ENPL_DICDI
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 03-AUG-2022, entry version 123.
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 (Slime mold).
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.DDB0215015; -.
DR PaxDb; Q9NKX1; -.
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: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 Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 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
