TNPO1_MOUSE
ID TNPO1_MOUSE Reviewed; 898 AA.
AC Q8BFY9; Q8C0S3; Q8K2E7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transportin-1;
DE AltName: Full=Importin beta-2;
DE AltName: Full=Karyopherin beta-2;
GN Name=Tnpo1; Synonyms=Kpnb2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Pituitary, and Testis;
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] (ISOFORM 2).
RC TISSUE=Mammary tumor, and Mesenchymal cell;
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 [3]
RP FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
RX PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT "Multiple pathways contribute to nuclear import of core histones.";
RL EMBO Rep. 2:690-696(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates (PubMed:11493596). May mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus (By similarity). Involved in nuclear import
CC of M9-containing proteins. In vitro, binds directly to the M9 region of
CC the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and
CC mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export.
CC Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5
CC (By similarity). In vitro, mediates nuclear import of SRP19 (By
CC similarity). Mediates the import of histones H2A, H2B, H3 and H4
CC (PubMed:11493596). Mediates nuclear import of ADAR/ADAR1 in a RanGTP-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q92973,
CC ECO:0000269|PubMed:11493596}.
CC -!- SUBUNIT: Identified in a complex that contains TNPO1, RAN and RANBP1
CC (By similarity). Binds HNRPA1, HNRPA2, HNRNPDL, RPS7, RPL5 and RAN.
CC Interacts with H2A, H2B, H3 and H4 histones (PubMed:11493596).
CC Interacts with isoform 1 and isoform 5 of ADAR/ADAR1 (via DRBM 3
CC domain). Interacts with SNAI1 (via zinc fingers); the interaction
CC mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc fingers)
CC (By similarity). Interacts with RPL23A (via BIB domain) AND SRP19; this
CC interaction is involved in RPL23A and SRP19 import into the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:Q92973,
CC ECO:0000269|PubMed:11493596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BFY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFY9-2; Sequence=VSP_038030;
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK029953; BAC26696.1; ALT_INIT; mRNA.
DR EMBL; AK030580; BAC27029.1; ALT_INIT; mRNA.
DR EMBL; AK045132; BAC32236.1; -; mRNA.
DR EMBL; BC031571; AAH31571.1; -; mRNA.
DR EMBL; BC055372; AAH55372.1; -; mRNA.
DR CCDS; CCDS26717.2; -. [Q8BFY9-1]
DR CCDS; CCDS36760.1; -. [Q8BFY9-2]
DR RefSeq; NP_001041732.1; NM_001048267.1. [Q8BFY9-2]
DR RefSeq; NP_848831.2; NM_178716.3. [Q8BFY9-1]
DR RefSeq; XP_006517699.1; XM_006517636.3. [Q8BFY9-2]
DR RefSeq; XP_006517700.1; XM_006517637.3. [Q8BFY9-2]
DR AlphaFoldDB; Q8BFY9; -.
DR SMR; Q8BFY9; -.
DR BioGRID; 232018; 70.
DR IntAct; Q8BFY9; 53.
DR MINT; Q8BFY9; -.
DR STRING; 10090.ENSMUSP00000105028; -.
DR iPTMnet; Q8BFY9; -.
DR PhosphoSitePlus; Q8BFY9; -.
DR SwissPalm; Q8BFY9; -.
DR EPD; Q8BFY9; -.
DR jPOST; Q8BFY9; -.
DR MaxQB; Q8BFY9; -.
DR PaxDb; Q8BFY9; -.
DR PeptideAtlas; Q8BFY9; -.
DR PRIDE; Q8BFY9; -.
DR ProteomicsDB; 259605; -. [Q8BFY9-1]
DR ProteomicsDB; 259606; -. [Q8BFY9-2]
DR Antibodypedia; 4275; 296 antibodies from 30 providers.
DR DNASU; 238799; -.
DR Ensembl; ENSMUST00000109399; ENSMUSP00000105026; ENSMUSG00000009470. [Q8BFY9-2]
DR Ensembl; ENSMUST00000109401; ENSMUSP00000105028; ENSMUSG00000009470. [Q8BFY9-1]
DR GeneID; 238799; -.
DR KEGG; mmu:238799; -.
DR UCSC; uc007rpd.1; mouse. [Q8BFY9-1]
DR CTD; 3842; -.
DR MGI; MGI:2681523; Tnpo1.
DR VEuPathDB; HostDB:ENSMUSG00000009470; -.
DR eggNOG; KOG2023; Eukaryota.
DR GeneTree; ENSGT00940000155389; -.
DR InParanoid; Q8BFY9; -.
DR OrthoDB; 525700at2759; -.
DR PhylomeDB; Q8BFY9; -.
DR TreeFam; TF300825; -.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 238799; 26 hits in 69 CRISPR screens.
DR ChiTaRS; Tnpo1; mouse.
DR PRO; PR:Q8BFY9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BFY9; protein.
DR Bgee; ENSMUSG00000009470; Expressed in undifferentiated genital tubercle and 255 other tissues.
DR ExpressionAtlas; Q8BFY9; baseline and differential.
DR Genevisible; Q8BFY9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..898
FT /note="Transportin-1"
FT /id="PRO_0000120766"
FT REPEAT 19..46
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT DOMAIN 41..109
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 51..89
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 98..131
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 137..174
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 181..211
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 224..251
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 263..290
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 306..397
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 405..433
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 445..472
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 486..519
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 527..560
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 568..606
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 614..665
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 676..707
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 715..748
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 756..791
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 799..832
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 841..872
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 875..895
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 468
FT /note="Important for interaction with cargo nuclear
FT localization signals"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT SITE 738
FT /note="Important for interaction with cargo nuclear
FT localization signals"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT VAR_SEQ 1..9
FT /note="MVWDRQTKM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038030"
FT CONFLICT 389
FT /note="A -> S (in Ref. 1; BAC26696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 102357 MW; E04FB7F8A67581E3 CRC64;
MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ YPDFNNYLIF
VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK SECLNNIGDS SPLIRATVGI
LITTIASKGE LQNWPDLLPK LCSLLDSEDY NTCEGAFGAL QKICEDSAEI LDSDVLDRPL
NIMIPKFLQF FKHSSPKIRS HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEAEVR
KNVCRALVML LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV
LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS RTVAQQHEED
GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD ELLPHILPLL KELLFHHEWV
VKESGILVLG AIAEGCMQGM IPYLPELIPH LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ
PPDTYLKPLM TELLKRILDS NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK
YQHKNLLILY DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS
VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPEQ YEAPDKDFMI VALDLLSGLA
EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG DLTKACFQHV KPCIADFMPI
LGTNLNPEFI SVCNNATWAI GEISIQMGIE MQPYIPMVLH QLVEIINRPN TPKTLLENTA
ITIGRLGYVC PQEVAPMLQQ FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF
IFFCDAVASW INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV
