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Heat shock protein HSP 90-alpha 1

 H90A1_DANRE             Reviewed;         725 AA.
Q90474; Q5RG13; Q6DI33;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
05-DEC-2018, entry version 145.
RecName: Full=Heat shock protein HSP 90-alpha 1;
Name=hsp90a.1; Synonyms=hsp90, hsp90a, hsp90aa1; ORFNames=zgc:86652;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Embryo;
PubMed=10364427; DOI=10.1006/dbio.1999.9262;
Lele Z., Hartson S.D., Martin C.C., Whitesell L., Matts R.L.,
Krone P.H.;
"Disruption of zebrafish somite development by pharmacologic
inhibition of Hsp90.";
Dev. Biol. 210:56-70(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH UNC45B.
PubMed=17586488; DOI=10.1016/j.ydbio.2007.05.014;
Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., Strahle U.;
"The UCS factor Steif/Unc-45b interacts with the heat shock protein
Hsp90a during myofibrillogenesis.";
Dev. Biol. 308:133-143(2007).
[3]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MYOSIN, AND SUBCELLULAR
LOCATION.
TISSUE=Embryo;
PubMed=18347070; DOI=10.1083/jcb.200709128;
Etard C., Roostalu U., Strahle U.;
"Shuttling of the chaperones Unc45b and Hsp90a between the A band and
the Z line of the myofibril.";
J. Cell Biol. 180:1163-1175(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-135, INDUCTION, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=7980538; DOI=10.1006/bbrc.1994.2522;
Krone P.H., Sass J.B.;
"HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and
are differentially regulated in developing embryos.";
Biochem. Biophys. Res. Commun. 204:746-752(1994).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=8652412; DOI=10.1016/0925-4773(95)00476-9;
Sass J.B., Weinberg E.S., Krone P.H.;
"Specific localization of zebrafish hsp90 alpha mRNA to myoD-
expressing cells suggests a role for hsp90 alpha during normal muscle
development.";
Mech. Dev. 54:195-204(1996).
[8]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10707908;
Sass J.B., Martin C.C., Krone P.H.;
"Restricted expression of the zebrafish hsp90alpha gene in slow and
fast muscle fiber lineages.";
Int. J. Dev. Biol. 43:835-838(1999).
[9]
FUNCTION, AND MUTAGENESIS OF GLY-94.
PubMed=18256191; DOI=10.1242/dev.018150;
Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
Strahle U., Wilson S.W.;
"The ATPase-dependent chaperoning activity of Hsp90a regulates thick
filament formation and integration during skeletal muscle
myofibrillogenesis.";
Development 135:1147-1156(2008).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 721-MET--ASP-725.
PubMed=18182494; DOI=10.1073/pnas.0707330105;
Du S.J., Li H., Bian Y., Zhong Y.;
"Heat-shock protein 90alpha1 is required for organized myofibril
assembly in skeletal muscles of zebrafish embryos.";
Proc. Natl. Acad. Sci. U.S.A. 105:554-559(2008).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved for instance in cell cycle control and signal
transduction. Undergoes a functional cycle that is linked to its
ATPase activity which is essential for its chaperone activity.
This cycle probably induces conformational changes in the client
proteins, thereby causing their activation. Interacts dynamically
with various co-chaperones that modulate its substrate
recognition, ATPase cycle and chaperone function. Engages with a
range of client protein classes via its interaction with various
co-chaperone proteins or complexes, that act as adapters,
simultaneously able to interact with the specific client and the
central chaperone itself. Recruitment of ATP and co-chaperone
followed by client protein forms a functional chaperone. After the
completion of the chaperoning process, properly folded client
protein and co-chaperone leave HSP90 in an ADP-bound partially
open conformation and finally, ADP is released from HSP90 which
acquires an open conformation for the next cycle (By similarity).
Plays a key role in slow and fast muscle development in the
embryo. Plays a role in myosin expression and assembly
(PubMed:10364427, PubMed:17586488, PubMed:18182494,
PubMed:18256191). {ECO:0000250|UniProtKB:P07900,
ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488,
ECO:0000269|PubMed:18182494, ECO:0000269|PubMed:18256191}.
-!- ACTIVITY REGULATION: In the resting state, through the
dimerization of its C-terminal domain, HSP90 forms a homodimer
which is defined as the open conformation. Upon ATP-binding, the
N-terminal domain undergoes significant conformational changes and
comes in contact to form an active closed conformation. After
HSP90 finishes its chaperoning tasks of assisting the proper
folding, stabilization and activation of client proteins under the
active state, ATP molecule is hydrolyzed to ADP which then
dissociates from HSP90 and directs the protein back to the resting
state. {ECO:0000250|UniProtKB:P07900}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with unc45b and
myosin. {ECO:0000250|UniProtKB:P07900,
ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:18347070}.
