ID   HS90B_XENLA             Reviewed;         722 AA.
AC   Q6AZV1;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Heat shock cognate protein HSP 90-beta {ECO:0000305};
GN   Name=hsp90ab1 {ECO:0000312|Xenbase:XB-GENE-866421};
GN   Synonyms=hsp90beta {ECO:0000312|EMBL:AAH77195.1};
GN   ORFNames=XELAEV_18028538mg {ECO:0000312|EMBL:OCT77446.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH77195.1};
RN   [1] {ECO:0000312|EMBL:AAH77195.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000312|EMBL:AAH77195.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAV41061.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Taherian A., Ovsenek N., Krone P.H.;
RT   "Expression analysis of Xenopus hsp90 genes.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [4] {ECO:0000312|EMBL:OCT77446.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J {ECO:0000312|EMBL:OCT77446.1};
RC   TISSUE=Blood {ECO:0000312|EMBL:OCT77446.1};
RA   Session A., Uno Y., Kwon T., Chapman J., Toyoda A., Takahashi S., Fukui A.,
RA   Hikosaka A., Putnam N., Stites J., Van Heeringen S., Quigley I., Heinz S.,
RA   Hellsten U., Lyons J., Suzuki A., Kondo M., Ogino H., Ochi H.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S., Van Kruijsbergen I.,
RA   Mozaffari S., Shu S., Schmutz J., Jenkins J., Grimwood J., Carlson J.,
RA   Mitros T., Simakov O., Heald R., Miller K., Haudenschild C., Kuroki Y.,
RA   Tanaka T., Michiue T., Watanabe M., Kinoshita T., Ohta Y., Mawaribuchi S.,
RA   Suzuki Y., Haramoto Y., Yamamoto T., Takagi C., Kitzman J., Shendure J.,
RA   Nakayama T., Izutsu Y., Robert J., Dichmann D., Flajnik M., Houston D.,
RA   Marcotte E., Wallingford J., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Jan Veenstra G., Fujiyama A., Harland R., Taira M., Rokhsar D.S.;
RT   "WGS assembly of Xenopus laevis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30561330; DOI=10.7554/elife.38497;
RA   Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M.,
RA   Brody S.L., Wallingford J.B.;
RT   "A liquid-like organelle at the root of motile ciliopathy.";
RL   Elife 7:0-0(2018).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=33263282; DOI=10.7554/elife.58662;
RA   Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA   Marcotte E.M., Wallingford J.B.;
RT   "Functional partitioning of a liquid-like organelle during assembly of
RT   axonemal dyneins.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle linked to its ATPase activity. This cycle probably
CC       induces conformational changes in the client proteins, thereby causing
CC       their activation. Interacts dynamically with various co-chaperones that
CC       modulate its substrate recognition, ATPase cycle and chaperone
CC       function. Engages with a range of client protein classes via its
CC       interaction with various co-chaperone proteins or complexes, that act
CC       as adapters, simultaneously able to interact with the specific client
CC       and the central chaperone itself. Recruitment of ATP and co-chaperone
CC       followed by client protein forms a functional chaperone. After the
CC       completion of the chaperoning process, properly folded client protein
CC       and co-chaperone leave HSP90 in an ADP-bound partially open
CC       conformation and finally, ADP is released from HSP90 which acquires an
CC       open conformation for the next cycle. {ECO:0000250|UniProtKB:P08238}.
CC   -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC       its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC       open conformation. Upon ATP-binding, the N-terminal domain undergoes
CC       significant conformational changes and comes in contact to form an
CC       active closed conformation. After HSP90 finishes its chaperoning tasks
CC       of assisting the proper folding, stabilization and activation of client
CC       proteins under the active state, ATP molecule is hydrolyzed to ADP
CC       which then dissociates from HSP90 and directs the protein back to the
CC       resting state. {ECO:0000250|UniProtKB:P08238}.
CC   -!- SUBUNIT: Monomer. Homodimer (By similarity).
CC       {ECO:0000250|UniProtKB:P08238}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Dynein
CC       axonemal particle {ECO:0000269|PubMed:30561330,
CC       ECO:0000269|PubMed:33263282}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC   -!- MISCELLANEOUS: In contrast to other HSP90 heat shock proteins, this one
CC       is not induced by heat shock or mitogenic stimuli but is strictly
CC       constitutive. {ECO:0000250|UniProtKB:Q04619}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; BC077195; AAH77195.1; -; mRNA.
DR   EMBL; AY785160; AAV41061.1; -; mRNA.
DR   EMBL; CM004475; OCT77446.1; -; Genomic_DNA.
DR   RefSeq; NP_001086624.1; NM_001093155.1.
DR   AlphaFoldDB; Q6AZV1; -.
DR   SMR; Q6AZV1; -.
DR   STRING; 8355.Q6AZV1; -.
DR   PaxDb; 8355-Q6AZV1; -.
DR   DNASU; 446459; -.
DR   GeneID; 446459; -.
DR   KEGG; xla:446459; -.
DR   AGR; Xenbase:XB-GENE-866421; -.
DR   CTD; 446459; -.
DR   Xenbase; XB-GENE-866421; hsp90ab1.S.
DR   OMA; TRMKAEQ; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Proteomes; UP000694892; Chromosome 5S.
DR   Bgee; 446459; Expressed in neurula embryo and 19 other cell types or tissues.
DR   GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
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; 1.20.120.790; Heat shock protein 90, C-terminal domain; 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; IPR037196; HSP90_C.
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:SF79; HEAT SHOCK PROTEIN HSP 90-BETA-RELATED; 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; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..722
FT                   /note="Heat shock cognate protein HSP 90-beta"
FT                   /id="PRO_0000452441"
FT   REGION          221..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           718..722
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        239..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
SQ   SEQUENCE   722 AA;  82957 MW;  69EBACA626E5C3CA CRC64;
     MPEVAHNGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
     DPSKLDSGKD LKIDIIPNRL ERTLTMIDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
     ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVKVD TGEPIGRGTK
     VILHLKEDQT EYLEEKRVKE TVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKEEKKEE
     EGENDKPKIE DVGSDEEEEG KDKKKKTKKI KEKYIDQEEL NKTKPIWTRN PDDITQEEYG
     EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFIPRRAPFD LFENKKKKNN IKLYVRRVFI
     MDSCDELIPE YLNFVRGVVD SEDLPLNISR EMLQQSKILK VIRKNIVKKC LELFCELAED
     KENYKKFYEG FSKNLKLGIH EDSTNRKKLS ELLRYHTSQT GDEMASLTEY VSRMKENQKS
     IYYITGESKD QVANSAFVER VRKRGFEVVY MTEPIDEYCV QQLKEFDGKT LVSVTKEGLE
     LPEDEEEKKT MEENKTKFES LCKLMKEILD KKVEKVTVSN RLVSSPCCIV TSTYGWTANM
     ERIMKAQALR DNSTMGYMMA KKHLEINPEH PIVETLRQKA DTDKNDKAVK DLVVLLFETA
     LLSSGFSLDD PQTHSNRIYR MIKLGLGIDD DDAPIEEASP SVPDDIPPLE GEEDASRMEE
     VD
//