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Database: UniProt
Entry: A0A3P8NQ95_ASTCA
LinkDB: A0A3P8NQ95_ASTCA
Original site: A0A3P8NQ95_ASTCA 
ID   A0A3P8NQ95_ASTCA        Unreviewed;       796 AA.
AC   A0A3P8NQ95;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Endoplasmin {ECO:0000256|ARBA:ARBA00039709};
DE   AltName: Full=Heat shock protein 90 kDa beta member 1 {ECO:0000256|ARBA:ARBA00042650};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000006955.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000006955.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000006955.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}. Sarcoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004564}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   AlphaFoldDB; A0A3P8NQ95; -.
DR   STRING; 8154.ENSACLP00000006955; -.
DR   Ensembl; ENSACLT00000007110.1; ENSACLP00000006955.1; ENSACLG00000004667.1.
DR   GeneTree; ENSGT01020000230401; -.
DR   OMA; KVSKTTW; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000265100; Chromosome 7.
DR   Bgee; ENSACLG00000004667; Expressed in ovary and 8 other cell types or tissues.
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:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0035889; P:otolith tethering; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; 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:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 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   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..796
FT                   /note="Endoplasmin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018187919"
FT   DOMAIN          96..255
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          291..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..318
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..796
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   796 AA;  91571 MW;  C897D39F0733E0D3 CRC64;
     MKRVWVIGLL FALLAFAAVK ADDEFDVDGT VEEDLGKSRD GSRTDDEVVQ REEEAIQLDG
     LNAAQIKELR EKSEKHAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLLSL
     TNEDAMATNE ELTIKIKSDK EKNMLHITDT GIGMTKEELV KNLGTIAKSG TSEFLNKMTE
     MQEEEQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNQF SVIEDPRGDT
     LGRGTTITLV LKEEASDYLE LETIKNLVKK YSQFINFPIY VWASKTETVE EPIDEDAEAA
     EEPEKEASED EAEVEEEEED KDKPKTKKVE KTVWDWELMN DIKPIWQRPA KEVEEDEYKA
     FYKTFSKDND DPMAHIHFTA EGEVTFKSIL FVPTSAPRGL FDEYGSKKND YIKLFVRRVF
     ITDDFNDMMP KYLNFIKGVV DSDDLPLNVS RETLQQHKLL KVIRKKLVRK TLDMIKKIAE
     EQYNDKFWKE FGTNIKLGVI EDHSNRTRLA KLLRFQTSNS ETDLASLEQY VERMKEKQDK
     IYFMAGTSRK EAESSPFVEK LLKKGYEVIY LTEPVDEYCI QALPEFDGKR FQNVAKEGVK
     FDESEKTKEK REALEKEFEP LTTWLKDKAL KDKIEKAVLS QRLTNSPCAL VASQYGWSGN
     MERIMKAQAY QTGKDISTNY YASQKKTLEL NPKHPLVKQL LNRVNTDAED QTASDLAVVL
     FETATLRSGY QLADTKAYGD RIERMLRLSL NVPLDEQIEE EPEEEPEGPA EDDSEDKEET
     VDEDDDEETT KDKDEL
//
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