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IPO11_MOUSE
ID   IPO11_MOUSE             Reviewed;         975 AA.
AC   Q8K2V6; Q8BU45; Q8K0B4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Importin-11;
DE            Short=Imp11;
DE   AltName: Full=Ran-binding protein 11;
DE            Short=RanBP11;
GN   Name=Ipo11; Synonyms=Ranbp11;
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   TISSUE=Retina;
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] OF 1-842 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
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   FUNCTION, AND INTERACTION WITH RPL12.
RX   PubMed=11809816; DOI=10.1128/mcb.22.4.1266-1275.2002;
RA   Plafker S.M., Macara I.G.;
RT   "Ribosomal protein L12 uses a distinct nuclear import pathway mediated by
RT   importin 11.";
RL   Mol. Cell. Biol. 22:1266-1275(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, 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 nuclear transport
CC       receptor. Serves as receptor for nuclear localization signals (NLS) in
CC       cargo substrates. Is thought to 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). Mediates the nuclear import
CC       of RPL12, and of UBE2E3 (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:11809816}.
CC   -!- SUBUNIT: Interacts with UBE2E3 and RPL12.
CC       {ECO:0000269|PubMed:11809816}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2V6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2V6-2; Sequence=VSP_010935;
CC   -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR   EMBL; BC029746; AAH29746.1; -; mRNA.
DR   EMBL; BC031900; AAH31900.1; -; mRNA.
DR   EMBL; AK087793; BAC40005.1; -; mRNA.
DR   CCDS; CCDS36776.1; -. [Q8K2V6-1]
DR   CCDS; CCDS88519.1; -. [Q8K2V6-2]
DR   RefSeq; NP_083941.2; NM_029665.3. [Q8K2V6-1]
DR   RefSeq; XP_006517849.1; XM_006517786.3.
DR   AlphaFoldDB; Q8K2V6; -.
DR   SMR; Q8K2V6; -.
DR   BioGRID; 218189; 2.
DR   IntAct; Q8K2V6; 2.
DR   MINT; Q8K2V6; -.
DR   STRING; 10090.ENSMUSP00000079667; -.
DR   iPTMnet; Q8K2V6; -.
DR   PhosphoSitePlus; Q8K2V6; -.
DR   SwissPalm; Q8K2V6; -.
DR   EPD; Q8K2V6; -.
DR   MaxQB; Q8K2V6; -.
DR   PaxDb; Q8K2V6; -.
DR   PeptideAtlas; Q8K2V6; -.
DR   PRIDE; Q8K2V6; -.
DR   ProteomicsDB; 269078; -. [Q8K2V6-1]
DR   ProteomicsDB; 269079; -. [Q8K2V6-2]
DR   Antibodypedia; 23693; 218 antibodies from 26 providers.
DR   DNASU; 76582; -.
DR   Ensembl; ENSMUST00000080856; ENSMUSP00000079667; ENSMUSG00000042590. [Q8K2V6-1]
DR   Ensembl; ENSMUST00000186033; ENSMUSP00000140046; ENSMUSG00000042590. [Q8K2V6-2]
DR   GeneID; 76582; -.
DR   KEGG; mmu:76582; -.
DR   UCSC; uc007rtx.1; mouse. [Q8K2V6-1]
DR   CTD; 51194; -.
DR   MGI; MGI:2442377; Ipo11.
DR   VEuPathDB; HostDB:ENSMUSG00000042590; -.
DR   eggNOG; KOG1993; Eukaryota.
DR   GeneTree; ENSGT00390000014071; -.
DR   HOGENOM; CLU_003886_0_0_1; -.
DR   InParanoid; Q8K2V6; -.
DR   OMA; SFHYVFH; -.
DR   OrthoDB; 228179at2759; -.
DR   PhylomeDB; Q8K2V6; -.
DR   TreeFam; TF324336; -.
DR   BioGRID-ORCS; 76582; 26 hits in 74 CRISPR screens.
DR   ChiTaRS; Ipo11; mouse.
DR   PRO; PR:Q8K2V6; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8K2V6; protein.
DR   Bgee; ENSMUSG00000042590; Expressed in floor plate of midbrain and 257 other tissues.
