H90A1_DANRE
ID H90A1_DANRE Reviewed; 725 AA.
AC Q90474; Q5RG13; Q6DI33;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Heat shock protein HSP 90-alpha 1;
GN Name=hsp90a.1; Synonyms=hsp90, hsp90a, hsp90aa1; ORFNames=zgc:86652;
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.
RC TISSUE=Embryo;
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, AND INTERACTION WITH UNC45B.
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], INTERACTION WITH MYOSIN, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo;
RX PubMed=18347070; DOI=10.1083/jcb.200709128;
RA Etard C., Roostalu U., Strahle U.;
RT "Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z
RT line of the myofibril.";
RL J. Cell Biol. 180:1163-1175(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-135, INDUCTION, AND DEVELOPMENTAL STAGE.
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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
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).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10707908;
RA Sass J.B., Martin C.C., Krone P.H.;
RT "Restricted expression of the zebrafish hsp90alpha gene in slow and fast
RT muscle fiber lineages.";
RL Int. J. Dev. Biol. 43:835-838(1999).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-94.
RX PubMed=18256191; DOI=10.1242/dev.018150;
RA Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
RA Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
RA Strahle U., Wilson S.W.;
RT "The ATPase-dependent chaperoning activity of Hsp90a regulates thick
RT filament formation and integration during skeletal muscle
RT myofibrillogenesis.";
RL Development 135:1147-1156(2008).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 721-MET--ASP-725.
RX PubMed=18182494; DOI=10.1073/pnas.0707330105;
RA Du S.J., Li H., Bian Y., Zhong Y.;
RT "Heat-shock protein 90alpha1 is required for organized myofibril assembly
RT in skeletal muscles of zebrafish embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:554-559(2008).
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 that is linked to its ATPase activity which is
CC essential for its chaperone activity. This cycle probably induces
CC conformational changes in the client proteins, thereby causing their
CC 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). Plays a key role
CC in slow and fast muscle development in the embryo. Plays a role in
CC myosin expression and assembly (PubMed:10364427, PubMed:17586488,
CC PubMed:18182494, PubMed:18256191). {ECO:0000250|UniProtKB:P07900,
CC ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488,
CC ECO:0000269|PubMed:18182494, ECO:0000269|PubMed:18256191}.
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:P07900}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with unc45b and myosin.
CC {ECO:0000250|UniProtKB:P07900, ECO:0000269|PubMed:17586488,
CC ECO:0000269|PubMed:18347070}.
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250|UniProtKB:P07900}.
CC Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070}.
CC Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070}.
CC Note=Expressed at the Z line and in the perinuclear region of
CC myofibrils. Shuttles between the Z line and A band in response to
CC stress conditions and fibril damage.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the early embryos within the
CC somitic slow muscle progenitors, the adaxial cells that lie on either
CC side of the notochord but not the notochord. Also expressed during the
CC early differentiation of fast fibers. Detected in developing cardiac
CC muscles and pectoral fin primordia. Not detected in mature muscle
CC fibers. {ECO:0000269|PubMed:10707908, ECO:0000269|PubMed:18182494,
CC ECO:0000269|PubMed:8652412}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable during embryogenesis at control
CC temperatures. Distributed throughout the cytoplasm of early developing
CC myocytes at 24 hours post fertilization (hpf).
CC {ECO:0000269|PubMed:10707908, ECO:0000269|PubMed:7980538}.
CC -!- INDUCTION: Up-regulated by heat shock in embryos and larvae with
CC highest levels of expression in 3 day old larvae.
CC {ECO:0000269|PubMed:7980538, ECO:0000269|PubMed:8652412}.
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; AF068773; AAC21567.1; -; mRNA.
DR EMBL; CR381646; CAI21043.1; -; Genomic_DNA.
DR EMBL; BC075757; AAH75757.1; -; mRNA.
DR EMBL; L35586; AAA97518.1; -; mRNA.
DR PIR; JC2343; JC2343.
DR RefSeq; NP_571403.1; NM_131328.1.
