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IPO4_MOUSE
ID   IPO4_MOUSE              Reviewed;        1082 AA.
AC   Q8VI75; Q3TBW0; Q99J52;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Importin-4 {ECO:0000303|PubMed:11823430};
DE            Short=Imp4 {ECO:0000303|PubMed:11823430};
DE   AltName: Full=Importin-4a {ECO:0000303|PubMed:11823430};
DE            Short=Imp4a {ECO:0000303|PubMed:11823430};
DE   AltName: Full=Ran-binding protein 4;
DE            Short=RanBP4;
GN   Name=Ipo4; Synonyms=Imp4a, Ranbp4;
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], FUNCTION, AND INTERACTION WITH RPS3A.
RX   PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA   Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT   "Importins fulfill a dual function as nuclear import receptors and
RT   cytoplasmic chaperones for exposed basic domains.";
RL   EMBO J. 21:377-386(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Pituitary;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-1082.
RC   TISSUE=Mammary cancer;
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   [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: Nuclear transport receptor that mediates nuclear import of
CC       proteins, such as histones, RPS3A, TNP2 and VDR. Serves as receptor for
CC       nuclear localization signals (NLS) in cargo substrates. Is thought to
CC       mediate docking of the importin/substrate complex to the nuclear pore
CC       complex (NPC) through binding to nucleoporin and the complex is
CC       subsequently translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to
CC       the importin, the importin/substrate complex dissociates and importin
CC       is re-exported from the nucleus to the cytoplasm where GTP hydrolysis
CC       releases Ran. The directionality of nuclear import is thought to be
CC       conferred by an asymmetric distribution of the GTP- and GDP-bound forms
CC       of Ran between the cytoplasm and nucleus. Mediates the nuclear import
CC       of the histone H3-H4 dimer when in complex with ASF1 (ASF1A or ASF1B).
CC       Mediates the ligand-independent nuclear import of vitamin D receptor
CC       (VDR). {ECO:0000250|UniProtKB:Q8TEX9}.
CC   -!- SUBUNIT: Found in a cytosolic complex with ASF1 (ASF1A or ASF1B) and
CC       histones H3 and H4. {ECO:0000250|UniProtKB:Q8TEX9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TEX9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8TEX9}.
CC   -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC26988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF123388; AAL55522.1; -; mRNA.
DR   EMBL; AK030490; BAC26988.1; ALT_INIT; mRNA.
DR   EMBL; AK147086; BAE27666.1; -; mRNA.
DR   EMBL; AK171031; BAE42197.1; -; mRNA.
DR   EMBL; BC003469; AAH03469.1; ALT_INIT; mRNA.
DR   CCDS; CCDS27121.1; -.
DR   RefSeq; NP_077229.4; NM_024267.6.
DR   AlphaFoldDB; Q8VI75; -.
DR   SMR; Q8VI75; -.
DR   BioGRID; 217713; 5.
DR   IntAct; Q8VI75; 1.
DR   STRING; 10090.ENSMUSP00000036555; -.
DR   iPTMnet; Q8VI75; -.
DR   PhosphoSitePlus; Q8VI75; -.
DR   EPD; Q8VI75; -.
DR   MaxQB; Q8VI75; -.
DR   PaxDb; Q8VI75; -.
DR   PeptideAtlas; Q8VI75; -.
DR   PRIDE; Q8VI75; -.
DR   ProteomicsDB; 301659; -.
DR   Antibodypedia; 47245; 112 antibodies from 20 providers.
DR   DNASU; 75751; -.
DR   Ensembl; ENSMUST00000047131; ENSMUSP00000036555; ENSMUSG00000002319.
DR   GeneID; 75751; -.
DR   KEGG; mmu:75751; -.
DR   UCSC; uc007tzp.1; mouse.
DR   CTD; 79711; -.
DR   MGI; MGI:1923001; Ipo4.
DR   VEuPathDB; HostDB:ENSMUSG00000002319; -.
DR   eggNOG; KOG2171; Eukaryota.
DR   GeneTree; ENSGT00550000075074; -.
DR   HOGENOM; CLU_003794_1_2_1; -.
DR   InParanoid; Q8VI75; -.
DR   OMA; VHEDIDI; -.
DR   OrthoDB; 331433at2759; -.