-!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250|UniProtKB:P07900}.
Cytoplasm, myofibril, sarcomere, Z line
{ECO:0000269|PubMed:18347070}. Cytoplasm, myofibril, sarcomere, A
band {ECO:0000269|PubMed:18347070}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:18347070}. Note=Expressed at the Z line and in
the perinuclear region of myofibrils. Shuttles between the Z line
and A band in response to stress conditions and fibril damage.
-!- TISSUE SPECIFICITY: Strongly expressed in the early embryos within
the somitic slow muscle progenitors, the adaxial cells that lie on
either side of the notochord but not the notochord. Also expressed
during the early differentiation of fast fibers. Detected in
developing cardiac muscles and pectoral fin primordia. Not
detected in mature muscle fibers. {ECO:0000269|PubMed:10707908,
ECO:0000269|PubMed:18182494, ECO:0000269|PubMed:8652412}.
-!- DEVELOPMENTAL STAGE: Barely detectable during embryogenesis at
control temperatures. Distributed throughout the cytoplasm of
early developing myocytes at 24 hours post fertilization (hpf).
{ECO:0000269|PubMed:10707908, ECO:0000269|PubMed:7980538}.
-!- INDUCTION: Up-regulated by heat shock in embryos and larvae with
highest levels of expression in 3 day old larvae.
{ECO:0000269|PubMed:7980538, ECO:0000269|PubMed:8652412}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF068773; AAC21567.1; -; mRNA.
EMBL; CR381646; CAI21043.1; -; Genomic_DNA.
EMBL; BC075757; AAH75757.1; -; mRNA.
EMBL; L35586; AAA97518.1; -; mRNA.
PIR; JC2343; JC2343.
RefSeq; NP_571403.1; NM_131328.1.
UniGene; Dr.75834; -.
ProteinModelPortal; Q90474; -.
SMR; Q90474; -.
ELM; Q90474; -.
STRING; 7955.ENSDARP00000022302; -.
PaxDb; Q90474; -.
PRIDE; Q90474; -.
Ensembl; ENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478.
Ensembl; ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478.
GeneID; 30591; -.
KEGG; dre:30591; -.
CTD; 30591; -.
ZFIN; ZDB-GENE-990415-94; hsp90aa1.1.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00940000153658; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; Q90474; -.
KO; K04079; -.
OMA; ASPCCIV; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; Q90474; -.
TreeFam; TF300686; -.
PRO; PR:Q90474; -.
Proteomes; UP000000437; Chromosome 20.
Bgee; ENSDARG00000010478; Expressed in 40 organ(s), highest expression level in muscle tissue.
GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
GO; GO:0030018; C:Z disc; IDA:ZFIN.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
GO; GO:0050900; P:leukocyte migration; IMP:ZFIN.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0030239; P:myofibril assembly; IMP:ZFIN.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:0009408; P:response to heat; IBA:GO_Central.
GO; GO:0010038; P:response to metal ion; IDA:ZFIN.
GO; GO:0048769; P:sarcomerogenesis; IMP:ZFIN.
GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:ZFIN.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:ZFIN.
GO; GO:0014866; P:skeletal myofibril assembly; IMP:ZFIN.
GO; GO:0071688; P:striated muscle myosin thick filament assembly; IMP:ZFIN.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm; Myogenesis;
Nucleotide-binding; Reference proteome; Stress response.
CHAIN 1 725 Heat shock protein HSP 90-alpha 1.
/FTId=PRO_0000062924.
REGION 675 725 Required for homodimerization.
{ECO:0000250|UniProtKB:P07900}.
MOTIF 716 725 TPR repeat-binding.
{ECO:0000250|UniProtKB:P07900}.
BINDING 48 48 ATP. {ECO:0000250}.
BINDING 90 90 ATP. {ECO:0000250}.
BINDING 109 109 ATP. {ECO:0000250}.
BINDING 135 135 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 393 393 ATP. {ECO:0000250}.
MUTAGEN 94 94 G->D: In slou45; absence of thick
filaments leading to loss of filamentous
organization of myofibrils.
{ECO:0000269|PubMed:18256191}.
MUTAGEN 721 725 Missing: Reduced binding to unc45b.
{ECO:0000269|PubMed:18182494}.
CONFLICT 4 11 KSAQPVME -> AHEQQMMED (in Ref. 1;
AAC21567). {ECO:0000305}.
CONFLICT 217 217 L -> F (in Ref. 5; AAH75757).
{ECO:0000305}.
CONFLICT 300 300 E -> D (in Ref. 5; AAH75757).
{ECO:0000305}.
CONFLICT 447 447 Q -> R (in Ref. 5; AAH75757).
{ECO:0000305}.
CONFLICT 646 646 D -> E (in Ref. 1; AAC21567).
{ECO:0000305}.
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


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