DR AlphaFoldDB; Q90474; -.
DR SMR; Q90474; -.
DR ELM; Q90474; -.
DR STRING; 7955.ENSDARP00000022302; -.
DR PaxDb; Q90474; -.
DR Ensembl; ENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478.
DR Ensembl; ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478.
DR GeneID; 30591; -.
DR KEGG; dre:30591; -.
DR CTD; 30591; -.
DR ZFIN; ZDB-GENE-990415-94; hsp90aa1.1.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q90474; -.
DR OMA; CILVTGE; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q90474; -.
DR TreeFam; TF300686; -.
DR PRO; PR:Q90474; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000010478; Expressed in somite and 34 other tissues.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0030018; C:Z disc; IDA:ZFIN.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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:0030239; P:myofibril assembly; IMP:ZFIN.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; 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:0010038; P:response to metal ion; IDA:ZFIN.
DR GO; GO:0048769; P:sarcomerogenesis; IMP:ZFIN.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:ZFIN.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:ZFIN.
DR GO; GO:0014866; P:skeletal myofibril assembly; IMP:ZFIN.
DR GO; GO:0071688; P:striated muscle myosin thick filament assembly; IMP:ZFIN.
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 Reference proteome; Stress response.
FT CHAIN 1..725
FT /note="Heat shock protein HSP 90-alpha 1"
FT /id="PRO_0000062924"
FT REGION 228..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..725
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT REGION 697..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 716..725
FT /note="TPR repeat-binding"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT COMPBIAS 239..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..725
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 94
FT /note="G->D: In slou45; absence of thick filaments leading
FT to loss of filamentous organization of myofibrils."
FT /evidence="ECO:0000269|PubMed:18256191"
FT MUTAGEN 721..725
FT /note="Missing: Reduced binding to unc45b."
FT /evidence="ECO:0000269|PubMed:18182494"
FT CONFLICT 4..11
FT /note="KSAQPVME -> AHEQQMMED (in Ref. 1; AAC21567)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="L -> F (in Ref. 5; AAH75757)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="E -> D (in Ref. 5; AAH75757)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="Q -> R (in Ref. 5; AAH75757)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="D -> E (in Ref. 1; AAC21567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 83319 MW; 78CB3B97976531A7 CRC64;
MPEKSAQPVM EEEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNSS DALDKIRYES
LTDPSKLDSC KDLKIELIPD QKERTLTIID TGIGMTKADL INNLGTIAKS GTKAFMEALQ
AGADISMIGQ FGVGFYSAYL VAEKVTVITK HNDDEQYIWE SAAGGSFTVK PDFGESIGRG
TKVILHLKED QSEYVEEKRI KEVVKKHSQF IGYPITLYIE KQREKEVDLE EGEKQEEEEV
AAGEDKDKPK IEDLGADEDE DSKDGKNKRK KKVKEKYIDA QELNKTKPIW TRNPDDITNE
EYGEFYKSLS NDWEDHLAVK HFSVEGQLEF RALLFVPRRA AFDLFENKKK RNNIKLYVRR
VFIMDNCEEL IPEYLNFIKG VVDSEDLPLN ISREMLQQSK ILKVIRKNLV KKCLDLFTEL
AEDKDNYKKY YEQFSKNIKL GIHEDSQNRK KLSDLLRYYT SASGDEMVSL KDYVSRMKDT
QKHIYYITGE TKDQVANSAF VERLRKAGLE VIYMIEPIDE YCVQQLKEYD GKNLVSVTKE
GLELPEDEEE KKKQDELKAK YENLCKIMKD ILDKKIEKVT VSNRLVSSPC CIVTSTYGWT
ANMERIMKSQ ALRDNSTMGY MTAKKHLEIN PAHPIVETLR EKAEADKNDK AVKDLVILLF
ETALLSSGFT LDDPQTHANR IYRMIKLGLG IDDDDSVVEE ISQPAEEDMP VLEGDDDTSR
MEEVD