DR   PhylomeDB; Q8VI75; -.
DR   TreeFam; TF323157; -.
DR   BioGRID-ORCS; 75751; 11 hits in 73 CRISPR screens.
DR   ChiTaRS; Ipo4; mouse.
DR   PRO; PR:Q8VI75; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q8VI75; protein.
DR   Bgee; ENSMUSG00000002319; Expressed in internal carotid artery and 256 other tissues.
DR   ExpressionAtlas; Q8VI75; baseline and differential.
DR   Genevisible; Q8VI75; MM.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0061608; F:nuclear import signal receptor activity; ISS:UniProtKB.
DR   GO; GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR   GO; GO:0042254; P:ribosome biogenesis; ISO:MGI.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR040122; Importin_beta.
DR   PANTHER; PTHR10527; PTHR10527; 1.
DR   Pfam; PF02985; HEAT; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN           1..1082
FT                   /note="Importin-4"
FT                   /id="PRO_0000120749"
FT   DOMAIN          24..90
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   REPEAT          348..385
FT                   /note="HEAT 1"
FT   REPEAT          390..427
FT                   /note="HEAT 2"
FT   REPEAT          431..471
FT                   /note="HEAT 3"
FT   REPEAT          475..513
FT                   /note="HEAT 4"
FT   REPEAT          896..933
FT                   /note="HEAT 5"
FT   REPEAT          937..975
FT                   /note="HEAT 6"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TEX9"
SQ   SEQUENCE   1082 AA;  119275 MW;  BF78D395A3111FF3 CRC64;
     MEPAGLEQIL KELLLPDTER IRRATEQLQT ILRDPAALPA LFDLLATATD SQIRQFAAVL
     TRRRLNNRWR RLAPEQRESL KSLVLTALQK ETVHSVSVSL AQLSATIFRK EGLQGWPQFM
     NLLQHSTHSS HSPEKEVGLL LLSVVVSSQP EAFHAHQHEL LQLLNETLSD VSFPGVLFYS
     LRTLTAIARY VRPDDVSLAR MLVPKVVTAL RTLIPLDEVK ACEALEALDE MLETELPIIN
     PHLSEVLTFC LEVAKNVALG EPLRVRVLCC LTFLVKVKSK ALLKNRLVPP LLHALFPLMA
     AEPPMGQLDP EDQDSDDDDL EIGLMGETPK HFAVQVVDML ALHLPPEKLC PHVMPMLEEA
     LRSEDPYQRK AGFLVLAVLS DGAGDHIRQR LLYPLLQIVC KGLDDPSQIV RNAALFALGQ
     FSENLQPHIS SYSEEVMPLL LSYLKSVPMG NTHHLAKACY ALENFVENLG PKVQPYLPEL
     MECMLQPLKN PSKARTKELA VSAIGAIATA AQDSLLPYFP TIMDLLREFL LTGHEDFHLV
     QIQSLETLGV LARALGESMK PLAEECCQLG LGLCIHIDDP DVRRCTYSLF AALSGLMGEG
     LGPYLPQITT LMLLSLRSTE GIVPQYDGIS SFLLFDDDSE AEEEEELMDE DMEEEGDDSE
     ISGYSVENAF FDEKEDTCTA LGEISMNTCV AFLPFMDATF DEVYKLLECP HMNVRKSAYE
     ALGQFCCALH KASQRSSSDP SSSPVLQTSL ARVMPAYMQA VKVERERPVV MAVLESLTGV
     LRTCGSLALQ PPGRLSELCN VLKAVLQKKT ACQDAEEDDD EDDDQAEYDA MLLEHAGEAI
     PVLAATAGGH AFAPFFATFL PLLLCKTKQS CTVAEKSFAV GTLAESIQGL GTASAQFVSR
     LFPVLLNNAR EADPEVRSNA IFGLGVLAEH GGCPAQDHFP KLLGLLLPLL ARERHDRVRD
     NICGALARVL MASPVGKTEP QVLATLLRAL PLKEDMEEWL TIGHLFSFLH QNNPEQVVDV
     ASELLRICSL ILPDNRIPPD TKAALLLLLT FLAKQHTDSF HTALGSLPND KAQELQAMMG
     LT
 
 
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