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IMA8_MOUSE
ID   IMA8_MOUSE              Reviewed;         499 AA.
AC   C0LLJ0; C0LLJ1; Q3UWY3; Q58HC5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Importin subunit alpha-8;
DE   AltName: Full=Karyopherin subunit alpha-7;
GN   Name=Kpna7;
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 [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   INTERACTION WITH KPNB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
RX   PubMed=20699224; DOI=10.1074/jbc.m110.117044;
RA   Hu J., Wang F., Yuan Y., Zhu X., Wang Y., Zhang Y., Kou Z., Wang S.,
RA   Gao S.;
RT   "Novel importin-alpha family member Kpna7 is required for normal fertility
RT   and fecundity in the mouse.";
RL   J. Biol. Chem. 285:33113-33122(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Hartmann E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-499 (ISOFORM 2).
RC   TISSUE=Embryo;
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).
CC   -!- FUNCTION: Functions in nuclear protein import. {ECO:0000250}.
CC   -!- SUBUNIT: Binds very efficiently to importin subunit beta-1/KPNB1 via
CC       the IBB domain. This complex dissociates in the presence of RAN-GTP (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20699224}. Note=In
CC       MII-stage oocytes, localizes to the spindle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=C0LLJ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=C0LLJ0-2; Sequence=VSP_041924;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in ovary. Isoform 1 is the
CC       predominant form. {ECO:0000269|PubMed:20699224}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at high levels in germinal vesicle-stage
CC       oocytes, as well as in zygotes and 2-cell embryos (at protein level).
CC       Drastically down-regulated after the 2-cell stage.
CC       {ECO:0000269|PubMed:20699224}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice exhibit abnormal preimplantation
CC       development. About half of the mutant embryos fail to develop into the
CC       blastocyst stage, or are delayed. Lethality is greater among female
CC       than among male embryos. {ECO:0000269|PubMed:20699224}.
CC   -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR   EMBL; FJ717332; ACN85341.1; -; mRNA.
DR   EMBL; FJ717333; ACN85342.1; -; mRNA.
DR   EMBL; AY950703; AAX50192.1; -; mRNA.
DR   EMBL; AC110556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466529; EDL19009.1; -; Genomic_DNA.
DR   EMBL; AK136027; BAE22781.1; -; mRNA.
DR   CCDS; CCDS19852.1; -. [C0LLJ0-1]
DR   CCDS; CCDS84996.1; -. [C0LLJ0-2]
DR   RefSeq; NP_001013796.2; NM_001013774.2. [C0LLJ0-1]
DR   RefSeq; NP_001334460.1; NM_001347531.1. [C0LLJ0-2]
DR   RefSeq; XP_017176433.1; XM_017320944.1.
DR   AlphaFoldDB; C0LLJ0; -.
DR   SMR; C0LLJ0; -.
DR   ComplexPortal; CPX-1067; Importin complex, KPNA7 variant.
DR   iPTMnet; C0LLJ0; -.
DR   PhosphoSitePlus; C0LLJ0; -.
DR   PaxDb; C0LLJ0; -.
DR   PeptideAtlas; C0LLJ0; -.
DR   PRIDE; C0LLJ0; -.
DR   Antibodypedia; 30296; 43 antibodies from 19 providers.
DR   DNASU; 381686; -.
DR   Ensembl; ENSMUST00000110672; ENSMUSP00000106300; ENSMUSG00000038770. [C0LLJ0-1]
DR   Ensembl; ENSMUST00000110673; ENSMUSP00000106301; ENSMUSG00000038770. [C0LLJ0-2]
DR   Ensembl; ENSMUST00000116454; ENSMUSP00000112155; ENSMUSG00000038770. [C0LLJ0-1]
DR   GeneID; 381686; -.
DR   KEGG; mmu:381686; -.
DR   UCSC; uc009alx.1; mouse. [C0LLJ0-2]
DR   UCSC; uc009aly.1; mouse. [C0LLJ0-1]
DR   CTD; 402569; -.
DR   MGI; MGI:2141165; Kpna7.
DR   VEuPathDB; HostDB:ENSMUSG00000038770; -.
DR   eggNOG; KOG0166; Eukaryota.
DR   GeneTree; ENSGT01050000244891; -.
DR   HOGENOM; CLU_018084_6_1_1; -.
DR   InParanoid; C0LLJ0; -.
DR   OMA; KENMCLL; -.
DR   OrthoDB; 1111872at2759; -.
DR   PhylomeDB; C0LLJ0; -.
DR   TreeFam; TF101178; -.
DR   BioGRID-ORCS; 381686; 2 hits in 59 CRISPR screens.
DR   ChiTaRS; Kpna7; mouse.
DR   PRO; PR:C0LLJ0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; C0LLJ0; protein.
DR   Bgee; ENSMUSG00000038770; Expressed in animal zygote and 20 other tissues.
DR   ExpressionAtlas; C0LLJ0; baseline and differential.
DR   Genevisible; C0LLJ0; MM.
DR   GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR   GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
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:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:1902466; P:positive regulation of histone H3-K27 trimethylation; IMP:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IC:ComplexPortal.
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; 5.
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   Alternative splicing; Nucleus; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN           1..499
FT                   /note="Importin subunit alpha-8"
FT                   /id="PRO_0000413537"
FT   DOMAIN          1..57
FT                   /note="IBB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT   REPEAT          101..141
FT                   /note="ARM 1"
FT   REPEAT          144..183
FT                   /note="ARM 2"
FT   REPEAT          186..226
FT                   /note="ARM 3"
FT   REPEAT          229..268
FT                   /note="ARM 4"
FT   REPEAT          271..310
FT                   /note="ARM 5"
FT   REPEAT          313..352
FT                   /note="ARM 6"
FT   REPEAT          354..393
FT                   /note="ARM 7"
FT   REPEAT          397..436
FT                   /note="ARM 8"
FT   VAR_SEQ         182
FT                   /note="A -> ADRKMPDTQVQIFTPSTREAKA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:20699224"
FT                   /id="VSP_041924"
FT   CONFLICT        161
FT                   /note="E -> D (in Ref. 1; ACN85342 and 2; AAX50192)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  55458 MW;  0B1094E04CAFA556 CRC64;
     MATSKAPKER LKNYKYRGKE MSLPRQQRIA SSLQLRKTRK DEQVLKRRNI DLFSSDMVSQ
     ALVKEVNFTL DDIIQAVNSS DPILHFRATR AAREMISQEN TPPLNLIIEA GLIPKLVDFL
     KATPHPKLQF EAAWVLTNIA SGTSEQTRAV VKEGAIQPLI ELLCSPHLTV SEQAVWALGN
     IAGDCAEFRD CVISNNAIPH LINLISKGIP ITFLRNISWT LSNLCRNKDP YPSESAVRQM
     LPPLCQLLLH RDNEILADTC WALSYLTKGG KEYIHHVVTT GILPRLVELM TSSELSISIP
     CLHTIGNIVA GTDEQTQMAI DAGMLKVLGQ VLKHPKTSIQ VLAAWTMSNV AAGPRHQVEQ
     LLCNLLPILV DLLRNAELKV QKEVVCTVIN IATGASQDQL TLLAHSGILE PMLSLLSAPD
     LEVVIIVLDI ISYLLQHIDN LQEKKRLYFQ IEKFGGFEKI ECLQHHHNIS ISNSALDIIE
     KYFCEDGDGD SLPGPGLRV
 
 
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