HS90B_XENLA
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 03-AUG-2022, entry version 130.
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 DNASU; 446459; -.
DR GeneID; 446459; -.
DR KEGG; xla:446459; -.
DR CTD; 446459; -.
DR Xenbase; XB-GENE-866421; hsp90ab1.S.
DR OMA; TRMKAEQ; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 446459; Expressed in neurula embryo and 19 other 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 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_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; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 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
