HS90B_DANRE
ID HS90B_DANRE Reviewed; 725 AA.
AC O57521; Q6P0Y9; Q90475;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Heat shock protein HSP 90-beta;
GN Name=hsp90ab1; Synonyms=hsp90b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10364427; DOI=10.1006/dbio.1999.9262;
RA Lele Z., Hartson S.D., Martin C.C., Whitesell L., Matts R.L., Krone P.H.;
RT "Disruption of zebrafish somite development by pharmacologic inhibition of
RT Hsp90.";
RL Dev. Biol. 210:56-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UNC45B, AND TISSUE
RP SPECIFICITY.
RX PubMed=17586488; DOI=10.1016/j.ydbio.2007.05.014;
RA Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., Strahle U.;
RT "The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a
RT during myofibrillogenesis.";
RL Dev. Biol. 308:133-143(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Coumailleau P., Angelier N.;
RT "Molecular cloning of a cDNA encoding the Danio rerio hsp90 beta isoform.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-132, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Embryo;
RX PubMed=7980538; DOI=10.1006/bbrc.1994.2522;
RA Krone P.H., Sass J.B.;
RT "HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and are
RT differentially regulated in developing embryos.";
RL Biochem. Biophys. Res. Commun. 204:746-752(1994).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=8652412; DOI=10.1016/0925-4773(95)00476-9;
RA Sass J.B., Weinberg E.S., Krone P.H.;
RT "Specific localization of zebrafish hsp90 alpha mRNA to myoD-expressing
RT cells suggests a role for hsp90 alpha during normal muscle development.";
RL Mech. Dev. 54:195-204(1996).
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 (By similarity). Not required for
CC myofibril formation in skeletal muscles (PubMed:10364427,
CC PubMed:17586488). {ECO:0000250|UniProtKB:P08238,
CC ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488}.
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). Interacts with unc45b
CC (PubMed:17586488). {ECO:0000250|UniProtKB:P08238,
CC ECO:0000269|PubMed:17586488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Dynein
CC axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}.
CC -!- TISSUE SPECIFICITY: Detected throughout the embryo and in low levels in
CC the musculature. Expressed predominantly in the developing brain, tail
CC bud and cells surrounding the posterior margin of the yolk tube.
CC {ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:8652412}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development.
CC {ECO:0000269|PubMed:7980538}.
CC -!- INDUCTION: By heat shock during early embryogenesis.
CC {ECO:0000269|PubMed:7980538}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AF068771; AAC21566.1; -; mRNA.
DR EMBL; AF042108; AAB96969.1; -; mRNA.
DR EMBL; BC065359; AAH65359.1; -; mRNA.
DR EMBL; L35587; AAA97519.1; -; mRNA.
DR RefSeq; NP_571385.2; NM_131310.3.
DR AlphaFoldDB; O57521; -.
DR SMR; O57521; -.
DR BioGRID; 78741; 1.
DR IntAct; O57521; 1.
DR MINT; O57521; -.
DR STRING; 7955.ENSDARP00000014978; -.
DR PaxDb; O57521; -.
DR PRIDE; O57521; -.
DR Ensembl; ENSDART00000020084; ENSDARP00000014978; ENSDARG00000029150.
DR Ensembl; ENSDART00000169321; ENSDARP00000137112; ENSDARG00000029150.
DR GeneID; 30573; -.
DR KEGG; dre:30573; -.
DR CTD; 3326; -.
DR ZFIN; ZDB-GENE-990415-95; hsp90ab1.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; O57521; -.
DR OMA; TRMKAEQ; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; O57521; -.
DR TreeFam; TF300686; -.
DR Reactome; R-DRE-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-DRE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DRE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DRE-3371511; HSF1 activation.
DR Reactome; R-DRE-3371568; Attenuation phase.
DR Reactome; R-DRE-3371571; HSF1-dependent transactivation.
DR Reactome; R-DRE-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-844456; The NLRP3 inflammasome.
DR Reactome; R-DRE-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-DRE-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-DRE-8939211; ESR-mediated signaling.
DR Reactome; R-DRE-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DRE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O57521; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000029150; Expressed in cleaving embryo and 56 other tissues.
DR ExpressionAtlas; O57521; baseline and differential.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IMP:ZFIN.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISS:AgBase.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Myogenesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..725
FT /note="Heat shock protein HSP 90-beta"
FT /id="PRO_0000062925"
FT REGION 220..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 721..725
FT /note="TPR repeat-binding"
FT COMPBIAS 239..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 98
FT /note="I -> M (in Ref. 5; AAA97519)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..418
FT /note="EL -> DV (in Ref. 1; AAC21566)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> C (in Ref. 3; AAB96969)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="K -> R (in Ref. 1; AAC21566)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> Y (in Ref. 1; AAC21566)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="K -> N (in Ref. 3; AAB96969)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="D -> T (in Ref. 3; AAB96969)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="S -> T (in Ref. 3; AAB96969)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="Missing (in Ref. 1; AAC21566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 83357 MW; 97FACE5422684DF9 CRC64;
MPEEMRQEEE AETFAFQAEI AQLMSLIINT FYSNKEIFLR ELVSNASDAL DKIRYESLTD
PTKLDSGKDL KIDIIPNVQE RTLTLIDTGI GMTKADLINN LGTIAKSGTK AFMEALQAGA
DISMIGQFGV GFYSAYLVAE KVTVITKHND DEQYAWESSA GGSFTVKVDH GEPIGRGTKV
ILHLKEDQTE YIEEKRVKEV VKKHSQFIGY PITLYVEKER DKEISDDEAE EEKAEKEEKE
EEGEDKPKIE DVGSDDEEDT KDKDKKKKKK IKEKYIDQEE LNKTKPIWTR NPDDISNEEY
GEFYKSLTND WEDHLAVKHF SVEGQLEFRA LLFIPRRAPF DLFENKKKKN NIKLYVRRVF
IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNIVKK CLELFAELAE
DKDNYKKFYD AFSKNLKLGI HEDSQNRKKL SELLRYQSSQ SGDEMTSLTE YVSRMKENQK
SIYYITGESK DQVAHSAFVE RVCKRGFEVL YMTEPIDEYC VQQLKDFDGK SLVSVTKEGL
ELPEDEDEKK KMEEDKAKFE NLCKLMKEIL DKKVEKVTVS NRLVSSPCCI VTSTYGWTAN
MERIMKAQAL RDNSTMGYMM AKKHLEINPD HPIMETLRQK AEADKNDKAV KDLVILLFET
ALLSSGFSLD DPQTHSNRIY RMIKLGLGID EDEDVPVEEP SSAAAPEDIP PLEGDDDASR
MEEVD
