ID   HS904_HUMAN             Reviewed;         418 AA.
AC   Q58FG1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Putative heat shock protein HSP 90-alpha A4;
DE   AltName: Full=Heat shock 90 kDa protein 1 alpha-like 2;
DE   AltName: Full=Heat shock protein 90-alpha D;
DE            Short=Heat shock protein 90Ad;
GN   Name=HSP90AA4P; Synonyms=HSP90AD, HSPCAL2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16269234; DOI=10.1016/j.ygeno.2005.08.012;
RA   Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.;
RT   "The HSP90 family of genes in the human genome: insights into their
RT   divergence and evolution.";
RL   Genomics 86:627-637(2005).
CC   -!- FUNCTION: Putative molecular chaperone that may promote the maturation,
CC       structural maintenance and proper regulation of specific target
CC       proteins. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AY956760; AAX38247.1; -; mRNA.
DR   AlphaFoldDB; Q58FG1; -.
DR   SMR; Q58FG1; -.
DR   IntAct; Q58FG1; 38.
DR   BindingDB; Q58FG1; -.
DR   iPTMnet; Q58FG1; -.
DR   PhosphoSitePlus; Q58FG1; -.
DR   SwissPalm; Q58FG1; -.
DR   BioMuta; HGNC:5255; -.
DR   EPD; Q58FG1; -.
DR   jPOST; Q58FG1; -.
DR   MassIVE; Q58FG1; -.
DR   MaxQB; Q58FG1; -.
DR   PeptideAtlas; Q58FG1; -.
DR   PRIDE; Q58FG1; -.
DR   ProteomicsDB; 62625; -.
DR   GeneCards; HSP90AA4P; -.
DR   HGNC; HGNC:5255; HSP90AA4P.
DR   neXtProt; NX_Q58FG1; -.
DR   InParanoid; Q58FG1; -.
DR   PhylomeDB; Q58FG1; -.
DR   PathwayCommons; Q58FG1; -.
DR   SignaLink; Q58FG1; -.
DR   Pharos; Q58FG1; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q58FG1; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0005524; F:ATP binding; IBA:GO_Central.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
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; 3.
DR   Pfam; PF00183; HSP90; 2.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   5: Uncertain;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..418
FT                   /note="Putative heat shock protein HSP 90-alpha A4"
FT                   /id="PRO_0000341969"
FT   REGION          255..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  47712 MW;  71D8B90EC37A3FB4 CRC64;
     MESLTDPSKL DSGKEPHISL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI TKSETKVFME
     VLQAGADISM IGQFSVGFYS AYSVAEKVTV ITKHNNDEQY AWESSLRGSF TEYREFYKSL
     TINWEDYLAV KHFSVEGQLE FRAFLFVPRL APFELLETRK KKNKIKLSAR RDLIMDNCEE
     LIPEYLNFIR GVVDSEDLPL NIFRETKDQV ANSTIVQRLW KHGLEVIYTI EPIDEYCVQQ
     LKEFEGKTLV SVTKEDLELP EDEEEKKKQE EGKQKTKQKK NQSLRTSAKS TYGWTANMER
     IMKAQALRDN STTGYMAAKK HLEINPDHSF IDTLRQKAET DKNDKSVKDL VILLYETALL
     SSDFGLEGPQ THANRIYRMN KLGLGTDEDD PTADDTSAAV TEEMPPLEGD DDTSRMEK