IMA7_MOUSE
ID IMA7_MOUSE Reviewed; 536 AA.
AC O35345; Q3U388; Q9CVP9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Importin subunit alpha-7;
DE AltName: Full=Importin alpha-S2;
DE AltName: Full=Karyopherin subunit alpha-6;
GN Name=Kpna6; Synonyms=Kpna5;
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=C57BL/6J, and NOD; TISSUE=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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-536.
RX PubMed=9369227; DOI=10.1016/s0014-5793(97)01092-2;
RA Tsuji L., Takumi T., Imamoto N., Yoneda Y.;
RT "Identification of novel homologues of mouse importin alpha, the alpha
RT subunit of the nuclear pore-targeting complex, and their tissue-specific
RT expression.";
RL FEBS Lett. 416:30-34(1997).
RN [4]
RP INTERACTION WITH ZIC3.
RX PubMed=18716025; DOI=10.1093/hmg/ddn239;
RA Hatayama M., Tomizawa T., Sakai-Kato K., Bouvagnet P., Kose S., Imamoto N.,
RA Yokoyama S., Utsunomiya-Tate N., Mikoshiba K., Kigawa T., Aruga J.;
RT "Functional and structural basis of the nuclear localization signal in the
RT ZIC3 zinc finger domain.";
RL Hum. Mol. Genet. 17:3459-3473(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 an adapter protein for
CC nuclear receptor KPNB1. Binds specifically and directly to substrates
CC containing either a simple or bipartite NLS motif. Docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) is
CC mediated by KPNB1 through binding to nucleoporin FxFG repeats and the
CC complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the
CC NPC, Ran binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. 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.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1 (By similarity).
CC Interacts with ZIC3. {ECO:0000250, ECO:0000269|PubMed:18716025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Only slightly detected in Ehrlich ascites tumor
CC cells, thymus and skeletal muscle, clearly detected in kidney, spleen,
CC liver, heart, and lung. High expression in testis.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic
CC central region composed of 10 repeats, and a short hydrophilic C-
CC terminus. The N-terminal hydrophilic region contains the importin beta
CC binding domain (IBB domain), which is sufficient for binding importin
CC beta and essential for nuclear protein import.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal autoinhibitory
CC NLS. Binding of KPNB1 probably overlaps the internal NLS and
CC contributes to a high affinity for cytoplasmic NLS-containing cargo
CC substrates. After dissociation of the importin/substrate complex in the
CC nucleus the internal autohibitory NLS contributes to a low affinity for
CC nuclear NLS-containing proteins (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved in
CC recognition of simple or bipartite NLS motifs. Structurally located
CC within in a helical surface groove they contain several conserved Trp
CC and Asn residues of the corresponding third helices (H3) of ARM repeats
CC which mainly contribute to binding (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AK007053; BAB24841.1; -; mRNA.
DR EMBL; AK154882; BAE32900.1; -; mRNA.
DR EMBL; BC004833; AAH04833.2; -; mRNA.
DR EMBL; AF020773; AAC53373.1; -; mRNA.
DR CCDS; CCDS18701.1; -.
DR RefSeq; NP_032494.3; NM_008468.4.
DR AlphaFoldDB; O35345; -.
DR SMR; O35345; -.
DR BioGRID; 201010; 9.
DR ComplexPortal; CPX-1065; Importin complex, KPNA6 variant.
DR DIP; DIP-48616N; -.
DR IntAct; O35345; 2.
DR STRING; 10090.ENSMUSP00000099650; -.
DR iPTMnet; O35345; -.
DR PhosphoSitePlus; O35345; -.
DR EPD; O35345; -.
DR jPOST; O35345; -.
DR PaxDb; O35345; -.
DR PeptideAtlas; O35345; -.
DR PRIDE; O35345; -.
DR ProteomicsDB; 267241; -.
DR Antibodypedia; 16877; 184 antibodies from 34 providers.
DR DNASU; 16650; -.
DR Ensembl; ENSMUST00000102590; ENSMUSP00000099650; ENSMUSG00000003731.
DR GeneID; 16650; -.
DR KEGG; mmu:16650; -.
DR UCSC; uc008uxz.2; mouse.
DR CTD; 23633; -.
DR MGI; MGI:1100836; Kpna6.
DR VEuPathDB; HostDB:ENSMUSG00000003731; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR InParanoid; O35345; -.
DR OMA; SEAPMEG; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; O35345; -.
DR TreeFam; TF354205; -.
DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
DR BioGRID-ORCS; 16650; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Kpna6; mouse.
DR PRO; PR:O35345; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O35345; protein.
DR Bgee; ENSMUSG00000003731; Expressed in spermatid and 258 other tissues.
DR ExpressionAtlas; O35345; baseline and differential.
DR Genevisible; O35345; MM.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0075506; P:entry of viral genome into host nucleus through nuclear pore complex via importin; IMP:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:MGI.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0019079; P:viral genome replication; IMP:MGI.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..536
FT /note="Importin subunit alpha-7"
FT /id="PRO_0000120730"
FT DOMAIN 1..60
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 76..115
FT /note="ARM 1; truncated"
FT REPEAT 116..159
FT /note="ARM 2"
FT REPEAT 160..204
FT /note="ARM 3"
FT REPEAT 205..243
FT /note="ARM 4"
FT REPEAT 244..288
FT /note="ARM 5"
FT REPEAT 289..328
FT /note="ARM 6"
FT REPEAT 329..370
FT /note="ARM 7"
FT REPEAT 371..410
FT /note="ARM 8"
FT REPEAT 411..453
FT /note="ARM 9"
FT REPEAT 457..502
FT /note="ARM 10; atypical"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..239
FT /note="NLS binding site (major)"
FT /evidence="ECO:0000250"
FT REGION 316..404
FT /note="NLS binding site (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 45..54
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60684"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60684"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60684"
FT CONFLICT 86
FT /note="V -> E (in Ref. 1; BAE32900)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> A (in Ref. 1; BAE32900)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="S -> T (in Ref. 1; BAB24841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 59964 MW; 553A6265023052AC CRC64;
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
NTPGVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
EDVQEQAVWA LGNIAGDSSL CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSSKE SIRKEACWTI
SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQESKRSG SGVNPYCGLI EEAYGLDKIE
FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
