ID   ENPL_DICDI              Reviewed;         768 AA.
AC   Q9NKX1; Q54VP2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Endoplasmin homolog;
DE   AltName: Full=92 kDa phosphoprotein;
DE   AltName: Full=Glucose-regulated protein 94 homolog;
DE            Short=GRP-94 homolog;
DE   Flags: Precursor;
GN   Name=grp94; ORFNames=DDB_G0280057;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=10913338; DOI=10.1006/bbrc.2000.3096;
RA   Morita T., Saitoh K., Takagi T., Maeda Y.;
RT   "Involvement of the glucose-regulated protein 94 (Dd-GRP94) in starvation
RT   response of Dictyostelium discoideum cells.";
RL   Biochem. Biophys. Res. Commun. 274:323-331(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15652353; DOI=10.1016/j.yexcr.2004.10.005;
RA   Yamaguchi H., Morita T., Amagai A., Maeda Y.;
RT   "Changes in spatial and temporal localization of Dictyostelium homologues
RT   of TRAP1 and GRP94 revealed by immunoelectron microscopy.";
RL   Exp. Cell Res. 303:415-424(2005).
CC   -!- FUNCTION: May play a role in late differentiation as well as in
CC       starvation response. When overexpressed, suppresses the ability to form
CC       normal fruiting bodies and impairs prespore differentiation as well as
CC       maturation into spores.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus. Note=In
CC       prespore cells, preferentially localizes in Golgi vesicles and
CC       cisternae. Colocalizes with trap1 in the prespore-specific vacuole.
CC   -!- INDUCTION: Expression is greatly reduced following starvation.
CC   -!- PTM: Phosphorylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AB040814; BAA94290.2; -; mRNA.
DR   EMBL; AAFI02000035; EAL67255.1; -; Genomic_DNA.
DR   PIR; JC7352; JC7352.
DR   RefSeq; XP_641313.1; XM_636221.1.
DR   AlphaFoldDB; Q9NKX1; -.
DR   SMR; Q9NKX1; -.
DR   STRING; 44689.Q9NKX1; -.
DR   GlyCosmos; Q9NKX1; 3 sites, No reported glycans.
DR   PaxDb; 44689-DDB0215015; -.
DR   EnsemblProtists; EAL67255; EAL67255; DDB_G0280057.
DR   GeneID; 8622445; -.
DR   KEGG; ddi:DDB_G0280057; -.
DR   dictyBase; DDB_G0280057; grp94.
DR   eggNOG; KOG0020; Eukaryota.
DR   InParanoid; Q9NKX1; -.
DR   PhylomeDB; Q9NKX1; -.
DR   Reactome; R-DDI-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   PRO; PR:Q9NKX1; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005798; C:Golgi-associated vesicle; IDA:dictyBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; 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; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..768
FT                   /note="Endoplasmin homolog"
FT                   /id="PRO_0000327690"
FT   REGION          266..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           765..768
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        282..298
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   SITE            426
FT                   /note="Important for ATP hydrolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        309
FT                   /note="T -> I (in Ref. 1; BAA94290)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444..445
FT                   /note="LV -> G (in Ref. 2; EAL67255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   768 AA;  87269 MW;  7EB40FDDC56059E0 CRC64;
     MKSITKIFLI LGLFAFLLVA FAPSSSVATV NLESDGYTEA EAKLIEEKGE KFTFQTEVNK
     LMNIIINSLY SKKEIFLREL ISNASDALDK IRFLALTNAD LLGEGEQSNL DIHIKIDKAN
     NVLHITDRGV GMTKDELVRN LGTIAQSGTK EFIKKVSDSA ESSNLIGQFG VGFYSLFLVA
     DSVVVTSKSN DDDQYVWTSD SQSSYTIAKD PKGNTLGRGT RISLHIKDDS KEFLDQEVIK
     QLVKKYSQFI NFPIYLYVSE EVEIPKEEQE DSKPITDDQV EETTTTTEEG EEETTTEEEG
     QTEEKKTKTV YKWEELNDSK PLWMKAAKDV TKEEYTEFFR SLSKTQDTPI TYSHFKTEGD
     TEFRSILYIP ENPPSNMFDL EAAGSGLKLF VRRVFITDNL KELVPNWLRF LVGVIDSDDL
     PLNVSREMLQ QNKILDAIKK KVILVKFISM IKELSEDEDK TKYNEFFKKF GSSMKLGAIE
     DQANKKRLTK YLLFPSSKEE LTTFAGYVER MKEGQDQIYF ITGKSKDSVE ASPLIEQAIK
     KGYEVLFLVD PIDEYLVPQL DKFDDKYKFT NLARSGVKFN EDKEEEDQRK QTAEEFKPLL
     SYLKKTLSDK LEKVVISKVL ADSPSILVSN SWGVTANQER IMKAQAHQAN AQPQFNSKKI
     MEINPSHPLI KKLLNRLNEF GEEDETTKVS AHVLYETSAL TAGYSIDNPT NFADFIYKLM
     MINGDSLAQT NFETTKNENS GPSVSFGDDD ENQQQDFQQP PQSTHDEL
//