ID G3PHE5_GASAC Unreviewed; 723 AA.
AC G3PHE5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 {ECO:0000313|Ensembl:ENSGACP00000017020.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000017020.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000017020.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000017020.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR AlphaFoldDB; G3PHE5; -.
DR STRING; 69293.ENSGACP00000017020; -.
DR Ensembl; ENSGACT00000017054.1; ENSGACP00000017020.1; ENSGACG00000012875.1.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR InParanoid; G3PHE5; -.
DR OMA; MSTEMET; -.
DR TreeFam; TF300686; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000012875; Expressed in heart and 4 other cell types or tissues.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
DR GO; GO:0048769; P:sarcomerogenesis; IEA:Ensembl.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IEA:Ensembl.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IEA:Ensembl.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF122; HEAT SHOCK PROTEIN HSP 90-ALPHA 1; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 35..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 224..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 83102 MW; DA444BE1BCDD23B7 CRC64;
MPAAGNVMEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNSSDA LDKIRYESLT
DPSRLETCKD LKIEIKPDLH ARTLTLIDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA ERVTVITKHN DDEQYIWESA AGGSFTVKTD PGESIGRGTR
VILHLKEDQT EYCEEKRVKE VVKKHSQFIG YPITLYVEKT REKEVDLEEG EKEEEVEKDA
AENKDKPKIE DVGSDEDEDT KEGKNKRKKK VKEKYIDAQE LNKTKPIWTR NPDDITNEEY
GEFYKSLTND WEDHLAVKHF SVEGQLEFRA LLFVPRRASF DLFENKKKKN NIKLYVRRVF
IMDNCDELIP EYLNFIKGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK CLDLFTELAE
DKDNYKKYYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSN SGDETVSLKD YVSRMKDNQK
HIYYITGETK DQVANSAFVE RLRKAGLEVI YMIEPIDEYC VQQLKEYDGK NLVSVTKEGL
ELPEDEENLK KQEELKNKFE NICKIMKDIL DKKIEKVTVS NRLVSSPCCI VTSTYGWTAN
MERIMKSQAL RDNSTMGYMT AKKHLEINPL HPIVETLRVK AEADKNDKAV KDLVILLFET
ALLSSGFTLE DPQTHANRIY RMIKLGLGID DDDSAVDDLI HPAEEDMPVL EGDDDTSRME
EVD
//
