ID Q8C5U3_MOUSE Unreviewed; 557 AA. AC Q8C5U3; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387}; DE Flags: Fragment; GN Name=Hsp90aa1 {ECO:0000313|MGI:MGI:96250}; GN Synonyms=Hspca {ECO:0000313|MGI:MGI:96250}; 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 {ECO:0000313|EMBL:BAC36610.1}; RN [1] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; 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] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; 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 prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; 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., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group 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] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K., RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., RA Hayashizaki Y.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAC36610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC36610.1}; RC TISSUE=Testis {ECO:0000313|EMBL:BAC36610.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. CC {ECO:0000256|ARBA:ARBA00008239}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK077095; BAC36610.1; -; mRNA. DR AlphaFoldDB; Q8C5U3; -. DR PeptideAtlas; Q8C5U3; -. DR AGR; MGI:96250; -. DR MGI; MGI:96250; Hsp90aa1. DR ChiTaRS; Hsp90aa1; mouse. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR CDD; cd16927; HATPase_Hsp90-like; 1. DR Gene3D; 3.30.230.80; -; 1. DR Gene3D; 3.40.50.11260; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_00505; HSP90; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR019805; Heat_shock_protein_90_CS. DR InterPro; IPR001404; Hsp90_fam. DR InterPro; IPR020575; Hsp90_N. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1. DR PANTHER; PTHR11528:SF87; HEAT SHOCK PROTEIN HSP 90-ALPHA; 1. DR Pfam; PF13589; HATPase_c_3; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00298; HSP90; 1. PE 2: Evidence at transcript level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}. FT DOMAIN 40..194 FT /note="Histidine kinase/HSP90-like ATPase" FT /evidence="ECO:0000259|SMART:SM00387" FT REGION 225..279 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..257 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 557 FT /evidence="ECO:0000313|EMBL:BAC36610.1" SQ SEQUENCE 557 AA; 64849 MW; 40C2A4338C7CBC6F CRC64; MPEETQTQDQ PIEEEEVETF 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 LNQTKPIWTR 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 ELPEDEE //