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IPO13_MOUSE
ID   IPO13_MOUSE             Reviewed;         963 AA.
AC   Q8K0C1; Q6ZQ60;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Importin-13;
DE            Short=Imp13;
GN   Name=Ipo13; Synonyms=Kiaa0724;
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] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, 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 UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of
CC       the paired homeobox family. Also mediates nuclear export of eIF-1A, and
CC       the cytoplasmic release of eIF-1A is triggered by the loading of import
CC       substrates onto IPO13 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with UBC9, RAN, RBM8A, eIF-1A and PAX6.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0C1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0C1-2; Sequence=VSP_010936, VSP_010937;
CC   -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR   EMBL; AK129200; BAC98010.2; -; Transcribed_RNA.
DR   EMBL; BC031823; AAH31823.1; -; mRNA.
DR   EMBL; AK052257; BAC34899.1; -; mRNA.
DR   CCDS; CCDS18542.1; -. [Q8K0C1-1]
DR   RefSeq; NP_666264.1; NM_146152.3. [Q8K0C1-1]
DR   AlphaFoldDB; Q8K0C1; -.
DR   SMR; Q8K0C1; -.
DR   BioGRID; 230998; 2.
DR   STRING; 10090.ENSMUSP00000035989; -.
DR   iPTMnet; Q8K0C1; -.
DR   PhosphoSitePlus; Q8K0C1; -.
DR   EPD; Q8K0C1; -.
DR   MaxQB; Q8K0C1; -.
DR   PaxDb; Q8K0C1; -.
DR   PeptideAtlas; Q8K0C1; -.
DR   PRIDE; Q8K0C1; -.
DR   ProteomicsDB; 269080; -. [Q8K0C1-1]
DR   ProteomicsDB; 269081; -. [Q8K0C1-2]
DR   Antibodypedia; 32405; 119 antibodies from 20 providers.
DR   DNASU; 230673; -.
DR   Ensembl; ENSMUST00000036156; ENSMUSP00000035989; ENSMUSG00000033365. [Q8K0C1-1]
DR   GeneID; 230673; -.
DR   KEGG; mmu:230673; -.
DR   UCSC; uc008ujg.1; mouse. [Q8K0C1-1]
DR   CTD; 9670; -.
DR   MGI; MGI:2385205; Ipo13.
DR   VEuPathDB; HostDB:ENSMUSG00000033365; -.
DR   eggNOG; KOG2022; Eukaryota.
DR   GeneTree; ENSGT00530000063347; -.
DR   HOGENOM; CLU_005996_3_0_1; -.
DR   InParanoid; Q8K0C1; -.
DR   OMA; DTFMYCY; -.
DR   OrthoDB; 1032285at2759; -.
DR   PhylomeDB; Q8K0C1; -.
DR   TreeFam; TF314539; -.
DR   BioGRID-ORCS; 230673; 27 hits in 73 CRISPR screens.
DR   PRO; PR:Q8K0C1; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8K0C1; protein.
DR   Bgee; ENSMUSG00000033365; Expressed in hindlimb stylopod muscle and 228 other tissues.
DR   Genevisible; Q8K0C1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
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; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR040709; Importin_rep_1.
DR   InterPro; IPR040944; Importin_rep_2.
DR   InterPro; IPR040520; Importin_rep_3.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF18773; Importin_rep; 1.
DR   Pfam; PF18786; Importin_rep_2; 2.
DR   Pfam; PF18806; Importin_rep_3; 1.