DR   ExpressionAtlas; Q8K2V6; baseline and differential.
DR   Genevisible; Q8K2V6; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0061608; F:nuclear import signal receptor activity; IDA:MGI.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:MGI.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001494; Importin-beta_N.
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   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..975
FT                   /note="Importin-11"
FT                   /id="PRO_0000120757"
FT   DOMAIN          28..100
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   REPEAT          123..160
FT                   /note="HEAT 1"
FT   REPEAT          283..317
FT                   /note="HEAT 2"
FT   REPEAT          318..356
FT                   /note="HEAT 3"
FT   REPEAT          422..459
FT                   /note="HEAT 4"
FT   REPEAT          473..509
FT                   /note="HEAT 5"
FT   REPEAT          511..548
FT                   /note="HEAT 6"
FT   REPEAT          555..593
FT                   /note="HEAT 7"
FT   REPEAT          600..636
FT                   /note="HEAT 8"
FT   REPEAT          640..677
FT                   /note="HEAT 9"
FT   REPEAT          683..720
FT                   /note="HEAT 10"
FT   REPEAT          731..773
FT                   /note="HEAT 11"
FT   REPEAT          819..849
FT                   /note="HEAT 12"
FT   REPEAT          850..887
FT                   /note="HEAT 13"
FT   REPEAT          957..974
FT                   /note="HEAT 14"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI26"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI26"
FT   VAR_SEQ         698
FT                   /note="L -> LPSSCLANEL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010935"
FT   CONFLICT        349
FT                   /note="A -> V (in Ref. 2; BAC40005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   975 AA;  112416 MW;  3DEA79E8028C483D CRC64;
     MDLNSASSVV LQVLTQATSQ DTAVLKPAEE QLKQWETQPG FYSVLLNIFT NHTLDINVRW
     LAVLYFKHGI DRYWRRVAPH ALSEEEKSTL RAGLITNFNE PINQIATQIA VLIAKVARLD
     CPRQWPELIP TLVESVKVQD DLRQHRALLT FYHVTKTLAS KRLAADRKLF YDLASGIYNF
     ACSLWNHHTD TFLQHVSSGN EAAVLSSLER TLLSLKVLRK LTVNGFVEPH KNMEVMGFLH
     GIFERLKQFL ECSRSIGTDN VCRDRLEKTI ILFTKVLLDF LDQHPISFTP LIQRSLEFSV
     SYVFTEVGEG VTFERFIVQC MNLIKMIVKN YAYKPSKNFE DSSPETLEAH KIKMAFFTYP
     TLTEICRRLV SHYFLLTEEE LTMWEEDPEG FTVEETGGDS WKYSLRPCTE VLFIDIFHEY
     NQTLTPVLLE MMQTLEGPTN VEDMNALLIK DAVYNAVGLA AFELFDSVDF DQWFKTQLLP
     ELQVSHNRYK PLRRRVIWLI GQWISVKFKS DLRPMLYEAI CNLLQDQDLV VRIETATTLK
     LTVDDFEFRT DQFLPYLETM FTLLFQLLQQ VTECDTKMHV LHVLSCVIER VNVQIRPYVG
     CLVQYLPLLW KQSEEHNMLR CAILTTLIHL VQGLGADSKN LYPFLLPVIQ LSTDVSQPPH
     VYLLEDGLEL WLVTLENSPC VTPELLRIFQ NMSPLLELSS ENLRTCFKII NGYIFLSSTE
     FLQTYAAGLC QSFYELLPEI TTEGQVQVLK VVENALKVNP VLGPQMFQRI LPCVFRGVIE
     GERYPVVMSI YLAVMGRVLL QNTSFFSSLL NEMGHEFNQE MDQLLGNVIE MWVDRMDNIT
     QPERKKLSAL ALLSLLPSDN SVIQDKFCGI INISVEALHD VMTEDPETRT YKDCMLMSQH
     EEPKVTEDEE PPTEQDKRKK MLALKDPVHT VSLQQFIYEK LKAQQEILGE QGFQSLMETV
     DTEIVTQLQE FLQGF
 
 
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