Also mediates the nuclear import
CC of serine/arginine (SR) protein CPSF6, independently of CPSF6
CC phosphorylation. The nuclear import process is regulated by the small
CC GTPase Ran that partitions between cytoplasm and nucleus in the
CC predominantly GDP- and GTP-bound form, respectively. Importin
CC associates with target cargo proteins in the cytoplasm, and the
CC competitive binding of GTP-bound Ran induces the release of cargos in
CC the nucleus. {ECO:0000250|UniProtKB:Q9Y5L0}.
CC -!- SUBUNIT: Interacts with (GTP-bound) Ran. Interacts with
CC (phosphorylated) SFRS1 and SFRS2; leading to their nuclear import.
CC Interacts with NUP62. Interacts with RBM4. Interacts with CPSF6,
CC promoting its nuclear import. {ECO:0000250|UniProtKB:Q9Y5L0}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q9Y5L0}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9Y5L0}. Note=Localizes to the nuclear
CC envelope and annulate lamellae, which consists in stacks of endoplasmic
CC reticulum membranes containing a high density of nuclear pores.
CC {ECO:0000250|UniProtKB:Q9Y5L0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P2B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2B1-2; Sequence=VSP_011179;
CC Name=3;
CC IsoId=Q6P2B1-3; Sequence=VSP_019595, VSP_019596;
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; AK049446; BAC33754.1; -; mRNA.
DR EMBL; AK077714; BAC36974.1; -; mRNA.
DR EMBL; BC052756; AAH52756.1; -; mRNA.
DR EMBL; BC064646; AAH64646.1; -; mRNA.
DR CCDS; CCDS19963.1; -. [Q6P2B1-1]
DR CCDS; CCDS85023.1; -. [Q6P2B1-2]
DR RefSeq; NP_001334008.1; NM_001347079.1. [Q6P2B1-2]
DR RefSeq; NP_796270.2; NM_177296.4. [Q6P2B1-1]
DR AlphaFoldDB; Q6P2B1; -.
DR SMR; Q6P2B1; -.
DR BioGRID; 236407; 6.
DR IntAct; Q6P2B1; 1.
DR MINT; Q6P2B1; -.
DR STRING; 10090.ENSMUSP00000012679; -.
DR iPTMnet; Q6P2B1; -.
DR PhosphoSitePlus; Q6P2B1; -.
DR SwissPalm; Q6P2B1; -.
DR EPD; Q6P2B1; -.
DR jPOST; Q6P2B1; -.
DR MaxQB; Q6P2B1; -.
DR PaxDb; Q6P2B1; -.
DR PeptideAtlas; Q6P2B1; -.
DR PRIDE; Q6P2B1; -.
DR ProteomicsDB; 259284; -. [Q6P2B1-1]
DR ProteomicsDB; 259285; -. [Q6P2B1-2]
DR ProteomicsDB; 259286; -. [Q6P2B1-3]
DR Antibodypedia; 17836; 152 antibodies from 30 providers.
DR DNASU; 320938; -.
DR Ensembl; ENSMUST00000012679; ENSMUSP00000012679; ENSMUSG00000012535. [Q6P2B1-1]
DR Ensembl; ENSMUST00000115251; ENSMUSP00000110906; ENSMUSG00000012535. [Q6P2B1-2]
DR GeneID; 320938; -.
DR KEGG; mmu:320938; -.
DR UCSC; uc009bdy.1; mouse. [Q6P2B1-1]
DR UCSC; uc009bea.1; mouse. [Q6P2B1-3]
DR CTD; 23534; -.
DR MGI; MGI:1196412; Tnpo3.
DR VEuPathDB; HostDB:ENSMUSG00000012535; -.
DR eggNOG; KOG2081; Eukaryota.
DR GeneTree; ENSGT00530000063347; -.
DR HOGENOM; CLU_005996_0_2_1; -.
DR InParanoid; Q6P2B1; -.
DR OMA; KTINYCR; -.
DR OrthoDB; 206228at2759; -.
DR PhylomeDB; Q6P2B1; -.
DR TreeFam; TF314539; -.
DR BioGRID-ORCS; 320938; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Tnpo3; mouse.
DR PRO; PR:Q6P2B1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6P2B1; protein.
DR Bgee; ENSMUSG00000012535; Expressed in floor plate of midbrain and 260 other tissues.
DR ExpressionAtlas; Q6P2B1; baseline and differential.
DR Genevisible; Q6P2B1; MM.
DR GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR Pfam; PF08389; Xpo1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..923
FT /note="Transportin-3"
FT /id="PRO_0000120782"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5L0"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5L0"
FT MOD_RES 896
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5L0"
FT VAR_SEQ 233..267
FT /note="QQDKTSSNLHEAASDCVCSALYAIENVETNLPLAM -> VSKAAPAIATFNN
FT QPSGTPQCFVGEKHFVCVLRLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019595"
FT VAR_SEQ 268..923
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019596"
FT VAR_SEQ 810
FT /note="D -> DLSVFLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011179"
FT MOD_RES Q6P2B1-3:242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
SQ SEQUENCE 923 AA; 104170 MW; B7D7D2E734A9491E CRC64;
MEGAKPTLQL VYQAVQALYH DPDPSGKERA SFWLGELQRS VHAWEISDQL LQIRQDVESC
YFAAQTMKMK IQTSFYELPT DSHASLRDSL LTHIQNLKDL SPVIVTQLAL AIADLALQMP
SWKGCVQTLV EKYSNDVTSL PFLLEILTVL PEEVHSRSLR IGANRRTEII EDLAFYSSTV
VSLLMTCVEK AGTDEKMLMK VFRCLGSWFN LGVLDSNFMA NNKLLALLFE VLQQDKTSSN
LHEAASDCVC SALYAIENVE TNLPLAMQLF QGVLTLETAY HMAVAREDLD KVLNYCRIFT
ELCETFLEKI VCTPGQGLGD LRTLELLLIC AGHPQYEVVE ISFNFWYRLG EHLYKTNDEV
IHSIFKAYIQ RLLHALARHC QLEPDHEGVP EETDDFGEFR MRVSDLVKDL IFLIGSMECF
AQLYSTLKEG NPPWEVTEAV LFIMAAIAKS VDPENNPTLV EVLEGVVHLP ETVHTAVRYT
SIELVGEMSE VVDRNPQFLD PVLGYLMKGL CEKPLASAAA KAIHNICSVC RDHMAQHFNG
LLEIAHSLDS FMLSPEAAVG LLKGTALVLA RLPLDKITEC LSELCSVQVM ALKKLLSQEP
SNGISSDPTV FLDRLAVIFR HTNPIVENGQ THPCQKVIQE IWPVLSETLN KHRADNRIVE
RCCRCLRFAV RCVGKGSAAL LQPLVTQMVN VYHVHQHSCF LYLGSILVDE YGMEEGCRQG
LLDMLQALCI PTFQLLEQQN GLQNHPDTVD DLFRLATRFI QRSPVTLLRS QVVIPILQWA
IASTTLDHRD ANSSVMRFLR DLIHTGVAND HEEDFELRKE LIGQVMSQLG QQLVSQLLHT
CCFCLPPYTL PDVAEVLWEI MQVDRPTFCR WLENSLKGLP KETTVGAVTV THKQLTDFHK
QVTSAEECKQ VCWALRDFTR LFR