DR   Pfam; PF08389; Xpo1; 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..963
FT                   /note="Importin-13"
FT                   /id="PRO_0000120759"
FT   REPEAT          24..54
FT                   /note="HEAT 1"
FT   DOMAIN          45..111
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   REPEAT          56..88
FT                   /note="HEAT 2"
FT   REPEAT          95..135
FT                   /note="HEAT 3"
FT   REPEAT          142..179
FT                   /note="HEAT 4"
FT   REPEAT          194..231
FT                   /note="HEAT 5"
FT   REPEAT          236..268
FT                   /note="HEAT 6"
FT   REPEAT          276..325
FT                   /note="HEAT 7"
FT   REPEAT          330..372
FT                   /note="HEAT 8"
FT   REPEAT          375..438
FT                   /note="HEAT 9"
FT   REPEAT          440..476
FT                   /note="HEAT 10"
FT   REPEAT          487..522
FT                   /note="HEAT 11"
FT   REPEAT          524..558
FT                   /note="HEAT 12"
FT   REPEAT          562..600
FT                   /note="HEAT 13"
FT   REPEAT          603..648
FT                   /note="HEAT 14"
FT   REPEAT          676..716
FT                   /note="HEAT 15"
FT   REPEAT          720..754
FT                   /note="HEAT 16"
FT   REPEAT          761..803
FT                   /note="HEAT 17"
FT   REPEAT          815..845
FT                   /note="HEAT 18"
FT   REPEAT          860..893
FT                   /note="HEAT 19"
FT   REPEAT          897..931
FT                   /note="HEAT 20"
FT   VAR_SEQ         369..375
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_010936"
FT   VAR_SEQ         872..886
FT                   /note="AIGGQASRSLMDCFA -> VSWSKWLGVGRPSLLRRLALCCG (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_010937"
SQ   SEQUENCE   963 AA;  108229 MW;  3ABBCE15668B6BCB CRC64;
     MERREEQLGA AGAGAAPALD FTVENVEKAL HQLYYDPNID NKNLAQKWLM QAQVSPQAWH
     FSWQLLQPDK VPEIQYFGAS ALHIKISRYW SDIPTDQYES LKAQLFTQIT RFASGSKIVL
     TRLCVALASL ALSMMPDAWP CAVADMVRLF QAEDSPVDSQ GRCLALLELL TVLPEEFQTS
     RLPQYRKGLV RTSLAVECGT VFPLLEQLLQ QPSSPSCVRQ KVLKCFSSWV QLEVPLQDCE
     ALIQAAFAAL QDSELFDSSV EAIVNAISQP DAQRYVNTLL KLIPLVLGLQ EQLRQAVQNG
     DMETSHGICR IAVALGENHS RALLDQVEHW QSFLALVNMI MFCTGIPGHY PVNETTSSLT
     LTFWYTLQDD ILSFEAEKQA VYQQVYRPVY FQLVDVLLHK AQFPSDEEYG FWSSDEKEQF
     RIYRVDISDT LMYVYEMLGA ELLSNLYDKL GRLLTSSEEP YSWQHTEALL YGFQSIAETI
     DVNYSDVVPG LIGLIPRISI SNVQLADTVM FTIGALSEWL ADHPVMINSV LPLVLHALGN
     PELSVSSVST LKKICRECKY DLPPYAANIV AVSQDVLMKQ IHKTSQCMWL MQALGFLLSA
     LQVEEILKNL HSLISPYIQQ LEKLAEEIPN PSNKLAIVHI LGLLSNLFTT LDVSHHEDDH
     EGPELRKLPV PQGPNPVVVV LQQVFQLIQK VLSKWLNDAQ VVEAVCAIFE KSVKTLLDDF
     APMVPQLCEM LGRMYSTVPQ ASALDLTRQL VHIFAHEPAH FPPIEALFLL VTSVTLSLFQ
     QGPRDHPDIV DSFMQLLAQA LKRKPDLFLC ERLDVKAVFQ CAVLALKFPE APTVKASCGF
     FTELLPRCGE IESVGKVVQE DGRMLLIAVL EAIGGQASRS LMDCFADILF ALNKHCFSLL
     SMWIKEALQP PGFPSARLSP EQKDTFSQQI LRERVNKRRV KEMVKEFTLL CRGLHGTDYT
     ADY
 
 
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