ID   Q3TKB9_MOUSE            Unreviewed;       556 AA.
AC   Q3TKB9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   19-FEB-2014, entry version 69.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Hsp90aa1; Synonyms=Hspca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
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DR   EMBL; AK166867; BAE39080.1; -; mRNA.
DR   EMBL; AK167065; BAE39226.1; -; mRNA.
DR   UniGene; Mm.1843; -.
DR   UniGene; Mm.315997; -.
DR   UniGene; Mm.341186; -.
DR   UniGene; Mm.440626; -.
DR   UniGene; Mm.486334; -.
DR   MGI; MGI:96250; Hsp90aa1.
DR   HOVERGEN; HBG007374; -.
DR   InParanoid; Q3TKB9; -.
DR   Genevestigator; Q3TKB9; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0016887; F:ATPase activity; IEA:Ensembl.
DR   GO; GO:0002135; F:CTP binding; IEA:Ensembl.
DR   GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0002134; F:UTP binding; IEA:Ensembl.
DR   GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0045040; P:protein import into mitochondrial outer membrane; IEA:Ensembl.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR   GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR   Gene3D; 3.30.565.10; -; 2.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_ATP-bd.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     556    556
SQ   SEQUENCE   556 AA;  64738 MW;  50358D16961C6F31 CRC64;
     MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
     YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
     ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
     GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE
     KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
     NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN
     NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK
     CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD
     YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK
     TLVSVTKEGL ELPEDE
//