HS90A_CHICK
ID HS90A_CHICK Reviewed; 728 AA.
AC P11501;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Heat shock protein HSP 90-alpha;
GN Name=HSP90AA1; Synonyms=HSPCA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Gizzard, and Stomach;
RX PubMed=2923621; DOI=10.1016/0006-291x(89)92415-7;
RA Binart N., Chambraud B., Dumas B., Rowlands D.A., Bigogne C., Levin J.M.,
RA Garnier J., Baulieu E.-E., Catelli M.-G.;
RT "The cDNA-derived amino acid sequence of chick heat shock protein Mr 90,000
RT (HSP 90) reveals a 'DNA like' structure: potential site of interaction with
RT steroid receptors.";
RL Biochem. Biophys. Res. Commun. 159:140-147(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
RX PubMed=2762125; DOI=10.1093/nar/17.13.5259;
RA Vourc'H C., Binart N., Chambraud B., David J.P., Jerome V., Baulieu E.-E.,
RA Catelli M.-G.;
RT "Isolation and functional analysis of chicken 90-kDa heat shock protein
RT gene promoter.";
RL Nucleic Acids Res. 17:5259-5272(1989).
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. {ECO:0000250|UniProtKB:P07900}.
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. {ECO:0000250|UniProtKB:P07900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07901}.
CC Melanosome {ECO:0000250|UniProtKB:P07900}.
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; X07265; CAA30251.1; -; Genomic_DNA.
DR EMBL; X15028; CAA33132.1; -; Genomic_DNA.
DR PIR; A32298; HHCH90.
DR RefSeq; NP_001103255.1; NM_001109785.1.
DR AlphaFoldDB; P11501; -.
DR BMRB; P11501; -.
DR SMR; P11501; -.
DR BioGRID; 683988; 6.
DR IntAct; P11501; 1.
DR PaxDb; P11501; -.
DR PRIDE; P11501; -.
DR GeneID; 423463; -.
DR KEGG; gga:423463; -.
DR CTD; 3320; -.
DR VEuPathDB; HostDB:geneid_423463; -.
DR InParanoid; P11501; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P11501; -.
DR PRO; PR:P11501; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IDA:AgBase.
DR GO; GO:0009986; C:cell surface; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
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; IDA:AgBase.
DR GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IMP:AgBase.
DR GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IPI:AgBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IMP:AgBase.
DR GO; GO:0042802; F:identical protein binding; IMP:AgBase.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:AgBase.
DR GO; GO:0033142; F:nuclear progesterone receptor binding; IPI:AgBase.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:AgBase.
DR GO; GO:0008022; F:protein C-terminus binding; IMP:AgBase.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0046790; F:virion binding; IDA:AgBase.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:AgBase.
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; IMP:AgBase.
DR GO; GO:0046677; P:response to antibiotic; IDA:AgBase.
DR GO; GO:0009409; P:response to cold; IDA:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:AgBase.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA: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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..728
FT /note="Heat shock protein HSP 90-alpha"
FT /id="PRO_0000062922"
FT REGION 226..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..728
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT REGION 698..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 719..728
FT /note="TPR repeat-binding"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 728 AA; 84059 MW; 6EC5660F4D5006CE CRC64;
MPEAVQTQDQ PMEEEVETFA FQAEIAQLMS LIINTFYSNK EIFLRELISN SSDALDKIRY
ESLTDPSKLD SGKDLKINLI PNKHDRTLTI VDTGIGMTKA DLVNNLGTIA KSGTKAFMEA
LQAGADISMI GQFGVGSYSA YLVAEKVTVI TKHNDDEQYA WESSAGGSFT VRLDNGEPLG
RGTKVILHLK EDQTEYLEER RIKEIVKKHS QFIGYPIRLF VEKERDKEVS DDEAEEKEEE
KEEKEEKTED KPEIEDVGSD EEEEKKDGDK KKKKKIKEKY IDEEELNKTK PIWTRNPDDI
TNEEYGEFYK SLTNDWEDHL AVKHFSVEGQ LEFRALLFVP RRAPFDLFEN RKKKNNIKLY
VRRVFIMDNC EELIPEYLNF MRGVVDSEDL PLNISREMLQ QSKILKVIRK NLVKKCLELF
TELAEDKENY KKFYEQFSKN IKLGIHEDSQ NRKKLSELLR YYTSASGDEM VSLKDYCTRM
KENQKHVYYI TGETKDQVAN SAFVERLRKH GLEVIYMIEP IDEYCVQQLK EFEGKTLVSV
TKEGLELPED EEEKKKQEEK KAKFENLCKI MKDILEKKVE KVVVSNRLVT SPCCIVTSTY
GWTANMERIM KAQALRDNST MGYMAAKKHL EINPDHSIIE TLRQKAEADK NDKSVKDLVI
LLYETALLSS GFSLEDPQTH ANRIYRMIKL GLGIDEDDTA AEEASPAVTE EMPPLEGDDD
TSRMEEVD
