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Database: UniProt
Entry: A8DR93_SHEEP
LinkDB: A8DR93_SHEEP
Original site: A8DR93_SHEEP 
ID   A8DR93_SHEEP            Unreviewed;       733 AA.
AC   A8DR93;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Heat shock protein HSP 90-alpha {ECO:0000256|ARBA:ARBA00039928};
GN   Name=HSPCA {ECO:0000313|EMBL:ABI99473.1};
GN   Synonyms=HSP90AA1 {ECO:0000313|Ensembl:ENSOARP00000004171.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|EMBL:ABI99473.1};
RN   [1] {ECO:0000313|EMBL:ABI99473.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18347938; DOI=10.1007/s12192-007-0004-2;
RA   Marcos-Carcavilla A., Calvo J.H., Gonzalez C., Moazami-Goudarzi K.,
RA   Laurent P., Bertaud M., Hayes H., Beattie A.E., Serrano C., Lyahyai J.,
RA   Martin-Burriel I., Serrano M.;
RT   "Structural and functional analysis of the HSP90AA1 gene: distribution of
RT   polymorphisms among sheep with different responses to scrapie.";
RL   Cell Stress Chaperones 13:19-29(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000004171.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000004171.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [3] {ECO:0000313|Ensembl:ENSOARP00000004171.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000256|ARBA:ARBA00004223}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; AMGL01043307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ983231; ABI99473.1; -; Genomic_DNA.
DR   RefSeq; XP_004018044.1; XM_004017995.3.
DR   STRING; 9940.ENSOARP00000004171; -.
DR   PaxDb; 9940-ENSOARP00000004171; -.
DR   Ensembl; ENSOART00000004244.1; ENSOARP00000004171.1; ENSOARG00000003903.1.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000002356; Chromosome 18.
DR   Bgee; ENSOARG00000003903; Expressed in cerebellum and 53 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0046677; P:response to antibiotic; ISS:AgBase.
DR   GO; GO:0009409; P:response to cold; ISS:AgBase.
DR   GO; GO:0009408; P:response to heat; ISS:AgBase.
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:SF87; HEAT SHOCK PROTEIN HSP 90-ALPHA; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Stress response {ECO:0000313|EMBL:ABI99473.1}.
FT   DOMAIN          40..194
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          225..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  84731 MW;  B8D9EB475B613DBE CRC64;
     MPEETQAQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
     YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
     ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
     GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED
     KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
     NPDDITNEEY GEFYKSLTND WEDHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN
     NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK
     CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD
     YCTRMKENQK HIYYITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK
     TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
     VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV
     KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTADDSS AAVTEEMPPL
     EGDDDTSRME EVD
//
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