HS90B_CHICK
ID HS90B_CHICK Reviewed; 725 AA.
AC Q04619;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Heat shock cognate protein HSP 90-beta;
GN Name=HSP90AB1; Synonyms=HSPCB;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=7916597; DOI=10.1006/bbrc.1993.1095;
RA Meng X., Jerome V., Devin J., Baulieu E.-E., Catelli M.-G.;
RT "Cloning of chicken hsp90 beta: the only vertebrate hsp90 insensitive to
RT heat shock.";
RL Biochem. Biophys. Res. Commun. 190:630-636(1993).
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. {ECO:0000250|UniProtKB:P08238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}.
CC Melanosome {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q6AZV1}.
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.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70101; CAA49704.1; -; mRNA.
DR PIR; JC1468; JC1468.
DR RefSeq; NP_996842.1; NM_206959.1.
DR AlphaFoldDB; Q04619; -.
DR SMR; Q04619; -.
DR BioGRID; 676448; 6.
DR STRING; 9031.ENSGALP00000016523; -.
DR PaxDb; Q04619; -.
DR PRIDE; Q04619; -.
DR ABCD; Q04619; 1 sequenced antibody.
DR GeneID; 396188; -.
DR KEGG; gga:396188; -.
DR CTD; 3326; -.
DR VEuPathDB; HostDB:geneid_396188; -.
DR eggNOG; KOG0019; Eukaryota.
DR InParanoid; Q04619; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q04619; -.
DR PRO; PR:Q04619; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
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..725
FT /note="Heat shock cognate protein HSP 90-beta"
FT /id="PRO_0000062923"
FT REGION 220..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 721..725
FT /note="TPR repeat-binding"
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 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 725 AA; 83427 MW; C0BF463D3219422F CRC64;
MPEQVQHGED EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
DPSKLDTGKD LKIDIVPNPR DPTLTLLDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRTD HGEPIGRGTK
VILYLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYVEKE REKEVSDDEA EEEKVEKEEE
ESKDEEKPKI EDVGSDEEEE EGEKSKKKKT KKIKEKYIDQ EELNKTKPIW TRNPDDITQE
EYGEFYKSLT NDWEDHLAVK HFSVEGQLEF RALLFIPRRA PFDLFENKKK KNNIKLYVRR
VFIMDSCDEL IPEYLNFIRG VVDSEDLPLN ISREMLQQSK ILKVIRKNIV KKCLELFTEL
AEDKENYKKF YEAFSKNLKL GIHEDSTNRK RLSELLRYHT SQSGDEMTSL SEYVSRMKES
QKSIYYITGE SKEQVANSAF VERVRKRGFE VVYMTEPIDE YCVQQLKEFD GKTLVSVTKE
GLELPEDEEE KKNMEESKAK FETLCKLMKE ILDKKVEKVT ISNRLVSSPC CIVTSTYGWT
ANMERIMKAQ ALRDNSTMGY MMAKKHLEIN PDHPIVETLR QKADANKNDK AVKDLVVLLF
ETALLSSGFS LEDPQTHSNR IYRMIKLGLG IDEDEVIAEE SSIAPPDEIP PLEGDEDTSR
MEEVD
